diff options
| author | Navan Chauhan <navanchauhan@gmail.com> | 2020-09-11 16:18:38 +0530 |
|---|---|---|
| committer | Navan Chauhan <navanchauhan@gmail.com> | 2020-09-11 16:18:38 +0530 |
| commit | 9dadfdb3332b073aaff508d126e90200ad09868d (patch) | |
| tree | 1578ff007b42b2175691f3dab11566611ec44907 /plip/test/pdb/2pvb.pdb | |
| parent | 004f4513c8cd5cfffbf69484fb39a3d7bc98bd49 (diff) | |
removed downloaded plip
Diffstat (limited to 'plip/test/pdb/2pvb.pdb')
| -rw-r--r-- | plip/test/pdb/2pvb.pdb | 2605 |
1 files changed, 0 insertions, 2605 deletions
diff --git a/plip/test/pdb/2pvb.pdb b/plip/test/pdb/2pvb.pdb deleted file mode 100644 index e9489af..0000000 --- a/plip/test/pdb/2pvb.pdb +++ /dev/null @@ -1,2605 +0,0 @@ -HEADER METAL BINDING PROTEIN 02-OCT-98 2PVB -TITLE PIKE PARVALBUMIN (PI 4.10) AT LOW TEMPERATURE (100K) AND -TITLE 2 ATOMIC RESOLUTION (0.91 A). -COMPND MOL_ID: 1; -COMPND 2 MOLECULE: PROTEIN (PARVALBUMIN); -COMPND 3 CHAIN: A; -COMPND 4 OTHER_DETAILS: (PIKE PI 4.10) -SOURCE MOL_ID: 1; -SOURCE 2 ORGANISM_SCIENTIFIC: ESOX LUCIUS; -SOURCE 3 ORGANISM_COMMON: NORTHERN PIKE; -SOURCE 4 ORGANISM_TAXID: 8010; -SOURCE 5 TISSUE: MUSCLE -KEYWDS CALCIUM BINDING PROTEIN, METAL BINDING PROTEIN -EXPDTA X-RAY DIFFRACTION -AUTHOR J.P.DECLERCQ,C.EVRARD -REVDAT 4 24-FEB-09 2PVB 1 VERSN -REVDAT 3 05-MAY-00 2PVB 1 JRNL -REVDAT 2 22-DEC-99 2PVB 4 HEADER COMPND REMARK JRNL -REVDAT 2 2 4 ATOM SOURCE SEQRES -REVDAT 1 07-OCT-98 2PVB 0 -JRNL AUTH J.P.DECLERCQ,C.EVRARD,V.LAMZIN,J.PARELLO -JRNL TITL CRYSTAL STRUCTURE OF THE EF-HAND PARVALBUMIN AT -JRNL TITL 2 ATOMIC RESOLUTION (0.91 A) AND AT LOW TEMPERATURE -JRNL TITL 3 (100 K). EVIDENCE FOR CONFORMATIONAL MULTISTATES -JRNL TITL 4 WITHIN THE HYDROPHOBIC CORE. -JRNL REF PROTEIN SCI. V. 8 2194 1999 -JRNL REFN ISSN 0961-8368 -JRNL PMID 10548066 -REMARK 1 -REMARK 1 REFERENCE 1 -REMARK 1 AUTH J.P.DECLERCQ,C.EVRARD,D.C.CARTER,B.S.WRIGHT, -REMARK 1 AUTH 2 G.ETIENNE,J.PARELLO -REMARK 1 TITL A CRYSTAL OF A TYPICAL EF-HAND PROTEIN GROWN UNDER -REMARK 1 TITL 2 MICROGRAVITY DIFFRACTS X- RAYS BEYOND 0.9 A -REMARK 1 TITL 3 RESOLUTION -REMARK 1 REF J.CRYST.GROWTH V. 196 595 1999 -REMARK 1 REFN ISSN 0022-0248 -REMARK 1 REFERENCE 2 -REMARK 1 AUTH J.P.DECLERCQ,B.TINANT,J.PARELLO -REMARK 1 TITL X-RAY STRUCTURE OF A NEW CRYSTAL FORM OF PIKE 4.10 -REMARK 1 TITL 2 BETA PARVALBUMIN -REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 52 165 1996 -REMARK 1 REFN ISSN 0907-4449 -REMARK 1 REFERENCE 3 -REMARK 1 AUTH J.P.DECLERCQ,B.TINANT,J.PARELLO,J.RAMBAUD -REMARK 1 TITL IONIC INTERACTIONS WITH PARVALBUMINS. CRYSTAL -REMARK 1 TITL 2 STRUCTURE DETERMINATION OF PIKE 4.10 PARVALBUMIN -REMARK 1 TITL 3 IN FOUR DIFFERENT IONIC ENVIRONMENTS -REMARK 1 REF J.MOL.BIOL. V. 220 1017 1991 -REMARK 1 REFN ISSN 0022-2836 -REMARK 1 REFERENCE 4 -REMARK 1 AUTH J.P.DECLERCQ,B.TINANT,J.PARELLO,G.ETIENNE,R.HUBER -REMARK 1 TITL CRYSTAL STRUCTURE DETERMINATION AND REFINEMENT OF -REMARK 1 TITL 2 PIKE 4.10 PARVALBUMIN (MINOR COMPONENT FROM ESOX -REMARK 1 TITL 3 LUCIUS) -REMARK 1 REF J.MOL.BIOL. V. 202 349 1988 -REMARK 1 REFN ISSN 0022-2836 -REMARK 2 -REMARK 2 RESOLUTION. 0.91 ANGSTROMS. -REMARK 3 -REMARK 3 REFINEMENT. -REMARK 3 PROGRAM : SHELXL-97 -REMARK 3 AUTHORS : G.M.SHELDRICK -REMARK 3 -REMARK 3 DATA USED IN REFINEMENT. -REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.91 -REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00 -REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 -REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 -REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT -REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM, 5% -REMARK 3 -REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF). -REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.110 -REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.110 -REMARK 3 FREE R VALUE (NO CUTOFF) : 0.132 -REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000 -REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 3187 -REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 63698 -REMARK 3 -REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). -REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.109 -REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.109 -REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.131 -REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000 -REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 3103 -REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 62168 -REMARK 3 -REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. -REMARK 3 PROTEIN ATOMS : 873 -REMARK 3 NUCLEIC ACID ATOMS : 0 -REMARK 3 HETEROGEN ATOMS : 6 -REMARK 3 SOLVENT ATOMS : 217 -REMARK 3 -REMARK 3 MODEL REFINEMENT. -REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 1025.00 -REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 784.00 -REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 16 -REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 9883 -REMARK 3 NUMBER OF RESTRAINTS : 12405 -REMARK 3 -REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. -REMARK 3 BOND LENGTHS (A) : 0.015 -REMARK 3 ANGLE DISTANCES (A) : 0.032 -REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL -REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.335 -REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.093 -REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.102 -REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.061 -REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.007 -REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.037 -REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.100 -REMARK 3 -REMARK 3 BULK SOLVENT MODELING. -REMARK 3 METHOD USED: MOEWS & KRETSINGER -REMARK 3 -REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER -REMARK 3 SPECIAL CASE: NULL -REMARK 3 -REMARK 3 OTHER REFINEMENT REMARKS: NULL -REMARK 4 -REMARK 4 2PVB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 -REMARK 100 -REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-SEP-99. -REMARK 100 THE RCSB ID CODE IS RCSB008041. -REMARK 200 -REMARK 200 EXPERIMENTAL DETAILS -REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION -REMARK 200 DATE OF DATA COLLECTION : 01-JUN-97 -REMARK 200 TEMPERATURE (KELVIN) : 100 -REMARK 200 PH : 8.0 -REMARK 200 NUMBER OF CRYSTALS USED : 1 -REMARK 200 -REMARK 200 SYNCHROTRON (Y/N) : Y -REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG -REMARK 200 BEAMLINE : X11 -REMARK 200 X-RAY GENERATOR MODEL : NULL -REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M -REMARK 200 WAVELENGTH OR RANGE (A) : 0.9096 -REMARK 200 MONOCHROMATOR : BENT SINGLE-CRYSTAL GERMANIUM -REMARK 200 TRIANGULAR MONOCHROMATOR -REMARK 200 OPTICS : SEGMENTED MIRROR -REMARK 200 -REMARK 200 DETECTOR TYPE : IMAGE PLATE -REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH -REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO -REMARK 200 DATA SCALING SOFTWARE : SCALEPACK -REMARK 200 -REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63698 -REMARK 200 RESOLUTION RANGE HIGH (A) : 0.910 -REMARK 200 RESOLUTION RANGE LOW (A) : 25.000 -REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL -REMARK 200 -REMARK 200 OVERALL. -REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 -REMARK 200 DATA REDUNDANCY : 4.900 -REMARK 200 R MERGE (I) : NULL -REMARK 200 R SYM (I) : 3.60000 -REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.2000 -REMARK 200 -REMARK 200 IN THE HIGHEST RESOLUTION SHELL. -REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.91 -REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 0.92 -REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3 -REMARK 200 DATA REDUNDANCY IN SHELL : 2.80 -REMARK 200 R MERGE FOR SHELL (I) : NULL -REMARK 200 R SYM FOR SHELL (I) : 12.40000 -REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300 -REMARK 200 -REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH -REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER -REMARK 200 SOFTWARE USED: NULL -REMARK 200 STARTING MODEL: PDB ENTRY 1PVB -REMARK 200 -REMARK 200 REMARK: STRUCTURE PREVIOUSLY SOLVED AT 1.75 A -REMARK 280 -REMARK 280 CRYSTAL -REMARK 280 SOLVENT CONTENT, VS (%): 36.20 -REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93 -REMARK 280 -REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROP, MICROGRAVITY -REMARK 280 CONDITIONS PROTEIN SOLUTION : 27 MG/ML, 0.02% (W/V) NAN3 -REMARK 280 RESERVOIR : 2.4M AMMONIUM SULFATE 0.03%(W/V) EDTA, 0.02% (W/V) -REMARK 280 NAN3 TRIS BUFFER (PH 8.0) DROP : 10 MICROL. PROTEIN SOLUTION + -REMARK 280 10 MICROL. RESERVOIR, VAPOR DIFFUSION - SITTING DROP IN -REMARK 280 MICROGRAVITY -REMARK 290 -REMARK 290 CRYSTALLOGRAPHIC SYMMETRY -REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 -REMARK 290 -REMARK 290 SYMOP SYMMETRY -REMARK 290 NNNMMM OPERATOR -REMARK 290 1555 X,Y,Z -REMARK 290 2555 -X+1/2,-Y,Z+1/2 -REMARK 290 3555 -X,Y+1/2,-Z+1/2 -REMARK 290 4555 X+1/2,-Y+1/2,-Z -REMARK 290 -REMARK 290 WHERE NNN -> OPERATOR NUMBER -REMARK 290 MMM -> TRANSLATION VECTOR -REMARK 290 -REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS -REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM -REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY -REMARK 290 RELATED MOLECULES. -REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 -REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 -REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 -REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 25.51500 -REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 -REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 17.28500 -REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 -REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.90500 -REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 17.28500 -REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.51500 -REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 24.90500 -REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 -REMARK 290 -REMARK 290 REMARK: NULL -REMARK 300 -REMARK 300 BIOMOLECULE: 1 -REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM -REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN -REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON -REMARK 300 BURIED SURFACE AREA. -REMARK 350 -REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN -REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE -REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS -REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND -REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. -REMARK 350 -REMARK 350 BIOMOLECULE: 1 -REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC -REMARK 350 APPLY THE FOLLOWING TO CHAINS: A -REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 -REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 -REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 -REMARK 500 -REMARK 500 GEOMETRY AND STEREOCHEMISTRY -REMARK 500 SUBTOPIC: COVALENT BOND ANGLES -REMARK 500 -REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES -REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE -REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN -REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). -REMARK 500 -REMARK 500 STANDARD TABLE: -REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) -REMARK 500 -REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 -REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 -REMARK 500 -REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 -REMARK 500 VAL A 33 CB - CA - C ANGL. DEV. = -14.2 DEGREES -REMARK 500 ASP A 100 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES -REMARK 500 MET A 105 N - CA - CB ANGL. DEV. = 10.8 DEGREES -REMARK 500 -REMARK 500 REMARK: NULL -REMARK 600 -REMARK 600 HETEROGEN -REMARK 600 ACETYL IS COVALENTLY ATTACHED TO THE -REMARK 600 N-TERMINAL SERINE BY AN AMIDE LINKAGE -REMARK 620 -REMARK 620 METAL COORDINATION -REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; -REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): -REMARK 620 -REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL -REMARK 620 CA A 110 CA -REMARK 620 N RES CSSEQI ATOM -REMARK 620 1 ASP A 51 OD1 -REMARK 620 2 ASP A 53 OD1 82.6 -REMARK 620 3 SER A 55 OG 87.8 78.2 -REMARK 620 4 PHE A 57 O 82.9 150.3 75.3 -REMARK 620 5 GLU A 59 OE1 168.8 103.5 84.3 87.3 -REMARK 620 6 GLU A 62 OE1 103.6 128.4 151.7 80.4 80.1 -REMARK 620 7 GLU A 62 OE2 100.2 75.4 151.2 132.9 90.5 52.9 -REMARK 620 N 1 2 3 4 5 6 -REMARK 620 -REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL -REMARK 620 CA A 111 CA -REMARK 620 N RES CSSEQI ATOM -REMARK 620 1 ASP A 90 OD1 -REMARK 620 2 ASP A 92 OD1 84.8 -REMARK 620 3 ASP A 94 OD1 86.0 82.5 -REMARK 620 4 MET A 96 O 83.7 158.6 78.8 -REMARK 620 5 GLU A 101 OE1 116.3 117.9 149.8 83.5 -REMARK 620 6 GLU A 101 OE2 86.9 74.2 156.1 123.0 51.8 -REMARK 620 7 HOH A 201 O 161.9 97.1 76.5 88.5 78.8 111.0 -REMARK 620 N 1 2 3 4 5 6 -REMARK 800 -REMARK 800 SITE -REMARK 800 SITE_IDENTIFIER: CD -REMARK 800 EVIDENCE_CODE: AUTHOR -REMARK 800 SITE_DESCRIPTION: CATION BINDING SITE OCCUPIED BY CA2+ CA 110 A -REMARK 800 SITE_IDENTIFIER: EF -REMARK 800 EVIDENCE_CODE: AUTHOR -REMARK 800 SITE_DESCRIPTION: CATION BINDING SITE OCCUPIED BY CA2+ CA 111 A -REMARK 800 SITE_IDENTIFIER: AC1 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 110 -REMARK 800 SITE_IDENTIFIER: AC2 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 111 -REMARK 800 SITE_IDENTIFIER: AC3 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 A 200 -REMARK 800 SITE_IDENTIFIER: AC4 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 150 -REMARK 800 SITE_IDENTIFIER: AC5 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 151 -DBREF 2PVB A 1 107 UNP P02619 PRVB_ESOLU 1 107 -SEQRES 1 A 108 ACE SER PHE ALA GLY LEU LYS ASP ALA ASP VAL ALA ALA -SEQRES 2 A 108 ALA LEU ALA ALA CYS SER ALA ALA ASP SER PHE LYS HIS -SEQRES 3 A 108 LYS GLU PHE PHE ALA LYS VAL GLY LEU ALA SER LYS SER -SEQRES 4 A 108 LEU ASP ASP VAL LYS LYS ALA PHE TYR VAL ILE ASP GLN -SEQRES 5 A 108 ASP LYS SER GLY PHE ILE GLU GLU ASP GLU LEU LYS LEU -SEQRES 6 A 108 PHE LEU GLN ASN PHE SER PRO SER ALA ARG ALA LEU THR -SEQRES 7 A 108 ASP ALA GLU THR LYS ALA PHE LEU ALA ASP GLY ASP LYS -SEQRES 8 A 108 ASP GLY ASP GLY MET ILE GLY VAL ASP GLU PHE ALA ALA -SEQRES 9 A 108 MET ILE LYS ALA -HET ACE A 0 3 -HET CA A 110 1 -HET CA A 111 1 -HET NH4 A 200 1 -HET FMT A 150 3 -HET FMT A 151 3 -HETNAM ACE ACETYL GROUP -HETNAM CA CALCIUM ION -HETNAM NH4 AMMONIUM ION -HETNAM FMT FORMIC ACID -FORMUL 1 ACE C2 H4 O -FORMUL 2 CA 2(CA 2+) -FORMUL 4 NH4 H4 N 1+ -FORMUL 5 FMT 2(C H2 O2) -FORMUL 7 HOH *211(H2 O) -HELIX 1 1 ASP A 8 CYS A 18 1 11 -HELIX 2 2 HIS A 26 VAL A 33 1 8 -HELIX 3 3 LEU A 35 SER A 37 5 3 -HELIX 4 4 LEU A 40 ILE A 50 1 11 -HELIX 5 5 GLU A 60 LYS A 64 1 5 -HELIX 6 6 PHE A 66 ASN A 69 5 4 -HELIX 7 7 ASP A 79 GLY A 89 1 11 -HELIX 8 8 VAL A 99 ILE A 106 1 8 -LINK OD1 ASP A 51 CA CA A 110 1555 1555 2.27 -LINK OD1 ASP A 53 CA CA A 110 1555 1555 2.30 -LINK OG SER A 55 CA CA A 110 1555 1555 2.51 -LINK O PHE A 57 CA CA A 110 1555 1555 2.32 -LINK OE1 GLU A 59 CA CA A 110 1555 1555 2.33 -LINK OE1 GLU A 62 CA CA A 110 1555 1555 2.44 -LINK OE2 GLU A 62 CA CA A 110 1555 1555 2.51 -LINK OD1 ASP A 90 CA CA A 111 1555 1555 2.31 -LINK OD1 ASP A 92 CA CA A 111 1555 1555 2.35 -LINK OD1 ASP A 94 CA CA A 111 1555 1555 2.36 -LINK O MET A 96 CA CA A 111 1555 1555 2.37 -LINK OE1 GLU A 101 CA CA A 111 1555 1555 2.43 -LINK OE2 GLU A 101 CA CA A 111 1555 1555 2.54 -LINK CA CA A 111 O HOH A 201 1555 1555 2.37 -LINK C ACE A 0 N SER A 1 1555 1555 1.33 -SITE 1 CD 6 ASP A 51 ASP A 53 SER A 55 PHE A 57 -SITE 2 CD 6 GLU A 59 GLU A 62 -SITE 1 EF 6 ASP A 90 ASP A 92 ASP A 94 MET A 96 -SITE 2 EF 6 HOH A 201 GLU A 101 -SITE 1 AC1 6 ASP A 51 ASP A 53 SER A 55 PHE A 57 -SITE 2 AC1 6 GLU A 59 GLU A 62 -SITE 1 AC2 6 ASP A 90 ASP A 92 ASP A 94 MET A 96 -SITE 2 AC2 6 GLU A 101 HOH A 201 -SITE 1 AC3 6 ASP A 53 GLU A 59 ASP A 61 HOH A 212 -SITE 2 AC3 6 HOH A 293 HOH A 308 -SITE 1 AC4 6 LYS A 107 FMT A 151 HOH A 223 HOH A 226 -SITE 2 AC4 6 HOH A 277 HOH A 353 -SITE 1 AC5 7 THR A 78 ASP A 79 ALA A 80 LYS A 107 -SITE 2 AC5 7 FMT A 150 HOH A 306 HOH A 323 -CRYST1 51.030 49.810 34.570 90.00 90.00 90.00 P 21 21 21 4 -ORIGX1 1.000000 0.000000 0.000000 0.00000 -ORIGX2 0.000000 1.000000 0.000000 0.00000 -ORIGX3 0.000000 0.000000 1.000000 0.00000 -SCALE1 0.019596 0.000000 0.000000 0.00000 -SCALE2 0.000000 0.020076 0.000000 0.00000 -SCALE3 0.000000 0.000000 0.028927 0.00000 -HETATM 1 C ACE A 0 3.753 17.697 16.468 1.00 6.24 C -ANISOU 1 C ACE A 0 963 734 674 -159 -23 47 C -HETATM 2 O ACE A 0 3.169 17.058 17.352 1.00 7.96 O -ANISOU 2 O ACE A 0 1254 1133 640 -467 -26 59 O -HETATM 3 CH3 ACE A 0 3.163 17.765 15.090 1.00 8.20 C -ANISOU 3 CH3 ACE A 0 1510 876 729 -348 -241 152 C -ATOM 4 N SER A 1 4.877 18.359 16.704 1.00 6.66 N -ANISOU 4 N SER A 1 1067 743 720 -217 -87 188 N -ATOM 5 CA ASER A 1 5.448 18.370 18.030 0.46 8.09 C -ANISOU 5 CA ASER A 1 1071 1007 996 -402 -338 324 C -ATOM 6 CA BSER A 1 5.579 18.279 17.960 0.54 7.39 C -ANISOU 6 CA BSER A 1 953 1000 855 -305 -178 157 C -ATOM 7 C SER A 1 6.405 19.560 18.155 1.00 7.49 C -ANISOU 7 C SER A 1 985 1023 839 -300 -118 208 C -ATOM 8 O SER A 1 6.998 20.038 17.208 1.00 10.46 O -ANISOU 8 O SER A 1 1549 1555 870 -863 -268 347 O -ATOM 9 CB ASER A 1 6.225 17.109 18.342 0.46 10.67 C -ANISOU 9 CB ASER A 1 1326 1174 1553 -402 -441 752 C -ATOM 10 CB BSER A 1 6.500 17.057 17.937 0.54 11.64 C -ANISOU 10 CB BSER A 1 1895 976 1553 -15 -734 408 C -ATOM 11 OG ASER A 1 7.464 17.138 17.697 0.46 14.45 O -ANISOU 11 OG ASER A 1 1731 1696 2063 303 148 645 O -ATOM 12 OG BSER A 1 7.078 16.800 19.210 0.54 12.01 O -ANISOU 12 OG BSER A 1 2237 1064 1261 -17 -881 247 O -ATOM 13 N PHE A 2 6.458 20.045 19.377 1.00 6.93 N -ANISOU 13 N PHE A 2 865 844 924 -140 -178 152 N -ATOM 14 CA PHE A 2 7.323 21.172 19.687 1.00 6.96 C -ANISOU 14 CA PHE A 2 710 860 1076 -165 -66 114 C -ATOM 15 C PHE A 2 7.584 21.108 21.189 1.00 7.00 C -ANISOU 15 C PHE A 2 801 860 1000 -45 -96 102 C -ATOM 16 O PHE A 2 6.651 21.017 21.981 1.00 7.13 O -ANISOU 16 O PHE A 2 807 977 924 -36 -62 -161 O -ATOM 17 CB PHE A 2 6.627 22.488 19.323 1.00 7.51 C -ANISOU 17 CB PHE A 2 806 961 1088 -128 -140 233 C -ATOM 18 CG PHE A 2 7.511 23.700 19.330 1.00 6.69 C -ANISOU 18 CG PHE A 2 773 850 920 -75 -66 100 C -ATOM 19 CD1 PHE A 2 7.731 24.401 20.482 1.00 8.50 C -ANISOU 19 CD1 PHE A 2 1233 1127 870 -255 12 79 C -ATOM 20 CD2 PHE A 2 8.074 24.175 18.171 1.00 6.75 C -ANISOU 20 CD2 PHE A 2 928 812 823 -7 27 7 C -ATOM 21 CE1 PHE A 2 8.508 25.556 20.476 1.00 8.94 C -ANISOU 21 CE1 PHE A 2 1540 1040 815 -324 30 -109 C -ATOM 22 CE2 PHE A 2 8.856 25.316 18.156 1.00 7.63 C -ANISOU 22 CE2 PHE A 2 1024 968 909 -110 91 76 C -ATOM 23 CZ PHE A 2 9.057 26.019 19.315 1.00 8.66 C -ANISOU 23 CZ PHE A 2 1275 907 1109 -260 194 -78 C -ATOM 24 N ALA A 3 8.853 21.016 21.564 1.00 9.04 N -ANISOU 24 N ALA A 3 808 1355 1272 -33 -162 197 N -ATOM 25 CA ALA A 3 9.159 20.776 22.973 1.00 8.94 C -ANISOU 25 CA ALA A 3 870 1262 1265 64 -191 83 C -ATOM 26 C ALA A 3 8.445 21.762 23.869 1.00 9.21 C -ANISOU 26 C ALA A 3 1206 1137 1158 -8 -597 -60 C -ATOM 27 O ALA A 3 8.354 22.963 23.660 1.00 10.42 O -ANISOU 27 O ALA A 3 1400 1139 1419 -38 -501 -199 O -ATOM 28 CB ALA A 3 10.672 20.869 23.156 1.00 12.56 C -ANISOU 28 CB ALA A 3 1155 2250 1368 68 -395 259 C -ATOM 29 N GLY A 4 7.866 21.283 24.962 1.00 9.48 N -ANISOU 29 N GLY A 4 1128 1405 1069 303 -394 -17 N -ATOM 30 CA GLY A 4 7.151 22.063 25.901 1.00 9.59 C -ANISOU 30 CA GLY A 4 1287 1137 1220 373 -651 -64 C -ATOM 31 C GLY A 4 5.633 22.165 25.670 1.00 7.79 C -ANISOU 31 C GLY A 4 1253 845 861 241 -389 -7 C -ATOM 32 O GLY A 4 4.876 22.506 26.580 1.00 8.87 O -ANISOU 32 O GLY A 4 1309 1225 834 306 -359 -219 O -ATOM 33 N LEU A 6 5.204 21.859 24.449 1.00 7.05 N -ANISOU 33 N LEU A 6 1101 814 761 237 -376 -126 N -ATOM 34 CA LEU A 6 3.808 21.906 24.058 1.00 6.47 C -ANISOU 34 CA LEU A 6 1027 783 647 226 -179 -86 C -ATOM 35 C LEU A 6 3.301 20.505 23.930 1.00 6.36 C -ANISOU 35 C LEU A 6 965 808 645 177 -111 -7 C -ATOM 36 O LEU A 6 4.070 19.533 23.765 1.00 7.42 O -ANISOU 36 O LEU A 6 1054 790 974 229 -99 13 O -ATOM 37 CB LEU A 6 3.647 22.661 22.709 1.00 5.79 C -ANISOU 37 CB LEU A 6 832 713 653 127 -219 -67 C -ATOM 38 CG LEU A 6 4.234 24.076 22.716 1.00 6.77 C -ANISOU 38 CG LEU A 6 1068 667 839 131 -227 -93 C -ATOM 39 CD1 LEU A 6 4.050 24.736 21.363 1.00 7.11 C -ANISOU 39 CD1 LEU A 6 963 782 957 150 -180 33 C -ATOM 40 CD2 LEU A 6 3.604 24.952 23.804 1.00 7.91 C -ANISOU 40 CD2 LEU A 6 1310 746 950 158 -178 -128 C -ATOM 41 N LYS A 7 1.980 20.360 23.980 1.00 6.80 N -ANISOU 41 N LYS A 7 1043 852 691 173 -99 -43 N -ATOM 42 CA LYS A 7 1.357 19.030 23.804 1.00 6.82 C -ANISOU 42 CA LYS A 7 1118 821 653 58 72 152 C -ATOM 43 C LYS A 7 1.238 18.704 22.329 1.00 5.99 C -ANISOU 43 C LYS A 7 860 659 754 -67 -10 82 C -ATOM 44 O LYS A 7 0.736 19.508 21.537 1.00 6.37 O -ANISOU 44 O LYS A 7 1047 692 680 -92 -105 96 O -ATOM 45 CB LYS A 7 -0.003 19.111 24.459 1.00 9.00 C -ANISOU 45 CB LYS A 7 1189 1331 899 205 141 132 C -ATOM 46 CG LYS A 7 -0.708 17.838 24.547 1.00 11.73 C -ANISOU 46 CG LYS A 7 1258 1405 1792 14 140 -130 C -ATOM 47 CD LYS A 7 -1.908 18.019 25.507 1.00 25.13 C -ANISOU 47 CD LYS A 7 1333 3988 4225 347 1221 1436 C -ATOM 48 CE LYS A 7 -2.950 16.930 25.153 1.00 25.31 C -ANISOU 48 CE LYS A 7 1355 5163 3099 -78 385 1840 C -ATOM 49 NZ LYS A 7 -4.160 17.514 25.846 1.00 28.34 N -ANISOU 49 NZ LYS A 7 1560 6050 3159 -282 717 1506 N -ATOM 50 N ASP A 8 1.666 17.496 21.951 1.00 6.48 N -ANISOU 50 N ASP A 8 1087 683 694 -95 -19 111 N -ATOM 51 CA ASP A 8 1.608 17.088 20.572 1.00 6.24 C -ANISOU 51 CA ASP A 8 1002 661 709 -117 -6 69 C -ATOM 52 C ASP A 8 0.204 17.261 19.965 1.00 6.28 C -ANISOU 52 C ASP A 8 1071 589 726 -119 -32 54 C -ATOM 53 O ASP A 8 0.040 17.711 18.866 1.00 6.70 O -ANISOU 53 O ASP A 8 1081 696 770 -75 -106 126 O -ATOM 54 CB ASP A 8 2.056 15.655 20.373 1.00 7.13 C -ANISOU 54 CB ASP A 8 1132 688 891 -72 -82 27 C -ATOM 55 CG ASP A 8 3.532 15.407 20.614 1.00 8.85 C -ANISOU 55 CG ASP A 8 1040 967 1353 103 -97 -160 C -ATOM 56 OD1 ASP A 8 4.304 16.297 20.933 1.00 9.30 O -ANISOU 56 OD1 ASP A 8 1087 1156 1291 -51 -129 -144 O -ATOM 57 OD2 ASP A 8 3.930 14.248 20.404 1.00 18.32 O -ANISOU 57 OD2 ASP A 8 1228 1037 4695 170 -740 -726 O -ATOM 58 N ALA A 9 -0.846 16.877 20.748 1.00 6.88 N -ANISOU 58 N ALA A 9 1086 745 785 -164 -42 180 N -ATOM 59 CA ALA A 9 -2.166 16.932 20.185 1.00 7.78 C -ANISOU 59 CA ALA A 9 1010 842 1103 -212 15 158 C -ATOM 60 C ALA A 9 -2.551 18.390 19.874 1.00 7.07 C -ANISOU 60 C ALA A 9 926 811 950 -198 56 202 C -ATOM 61 O ALA A 9 -3.329 18.655 18.934 1.00 7.96 O -ANISOU 61 O ALA A 9 1053 834 1135 -196 -65 179 O -ATOM 62 CB ALA A 9 -3.195 16.352 21.115 1.00 10.73 C -ANISOU 62 CB ALA A 9 1117 1027 1932 -305 48 594 C -ATOM 63 N ASP A 10 -2.107 19.338 20.693 1.00 6.58 N -ANISOU 63 N ASP A 10 870 758 873 -111 3 153 N -ATOM 64 CA ASP A 10 -2.413 20.756 20.440 1.00 6.59 C -ANISOU 64 CA ASP A 10 975 811 719 -77 63 161 C -ATOM 65 C ASP A 10 -1.681 21.227 19.174 1.00 5.73 C -ANISOU 65 C ASP A 10 852 696 632 -125 -10 4 C -ATOM 66 O ASP A 10 -2.228 21.999 18.369 1.00 6.13 O -ANISOU 66 O ASP A 10 913 765 651 15 -29 99 O -ATOM 67 CB ASP A 10 -2.020 21.641 21.615 1.00 7.01 C -ANISOU 67 CB ASP A 10 1106 874 683 105 155 77 C -ATOM 68 CG ASP A 10 -2.842 21.430 22.877 1.00 8.41 C -ANISOU 68 CG ASP A 10 1156 1229 811 246 203 205 C -ATOM 69 OD1 ASP A 10 -3.982 20.984 22.793 1.00 12.60 O -ANISOU 69 OD1 ASP A 10 1029 2681 1078 27 249 253 O -ATOM 70 OD2 ASP A 10 -2.314 21.782 23.941 1.00 9.54 O -ANISOU 70 OD2 ASP A 10 1547 1374 704 223 227 119 O -ATOM 71 N VAL A 11 -0.424 20.824 19.029 1.00 5.52 N -ANISOU 71 N VAL A 11 835 663 601 -138 -18 -33 N -ATOM 72 CA VAL A 11 0.327 21.195 17.840 1.00 5.47 C -ANISOU 72 CA VAL A 11 857 651 571 -162 -56 11 C -ATOM 73 C VAL A 11 -0.357 20.634 16.582 1.00 5.19 C -ANISOU 73 C VAL A 11 688 673 609 -113 -41 8 C -ATOM 74 O VAL A 11 -0.547 21.331 15.585 1.00 5.39 O -ANISOU 74 O VAL A 11 861 639 546 -63 -65 18 O -ATOM 75 CB VAL A 11 1.801 20.743 17.938 1.00 5.64 C -ANISOU 75 CB VAL A 11 859 708 575 -204 -71 73 C -ATOM 76 CG1 VAL A 11 2.536 21.077 16.653 1.00 6.16 C -ANISOU 76 CG1 VAL A 11 914 790 635 -62 17 10 C -ATOM 77 CG2 VAL A 11 2.449 21.442 19.165 1.00 7.18 C -ANISOU 77 CG2 VAL A 11 958 1126 644 -322 -123 9 C -ATOM 78 N ALA A 12 -0.710 19.338 16.660 1.00 5.72 N -ANISOU 78 N ALA A 12 936 607 630 -170 -117 -2 N -ATOM 79 CA ALA A 12 -1.346 18.721 15.505 1.00 6.27 C -ANISOU 79 CA ALA A 12 1008 633 742 -87 -228 -44 C -ATOM 80 C ALA A 12 -2.685 19.388 15.177 1.00 6.35 C -ANISOU 80 C ALA A 12 969 627 818 -192 -234 50 C -ATOM 81 O ALA A 12 -3.038 19.569 13.992 1.00 7.30 O -ANISOU 81 O ALA A 12 1124 756 894 -218 -371 26 O -ATOM 82 CB ALA A 12 -1.546 17.240 15.808 1.00 8.71 C -ANISOU 82 CB ALA A 12 1458 582 1271 -215 -423 -66 C -ATOM 83 N ALA A 13 -3.445 19.776 16.213 1.00 6.95 N -ANISOU 83 N ALA A 13 838 900 904 -128 -115 138 N -ATOM 84 CA ALA A 13 -4.722 20.457 15.968 1.00 7.47 C -ANISOU 84 CA ALA A 13 850 1019 968 -205 -152 317 C -ATOM 85 C ALA A 13 -4.491 21.828 15.360 1.00 7.07 C -ANISOU 85 C ALA A 13 785 933 967 -42 4 204 C -ATOM 86 O ALA A 13 -5.262 22.245 14.495 1.00 7.79 O -ANISOU 86 O ALA A 13 882 1063 1014 -23 -211 137 O -ATOM 87 CB ALA A 13 -5.507 20.532 17.258 1.00 9.57 C -ANISOU 87 CB ALA A 13 942 1174 1520 -42 226 399 C -ATOM 88 N ALA A 14 -3.497 22.565 15.818 1.00 6.42 N -ANISOU 88 N ALA A 14 828 821 790 17 -5 59 N -ATOM 89 CA ALA A 14 -3.219 23.859 15.283 1.00 6.38 C -ANISOU 89 CA ALA A 14 871 709 845 90 59 76 C -ATOM 90 C ALA A 14 -2.826 23.786 13.813 1.00 5.96 C -ANISOU 90 C ALA A 14 827 620 817 97 61 41 C -ATOM 91 O ALA A 14 -3.216 24.630 13.008 1.00 6.87 O -ANISOU 91 O ALA A 14 966 769 875 200 47 108 O -ATOM 92 CB ALA A 14 -2.141 24.560 16.081 1.00 6.45 C -ANISOU 92 CB ALA A 14 950 674 828 45 24 -11 C -ATOM 93 N LEU A 15 -2.019 22.757 13.476 1.00 5.51 N -ANISOU 93 N LEU A 15 794 638 660 16 -79 -3 N -ATOM 94 CA LEU A 15 -1.640 22.566 12.085 1.00 5.48 C -ANISOU 94 CA LEU A 15 848 593 640 -7 -28 -64 C -ATOM 95 C LEU A 15 -2.852 22.208 11.240 1.00 5.95 C -ANISOU 95 C LEU A 15 859 587 817 -19 -84 -22 C -ATOM 96 O LEU A 15 -2.996 22.669 10.094 1.00 6.68 O -ANISOU 96 O LEU A 15 896 899 743 16 -130 87 O -ATOM 97 CB LEU A 15 -0.551 21.490 11.986 1.00 5.47 C -ANISOU 97 CB LEU A 15 851 550 679 -30 -85 -36 C -ATOM 98 CG LEU A 15 0.815 21.920 12.513 1.00 5.23 C -ANISOU 98 CG LEU A 15 757 577 653 15 -17 -46 C -ATOM 99 CD1 LEU A 15 1.713 20.701 12.667 1.00 6.48 C -ANISOU 99 CD1 LEU A 15 913 646 904 94 -76 -20 C -ATOM 100 CD2 LEU A 15 1.442 22.968 11.607 1.00 6.54 C -ANISOU 100 CD2 LEU A 15 804 701 979 -41 -66 153 C -ATOM 101 N ALA A 16 -3.741 21.356 11.734 1.00 6.65 N -ANISOU 101 N ALA A 16 947 694 887 -120 -268 85 N -ATOM 102 CA ALA A 16 -4.951 21.037 10.980 1.00 7.00 C -ANISOU 102 CA ALA A 16 1064 754 841 -126 -339 -44 C -ATOM 103 C ALA A 16 -5.813 22.306 10.770 1.00 6.80 C -ANISOU 103 C ALA A 16 882 785 915 -187 -265 77 C -ATOM 104 O ALA A 16 -6.416 22.460 9.715 1.00 7.34 O -ANISOU 104 O ALA A 16 956 893 941 -160 -285 104 O -ATOM 105 CB ALA A 16 -5.700 19.928 11.650 1.00 8.96 C -ANISOU 105 CB ALA A 16 1124 975 1305 -389 -494 265 C -ATOM 106 N ALA A 17 -5.859 23.180 11.764 1.00 6.96 N -ANISOU 106 N ALA A 17 859 846 940 -84 -172 39 N -ATOM 107 CA ALA A 17 -6.726 24.348 11.684 1.00 7.26 C -ANISOU 107 CA ALA A 17 764 956 1038 -29 -53 -42 C -ATOM 108 C ALA A 17 -6.274 25.341 10.626 1.00 7.03 C -ANISOU 108 C ALA A 17 814 831 1028 47 -196 -17 C -ATOM 109 O ALA A 17 -7.081 26.154 10.152 1.00 8.92 O -ANISOU 109 O ALA A 17 849 1121 1418 93 -138 258 O -ATOM 110 CB ALA A 17 -6.759 25.047 13.039 1.00 8.67 C -ANISOU 110 CB ALA A 17 1056 1204 1036 22 -15 -152 C -ATOM 111 N CYS A 18 -5.011 25.281 10.224 1.00 6.50 N -ANISOU 111 N CYS A 18 824 688 958 49 -142 121 N -ATOM 112 CA CYS A 18 -4.503 26.160 9.139 1.00 6.20 C -ANISOU 112 CA CYS A 18 903 646 808 28 -104 85 C -ATOM 113 C CYS A 18 -4.111 25.393 7.907 1.00 5.90 C -ANISOU 113 C CYS A 18 730 602 909 -44 -202 49 C -ATOM 114 O CYS A 18 -3.306 25.878 7.111 1.00 6.37 O -ANISOU 114 O CYS A 18 841 673 906 -48 -55 44 O -ATOM 115 CB CYS A 18 -3.396 27.073 9.644 1.00 6.69 C -ANISOU 115 CB CYS A 18 1149 572 820 -76 -175 88 C -ATOM 116 SG CYS A 18 -1.881 26.275 10.194 1.00 7.04 S -ANISOU 116 SG CYS A 18 914 818 944 -164 -186 71 S -ATOM 117 N SER A 19 -4.723 24.223 7.681 1.00 6.07 N -ANISOU 117 N SER A 19 809 585 913 -38 -100 15 N -ATOM 118 CA SER A 19 -4.374 23.412 6.552 1.00 6.13 C -ANISOU 118 CA SER A 19 784 607 938 -31 -87 32 C -ATOM 119 C SER A 19 -4.628 24.087 5.205 1.00 6.27 C -ANISOU 119 C SER A 19 842 626 912 -18 -88 -92 C -ATOM 120 O SER A 19 -3.851 23.865 4.293 1.00 7.64 O -ANISOU 120 O SER A 19 1172 773 959 82 84 20 O -ATOM 121 CB SER A 19 -5.130 22.067 6.615 1.00 6.54 C -ANISOU 121 CB SER A 19 850 548 1088 -31 -172 -9 C -ATOM 122 OG SER A 19 -6.535 22.247 6.641 1.00 6.57 O -ANISOU 122 OG SER A 19 835 747 915 -102 -36 -82 O -ATOM 123 N ALA A 20 -5.671 24.896 5.083 1.00 6.55 N -ANISOU 123 N ALA A 20 941 709 838 -37 -111 14 N -ATOM 124 CA ALA A 20 -5.968 25.588 3.847 1.00 6.51 C -ANISOU 124 CA ALA A 20 979 743 750 -39 -112 -27 C -ATOM 125 C ALA A 20 -5.067 26.798 3.677 1.00 6.70 C -ANISOU 125 C ALA A 20 952 751 843 20 -186 -36 C -ATOM 126 O ALA A 20 -4.868 27.585 4.589 1.00 6.49 O -ANISOU 126 O ALA A 20 893 739 834 -116 -97 -49 O -ATOM 127 CB ALA A 20 -7.413 26.076 3.802 1.00 7.10 C -ANISOU 127 CB ALA A 20 996 815 887 -109 -264 -35 C -ATOM 128 N ALA A 21 -4.547 26.985 2.456 1.00 8.00 N -ANISOU 128 N ALA A 21 1335 754 949 -223 197 -179 N -ATOM 129 CA ALA A 21 -3.758 28.172 2.158 1.00 8.04 C -ANISOU 129 CA ALA A 21 1199 784 1073 -157 106 -106 C -ATOM 130 C ALA A 21 -4.609 29.406 2.444 1.00 6.50 C -ANISOU 130 C ALA A 21 915 855 702 -106 -112 24 C -ATOM 131 O ALA A 21 -5.804 29.461 2.151 1.00 8.66 O -ANISOU 131 O ALA A 21 1100 1264 927 -121 -202 111 O -ATOM 132 CB ALA A 21 -3.329 28.172 0.697 1.00 12.03 C -ANISOU 132 CB ALA A 21 2371 997 1201 -576 637 -307 C -ATOM 133 N ASP A 22 -3.979 30.407 3.068 1.00 6.50 N -ANISOU 133 N ASP A 22 1029 697 742 -24 -137 58 N -ATOM 134 CA ASP A 22 -4.531 31.687 3.446 1.00 7.42 C -ANISOU 134 CA ASP A 22 1134 783 901 78 -161 60 C -ATOM 135 C ASP A 22 -5.452 31.612 4.652 1.00 7.18 C -ANISOU 135 C ASP A 22 1059 745 924 122 -114 113 C -ATOM 136 O ASP A 22 -5.974 32.646 5.027 1.00 9.99 O -ANISOU 136 O ASP A 22 1596 1033 1167 427 209 134 O -ATOM 137 CB ASP A 22 -5.101 32.467 2.266 1.00 8.80 C -ANISOU 137 CB ASP A 22 1209 1100 1034 183 -181 284 C -ATOM 138 CG ASP A 22 -3.937 32.917 1.392 1.00 10.71 C -ANISOU 138 CG ASP A 22 1387 1575 1107 -129 -290 508 C -ATOM 139 OD1 ASP A 22 -2.951 33.459 1.892 1.00 10.29 O -ANISOU 139 OD1 ASP A 22 1119 1178 1612 107 -161 31 O -ATOM 140 OD2 ASP A 22 -3.996 32.728 0.172 1.00 24.02 O -ANISOU 140 OD2 ASP A 22 2299 5834 994 -1344 -354 588 O -ATOM 141 N SER A 23 -5.511 30.457 5.328 1.00 6.48 N -ANISOU 141 N SER A 23 909 758 794 -30 -156 -1 N -ATOM 142 CA SER A 23 -6.247 30.345 6.587 1.00 6.38 C -ANISOU 142 CA SER A 23 757 783 884 -4 -199 27 C -ATOM 143 C SER A 23 -5.394 30.534 7.829 1.00 6.07 C -ANISOU 143 C SER A 23 892 674 739 -37 -81 -65 C -ATOM 144 O SER A 23 -5.950 30.559 8.932 1.00 7.23 O -ANISOU 144 O SER A 23 894 1082 772 -59 -34 -75 O -ATOM 145 CB SER A 23 -6.948 28.985 6.667 1.00 7.08 C -ANISOU 145 CB SER A 23 881 934 875 -60 -162 90 C -ATOM 146 OG SER A 23 -6.057 27.933 6.970 1.00 7.31 O -ANISOU 146 OG SER A 23 1136 740 900 -48 -120 65 O -ATOM 147 N PHE A 24 -4.076 30.637 7.695 1.00 6.14 N -ANISOU 147 N PHE A 24 727 777 828 95 -33 -78 N -ATOM 148 CA PHE A 24 -3.237 30.799 8.875 1.00 5.84 C -ANISOU 148 CA PHE A 24 762 683 775 55 -49 -12 C -ATOM 149 C PHE A 24 -3.491 32.146 9.474 1.00 5.58 C -ANISOU 149 C PHE A 24 702 664 756 -17 -37 40 C -ATOM 150 O PHE A 24 -3.536 33.172 8.770 1.00 6.81 O -ANISOU 150 O PHE A 24 962 719 907 9 -98 177 O -ATOM 151 CB PHE A 24 -1.783 30.646 8.502 1.00 6.61 C -ANISOU 151 CB PHE A 24 840 924 747 54 11 -145 C -ATOM 152 CG PHE A 24 -0.795 30.904 9.617 1.00 5.70 C -ANISOU 152 CG PHE A 24 702 772 692 132 17 -37 C -ATOM 153 CD1 PHE A 24 -0.527 29.966 10.589 1.00 5.94 C -ANISOU 153 CD1 PHE A 24 748 680 830 14 78 -26 C -ATOM 154 CD2 PHE A 24 -0.109 32.091 9.662 1.00 6.02 C -ANISOU 154 CD2 PHE A 24 786 779 722 67 63 117 C -ATOM 155 CE1 PHE A 24 0.428 30.203 11.560 1.00 5.77 C -ANISOU 155 CE1 PHE A 24 772 772 650 181 14 19 C -ATOM 156 CE2 PHE A 24 0.837 32.343 10.650 1.00 6.20 C -ANISOU 156 CE2 PHE A 24 726 734 895 21 100 5 C -ATOM 157 CZ PHE A 24 1.112 31.389 11.584 1.00 5.96 C -ANISOU 157 CZ PHE A 24 673 852 740 114 -15 -133 C -ATOM 158 N LYS A 25 -3.621 32.176 10.801 1.00 5.57 N -ANISOU 158 N LYS A 25 695 643 778 48 -59 25 N -ATOM 159 CA LYS A 25 -3.748 33.411 11.603 1.00 6.22 C -ANISOU 159 CA LYS A 25 883 636 842 71 -115 -15 C -ATOM 160 C LYS A 25 -2.780 33.210 12.749 1.00 5.98 C -ANISOU 160 C LYS A 25 752 630 890 82 -134 -26 C -ATOM 161 O LYS A 25 -3.054 32.393 13.651 1.00 6.19 O -ANISOU 161 O LYS A 25 830 744 776 3 -57 5 O -ATOM 162 CB LYS A 25 -5.194 33.585 12.054 1.00 8.06 C -ANISOU 162 CB LYS A 25 960 1142 959 349 -107 -206 C -ATOM 163 CG LYS A 25 -6.140 33.787 10.880 1.00 8.28 C -ANISOU 163 CG LYS A 25 866 1234 1046 401 -122 -244 C -ATOM 164 CD LYS A 25 -7.594 33.826 11.319 1.00 11.31 C -ANISOU 164 CD LYS A 25 919 2246 1131 498 26 -308 C -ATOM 165 CE LYS A 25 -8.593 34.114 10.236 1.00 13.25 C -ANISOU 165 CE LYS A 25 1136 2770 1127 556 -118 -363 C -ATOM 166 NZ LYS A 25 -8.548 33.128 9.154 1.00 14.71 N -ANISOU 166 NZ LYS A 25 1222 2891 1477 253 -51 -665 N -ATOM 167 N HIS A 26 -1.632 33.889 12.743 1.00 6.21 N -ANISOU 167 N HIS A 26 832 720 808 14 -30 102 N -ATOM 168 CA HIS A 26 -0.600 33.599 13.734 1.00 5.75 C -ANISOU 168 CA HIS A 26 693 629 865 40 -33 34 C -ATOM 169 C HIS A 26 -1.099 33.688 15.148 1.00 5.57 C -ANISOU 169 C HIS A 26 646 643 828 -3 -26 -87 C -ATOM 170 O HIS A 26 -0.732 32.849 15.965 1.00 5.84 O -ANISOU 170 O HIS A 26 721 684 813 -18 20 -34 O -ATOM 171 CB HIS A 26 0.643 34.443 13.505 1.00 6.66 C -ANISOU 171 CB HIS A 26 767 826 937 -31 13 -15 C -ATOM 172 CG HIS A 26 0.378 35.905 13.375 1.00 10.41 C -ANISOU 172 CG HIS A 26 670 797 2489 -110 223 -50 C -ATOM 173 ND1 HIS A 26 -0.083 36.435 12.220 1.00 16.77 N -ANISOU 173 ND1 HIS A 26 1121 1173 4079 -55 -330 1196 N -ATOM 174 CD2 HIS A 26 0.565 36.872 14.312 1.00 17.31 C -ANISOU 174 CD2 HIS A 26 1783 1051 3745 -440 1587 -1005 C -ATOM 175 CE1 HIS A 26 -0.212 37.736 12.449 1.00 24.01 C -ANISOU 175 CE1 HIS A 26 1577 1131 6415 303 1457 1474 C -ATOM 176 NE2 HIS A 26 0.173 38.006 13.693 1.00 25.02 N -ANISOU 176 NE2 HIS A 26 2309 789 6408 -154 2696 -264 N -ATOM 177 N LYS A 27 -1.935 34.678 15.488 1.00 6.25 N -ANISOU 177 N LYS A 27 790 610 975 83 -1 -108 N -ATOM 178 CA LYS A 27 -2.373 34.783 16.869 1.00 7.24 C -ANISOU 178 CA LYS A 27 912 835 1004 8 172 -259 C -ATOM 179 C LYS A 27 -3.300 33.609 17.242 1.00 6.26 C -ANISOU 179 C LYS A 27 739 778 862 115 30 -163 C -ATOM 180 O LYS A 27 -3.301 33.157 18.387 1.00 7.19 O -ANISOU 180 O LYS A 27 775 1012 944 -25 88 -206 O -ATOM 181 CB LYS A 27 -2.985 36.136 17.173 1.00 11.34 C -ANISOU 181 CB LYS A 27 1700 741 1867 10 838 -370 C -ATOM 182 CG LYS A 27 -1.804 37.171 17.273 1.00 17.41 C -ANISOU 182 CG LYS A 27 1821 1317 3475 -390 1465 -350 C -ATOM 183 CD LYS A 27 -2.224 38.580 17.469 1.00 17.34 C -ANISOU 183 CD LYS A 27 2485 1255 2849 -605 1381 -567 C -ATOM 184 CE ALYS A 27 -1.005 39.463 17.746 0.48 13.04 C -ANISOU 184 CE ALYS A 27 1734 1150 2071 312 -330 193 C -ATOM 185 CE BLYS A 27 -1.024 39.493 17.619 0.52 13.39 C -ANISOU 185 CE BLYS A 27 1527 1374 2187 -112 1261 -262 C -ATOM 186 NZ ALYS A 27 -1.370 40.910 17.483 0.48 9.47 N -ANISOU 186 NZ ALYS A 27 948 999 1654 28 182 18 N -ATOM 187 NZ BLYS A 27 -0.739 39.951 18.999 0.52 13.21 N -ANISOU 187 NZ BLYS A 27 818 2366 1835 505 170 645 N -ATOM 188 N GLU A 28 -4.094 33.127 16.291 1.00 6.28 N -ANISOU 188 N GLU A 28 640 756 988 84 -44 -69 N -ATOM 189 CA GLU A 28 -4.906 31.951 16.556 1.00 6.43 C -ANISOU 189 CA GLU A 28 573 887 984 109 -8 -3 C -ATOM 190 C GLU A 28 -4.016 30.696 16.743 1.00 5.62 C -ANISOU 190 C GLU A 28 557 785 795 17 4 -11 C -ATOM 191 O GLU A 28 -4.285 29.884 17.619 1.00 6.56 O -ANISOU 191 O GLU A 28 635 939 920 57 150 74 O -ATOM 192 CB GLU A 28 -5.954 31.706 15.463 1.00 6.75 C -ANISOU 192 CB GLU A 28 571 895 1099 67 -69 -29 C -ATOM 193 CG GLU A 28 -6.989 32.793 15.438 1.00 7.34 C -ANISOU 193 CG GLU A 28 722 1008 1059 180 -116 -82 C -ATOM 194 CD GLU A 28 -8.207 32.465 14.586 1.00 8.02 C -ANISOU 194 CD GLU A 28 665 1023 1361 143 -170 -155 C -ATOM 195 OE1 GLU A 28 -8.245 31.364 13.987 1.00 10.29 O -ANISOU 195 OE1 GLU A 28 866 1324 1718 230 -318 -519 O -ATOM 196 OE2 GLU A 28 -9.155 33.250 14.554 1.00 9.37 O -ANISOU 196 OE2 GLU A 28 763 1293 1503 323 -238 -325 O -ATOM 197 N PHE A 29 -2.999 30.574 15.889 1.00 5.30 N -ANISOU 197 N PHE A 29 567 762 685 4 22 -46 N -ATOM 198 CA PHE A 29 -2.081 29.450 16.018 1.00 4.91 C -ANISOU 198 CA PHE A 29 582 615 667 -3 26 -62 C -ATOM 199 C PHE A 29 -1.404 29.475 17.390 1.00 4.78 C -ANISOU 199 C PHE A 29 524 639 653 -24 55 -30 C -ATOM 200 O PHE A 29 -1.283 28.445 18.065 1.00 5.12 O -ANISOU 200 O PHE A 29 620 687 638 3 1 -14 O -ATOM 201 CB PHE A 29 -1.049 29.524 14.868 1.00 4.98 C -ANISOU 201 CB PHE A 29 589 698 606 30 -14 18 C -ATOM 202 CG PHE A 29 -0.112 28.345 14.851 1.00 5.59 C -ANISOU 202 CG PHE A 29 705 806 614 122 139 137 C -ATOM 203 CD1 PHE A 29 1.033 28.305 15.587 1.00 7.97 C -ANISOU 203 CD1 PHE A 29 586 1359 1084 141 122 525 C -ATOM 204 CD2 PHE A 29 -0.400 27.260 14.055 1.00 7.37 C -ANISOU 204 CD2 PHE A 29 1137 760 902 122 302 20 C -ATOM 205 CE1 PHE A 29 1.884 27.212 15.557 1.00 11.56 C -ANISOU 205 CE1 PHE A 29 783 1952 1657 499 376 1000 C -ATOM 206 CE2 PHE A 29 0.440 26.156 14.046 1.00 10.74 C -ANISOU 206 CE2 PHE A 29 1811 891 1378 508 863 356 C -ATOM 207 CZ PHE A 29 1.582 26.128 14.775 1.00 12.72 C -ANISOU 207 CZ PHE A 29 1643 1429 1763 889 895 933 C -ATOM 208 N PHE A 30 -0.919 30.648 17.811 1.00 5.33 N -ANISOU 208 N PHE A 30 701 709 616 -40 -1 -45 N -ATOM 209 CA APHE A 30 -0.253 30.781 19.092 0.41 5.91 C -ANISOU 209 CA APHE A 30 748 907 589 -100 0 -123 C -ATOM 210 CA BPHE A 30 -0.199 30.689 19.092 0.59 5.68 C -ANISOU 210 CA BPHE A 30 781 757 622 -116 -43 -17 C -ATOM 211 C PHE A 30 -1.135 30.286 20.241 1.00 5.62 C -ANISOU 211 C PHE A 30 858 671 605 -16 -10 -106 C -ATOM 212 O PHE A 30 -0.631 29.652 21.178 1.00 6.45 O -ANISOU 212 O PHE A 30 922 879 650 59 38 8 O -ATOM 213 CB APHE A 30 0.054 32.250 19.451 0.41 6.28 C -ANISOU 213 CB APHE A 30 841 896 650 -79 -50 -136 C -ATOM 214 CB BPHE A 30 0.370 32.114 19.277 0.59 6.84 C -ANISOU 214 CB BPHE A 30 1000 889 711 -203 -8 -106 C -ATOM 215 CG APHE A 30 0.948 32.981 18.508 0.41 6.50 C -ANISOU 215 CG APHE A 30 719 876 876 -174 -66 -219 C -ATOM 216 CG BPHE A 30 1.583 32.458 18.472 0.59 7.42 C -ANISOU 216 CG BPHE A 30 1019 1141 661 -401 28 -198 C -ATOM 217 CD1APHE A 30 1.893 32.342 17.752 0.41 8.04 C -ANISOU 217 CD1APHE A 30 568 1140 1348 -160 105 -248 C -ATOM 218 CD1BPHE A 30 2.667 31.620 18.314 0.59 8.37 C -ANISOU 218 CD1BPHE A 30 1032 1313 838 -334 213 -442 C -ATOM 219 CD2APHE A 30 0.834 34.371 18.371 0.41 6.74 C -ANISOU 219 CD2APHE A 30 797 984 782 -32 -54 43 C -ATOM 220 CD2BPHE A 30 1.662 33.713 17.869 0.59 8.95 C -ANISOU 220 CD2BPHE A 30 1073 1508 821 -546 -398 312 C -ATOM 221 CE1APHE A 30 2.692 33.046 16.880 0.41 9.56 C -ANISOU 221 CE1APHE A 30 1012 1535 1085 -319 172 -274 C -ATOM 222 CE1BPHE A 30 3.803 32.019 17.601 0.59 10.36 C -ANISOU 222 CE1BPHE A 30 1105 1883 951 -583 156 -512 C -ATOM 223 CE2APHE A 30 1.629 35.078 17.503 0.41 8.53 C -ANISOU 223 CE2APHE A 30 985 1225 1033 -528 63 -111 C -ATOM 224 CE2BPHE A 30 2.759 34.148 17.150 0.59 10.38 C -ANISOU 224 CE2BPHE A 30 1388 1904 652 -907 -493 422 C -ATOM 225 CZ APHE A 30 2.570 34.414 16.743 0.41 9.60 C -ANISOU 225 CZ APHE A 30 1221 1498 930 -484 238 -102 C -ATOM 226 CZ BPHE A 30 3.858 33.294 17.027 0.59 11.42 C -ANISOU 226 CZ BPHE A 30 1130 2572 638 -884 -171 92 C -ATOM 227 N ALA A 31 -2.412 30.620 20.185 1.00 5.82 N -ANISOU 227 N ALA A 31 870 673 669 -4 105 20 N -ATOM 228 CA ALA A 31 -3.342 30.170 21.221 1.00 6.70 C -ANISOU 228 CA ALA A 31 981 748 815 33 213 -106 C -ATOM 229 C ALA A 31 -3.538 28.670 21.139 1.00 6.38 C -ANISOU 229 C ALA A 31 841 725 859 65 231 15 C -ATOM 230 O ALA A 31 -3.453 27.973 22.146 1.00 6.62 O -ANISOU 230 O ALA A 31 928 816 772 67 83 59 O -ATOM 231 CB ALA A 31 -4.646 30.928 21.077 1.00 8.74 C -ANISOU 231 CB ALA A 31 1087 1033 1200 273 461 5 C -ATOM 232 N LYS A 32 -3.855 28.160 19.950 1.00 6.03 N -ANISOU 232 N LYS A 32 858 679 755 15 174 52 N -ATOM 233 CA LYS A 32 -4.215 26.743 19.808 1.00 6.56 C -ANISOU 233 CA LYS A 32 795 743 954 -9 143 18 C -ATOM 234 C LYS A 32 -3.079 25.840 20.183 1.00 6.30 C -ANISOU 234 C LYS A 32 756 674 962 -78 46 3 C -ATOM 235 O LYS A 32 -3.292 24.777 20.752 1.00 7.67 O -ANISOU 235 O LYS A 32 749 754 1410 -30 162 149 O -ATOM 236 CB LYS A 32 -4.712 26.504 18.396 1.00 7.55 C -ANISOU 236 CB LYS A 32 1149 847 874 35 63 -75 C -ATOM 237 CG LYS A 32 -5.309 25.137 18.183 1.00 9.08 C -ANISOU 237 CG LYS A 32 1143 1144 1161 24 69 -277 C -ATOM 238 CD LYS A 32 -6.540 24.871 19.016 1.00 16.22 C -ANISOU 238 CD LYS A 32 1316 1858 2990 -681 631 -1063 C -ATOM 239 CE LYS A 32 -7.083 23.453 18.801 1.00 24.33 C -ANISOU 239 CE LYS A 32 1691 1842 5711 -771 727 -1142 C -ATOM 240 NZ LYS A 32 -8.125 23.161 19.823 1.00 34.66 N -ANISOU 240 NZ LYS A 32 3072 2146 7952 -1421 2220 -897 N -ATOM 241 N VAL A 33 -1.843 26.214 19.825 1.00 6.28 N -ANISOU 241 N VAL A 33 765 689 932 -42 188 -156 N -ATOM 242 CA AVAL A 33 -0.756 25.292 20.149 0.58 7.87 C -ANISOU 242 CA AVAL A 33 776 862 1353 -16 100 -341 C -ATOM 243 CA BVAL A 33 -0.662 25.399 20.085 0.42 6.75 C -ANISOU 243 CA BVAL A 33 748 467 1349 -89 180 -335 C -ATOM 244 C VAL A 33 -0.301 25.373 21.591 1.00 6.98 C -ANISOU 244 C VAL A 33 653 662 1338 -19 141 -64 C -ATOM 245 O VAL A 33 0.458 24.517 22.012 1.00 9.20 O -ANISOU 245 O VAL A 33 861 791 1845 159 63 53 O -ATOM 246 CB AVAL A 33 0.637 25.454 19.498 0.58 6.28 C -ANISOU 246 CB AVAL A 33 801 693 891 140 -94 -28 C -ATOM 247 CB BVAL A 33 0.369 25.907 19.038 0.42 5.69 C -ANISOU 247 CB BVAL A 33 557 693 912 57 -57 -304 C -ATOM 248 CG1AVAL A 33 0.381 25.228 18.025 0.58 6.46 C -ANISOU 248 CG1AVAL A 33 1024 582 851 102 -157 -57 C -ATOM 249 CG1BVAL A 33 1.270 27.020 19.608 0.42 8.25 C -ANISOU 249 CG1BVAL A 33 752 912 1471 -367 358 -707 C -ATOM 250 CG2AVAL A 33 1.220 26.838 19.650 0.58 6.02 C -ANISOU 250 CG2AVAL A 33 683 1037 568 -47 47 -134 C -ATOM 251 CG2BVAL A 33 1.293 24.796 18.573 0.42 4.81 C -ANISOU 251 CG2BVAL A 33 702 551 573 140 -47 -68 C -ATOM 252 N GLY A 34 -0.780 26.382 22.320 1.00 6.81 N -ANISOU 252 N GLY A 34 823 768 996 65 -41 19 N -ATOM 253 CA GLY A 34 -0.499 26.533 23.746 1.00 7.62 C -ANISOU 253 CA GLY A 34 976 886 1032 0 6 80 C -ATOM 254 C GLY A 34 0.534 27.565 24.071 1.00 6.86 C -ANISOU 254 C GLY A 34 762 932 914 84 -78 -9 C -ATOM 255 O GLY A 34 0.817 27.766 25.270 1.00 8.26 O -ANISOU 255 O GLY A 34 1061 1153 924 -43 -36 38 O -ATOM 256 N LEU A 35 1.143 28.233 23.118 1.00 6.40 N -ANISOU 256 N LEU A 35 749 861 820 78 -17 -52 N -ATOM 257 CA LEU A 35 2.189 29.217 23.396 1.00 6.60 C -ANISOU 257 CA LEU A 35 749 952 808 50 13 -166 C -ATOM 258 C LEU A 35 1.642 30.467 24.112 1.00 6.49 C -ANISOU 258 C LEU A 35 785 852 830 -124 108 -53 C -ATOM 259 O LEU A 35 2.332 31.022 24.941 1.00 7.22 O -ANISOU 259 O LEU A 35 873 1076 795 -137 29 -152 O -ATOM 260 CB ALEU A 35 2.948 29.653 22.143 0.77 7.74 C -ANISOU 260 CB ALEU A 35 726 1204 1011 93 163 -51 C -ATOM 261 CB BLEU A 35 2.918 29.669 22.132 0.23 6.73 C -ANISOU 261 CB BLEU A 35 1109 592 856 -112 40 -215 C -ATOM 262 CG ALEU A 35 4.043 28.693 21.737 0.77 7.64 C -ANISOU 262 CG ALEU A 35 782 818 1301 -63 243 -224 C -ATOM 263 CG BLEU A 35 4.403 30.017 22.297 0.23 13.64 C -ANISOU 263 CG BLEU A 35 1006 1636 2540 -154 303 158 C -ATOM 264 CD1ALEU A 35 4.503 29.017 20.310 0.77 9.81 C -ANISOU 264 CD1ALEU A 35 1073 1288 1366 -309 584 -464 C -ATOM 265 CD1BLEU A 35 5.096 29.032 23.231 0.23 16.36 C -ANISOU 265 CD1BLEU A 35 494 2570 3153 301 250 429 C -ATOM 266 CD2ALEU A 35 5.236 28.723 22.679 0.77 10.96 C -ANISOU 266 CD2ALEU A 35 632 1721 1812 169 123 152 C -ATOM 267 CD2BLEU A 35 5.095 30.057 20.954 0.23 11.42 C -ANISOU 267 CD2BLEU A 35 697 1084 2557 115 248 -540 C -ATOM 268 N ALA A 36 0.431 30.880 23.772 1.00 7.22 N -ANISOU 268 N ALA A 36 875 872 996 23 -5 -120 N -ATOM 269 CA ALA A 36 -0.136 32.049 24.442 1.00 8.16 C -ANISOU 269 CA ALA A 36 1122 848 1129 21 103 -262 C -ATOM 270 C ALA A 36 -0.311 31.824 25.965 1.00 8.60 C -ANISOU 270 C ALA A 36 1011 1221 1034 214 27 -330 C -ATOM 271 O ALA A 36 -0.332 32.824 26.672 1.00 12.06 O -ANISOU 271 O ALA A 36 1712 1415 1455 192 -55 -650 O -ATOM 272 CB ALA A 36 -1.427 32.468 23.803 1.00 9.07 C -ANISOU 272 CB ALA A 36 1228 912 1308 123 -98 -141 C -ATOM 273 N SER A 37 -0.393 30.587 26.414 1.00 8.48 N -ANISOU 273 N SER A 37 932 1297 992 -47 133 -168 N -ATOM 274 CA ASER A 37 -0.559 30.202 27.813 0.61 9.54 C -ANISOU 274 CA ASER A 37 1028 1534 1061 153 211 -191 C -ATOM 275 CA BSER A 37 -0.545 30.349 27.852 0.40 10.01 C -ANISOU 275 CA BSER A 37 897 1832 1076 -204 160 -119 C -ATOM 276 C SER A 37 0.759 29.925 28.492 1.00 8.82 C -ANISOU 276 C SER A 37 1176 1300 875 -13 157 -155 C -ATOM 277 O SER A 37 0.746 29.619 29.681 1.00 11.82 O -ANISOU 277 O SER A 37 1516 2064 912 -6 173 11 O -ATOM 278 CB ASER A 37 -1.445 28.942 27.877 0.61 11.52 C -ANISOU 278 CB ASER A 37 1196 2326 855 -445 411 49 C -ATOM 279 CB BSER A 37 -1.602 29.277 28.095 0.40 13.55 C -ANISOU 279 CB BSER A 37 1469 2582 1097 -819 340 -130 C -ATOM 280 OG ASER A 37 -2.763 29.307 27.447 0.61 14.79 O -ANISOU 280 OG ASER A 37 1236 2995 1389 -476 68 396 O -ATOM 281 OG BSER A 37 -1.239 28.071 27.460 0.40 25.02 O -ANISOU 281 OG BSER A 37 3512 2594 3400 -1161 -441 -1395 O -ATOM 282 N LYS A 38 1.889 29.926 27.754 1.00 8.38 N -ANISOU 282 N LYS A 38 988 1305 892 173 56 40 N -ATOM 283 CA LYS A 38 3.203 29.712 28.341 1.00 8.90 C -ANISOU 283 CA LYS A 38 1180 1209 993 238 -2 44 C -ATOM 284 C LYS A 38 3.724 30.949 29.026 1.00 8.29 C -ANISOU 284 C LYS A 38 1051 1289 810 161 55 112 C -ATOM 285 O LYS A 38 3.417 32.080 28.652 1.00 9.08 O -ANISOU 285 O LYS A 38 1314 1339 797 394 -51 -162 O -ATOM 286 CB LYS A 38 4.197 29.256 27.257 1.00 9.06 C -ANISOU 286 CB LYS A 38 1120 1356 967 166 -34 -33 C -ATOM 287 CG LYS A 38 4.023 27.826 26.792 1.00 9.89 C -ANISOU 287 CG LYS A 38 1317 1467 974 330 45 -82 C -ATOM 288 CD LYS A 38 4.591 26.859 27.882 1.00 12.30 C -ANISOU 288 CD LYS A 38 1938 1616 1120 749 -1 -21 C -ATOM 289 CE LYS A 38 4.660 25.452 27.379 1.00 12.97 C -ANISOU 289 CE LYS A 38 1614 1637 1678 655 -571 -417 C -ATOM 290 NZ LYS A 38 5.433 24.593 28.353 1.00 13.46 N -ANISOU 290 NZ LYS A 38 2365 1359 1389 728 -560 -493 N -ATOM 291 N SER A 39 4.621 30.733 30.005 1.00 8.81 N -ANISOU 291 N SER A 39 1290 1334 724 224 33 20 N -ATOM 292 CA SER A 39 5.347 31.791 30.636 1.00 8.88 C -ANISOU 292 CA SER A 39 1304 1330 741 313 23 -64 C -ATOM 293 C SER A 39 6.199 32.560 29.614 1.00 7.78 C -ANISOU 293 C SER A 39 906 1294 755 248 -144 -188 C -ATOM 294 O SER A 39 6.647 32.017 28.613 1.00 8.07 O -ANISOU 294 O SER A 39 937 1396 732 275 -9 -346 O -ATOM 295 CB SER A 39 6.283 31.304 31.744 1.00 11.37 C -ANISOU 295 CB SER A 39 2000 1555 766 167 -204 -129 C -ATOM 296 OG SER A 39 7.271 30.526 31.275 1.00 15.52 O -ANISOU 296 OG SER A 39 2377 1869 1649 786 -1055 -524 O -ATOM 297 N LEU A 40 6.558 33.777 29.982 1.00 8.20 N -ANISOU 297 N LEU A 40 1100 1411 603 179 -3 -173 N -ATOM 298 CA LEU A 40 7.496 34.538 29.147 1.00 8.02 C -ANISOU 298 CA LEU A 40 1142 1236 668 275 76 -151 C -ATOM 299 C LEU A 40 8.800 33.785 28.937 1.00 7.90 C -ANISOU 299 C LEU A 40 1108 1185 708 170 -20 -282 C -ATOM 300 O LEU A 40 9.315 33.755 27.794 1.00 7.81 O -ANISOU 300 O LEU A 40 1086 1020 862 131 72 -310 O -ATOM 301 CB LEU A 40 7.762 35.925 29.783 1.00 9.19 C -ANISOU 301 CB LEU A 40 1519 1258 715 324 93 -228 C -ATOM 302 CG LEU A 40 8.758 36.769 29.022 1.00 10.07 C -ANISOU 302 CG LEU A 40 1620 1125 1082 224 21 -237 C -ATOM 303 CD1 LEU A 40 8.283 37.027 27.612 1.00 10.31 C -ANISOU 303 CD1 LEU A 40 1444 1346 1128 280 68 41 C -ATOM 304 CD2 LEU A 40 8.982 38.057 29.799 1.00 14.07 C -ANISOU 304 CD2 LEU A 40 2534 1245 1567 91 -34 -406 C -ATOM 305 N ASP A 41 9.339 33.170 29.967 1.00 9.38 N -ANISOU 305 N ASP A 41 1164 1602 798 314 -233 -321 N -ATOM 306 CA ASP A 41 10.565 32.384 29.799 1.00 10.82 C -ANISOU 306 CA ASP A 41 1119 1638 1353 284 -508 -406 C -ATOM 307 C ASP A 41 10.437 31.347 28.694 1.00 8.50 C -ANISOU 307 C ASP A 41 972 1289 967 359 -171 -134 C -ATOM 308 O ASP A 41 11.310 31.161 27.852 1.00 9.41 O -ANISOU 308 O ASP A 41 789 1341 1447 308 -95 -200 O -ATOM 309 CB ASP A 41 11.007 31.698 31.101 1.00 14.05 C -ANISOU 309 CB ASP A 41 1751 2314 1275 658 -893 -582 C -ATOM 310 CG ASP A 41 12.169 30.719 31.027 1.00 24.28 C -ANISOU 310 CG ASP A 41 3083 3075 3066 1654 -772 150 C -ATOM 311 OD1 ASP A 41 13.274 30.989 30.462 1.00 25.64 O -ANISOU 311 OD1 ASP A 41 2595 3899 3247 1994 -724 -1125 O -ATOM 312 OD2 ASP A 41 12.055 29.602 31.643 1.00 34.84 O -ANISOU 312 OD2 ASP A 41 6248 3192 3796 1950 -1193 656 O -ATOM 313 N ASP A 42 9.343 30.619 28.728 1.00 7.94 N -ANISOU 313 N ASP A 42 979 1278 758 264 -37 -38 N -ATOM 314 CA ASP A 42 9.109 29.568 27.772 1.00 7.35 C -ANISOU 314 CA ASP A 42 946 1079 767 336 -53 -20 C -ATOM 315 C ASP A 42 8.842 30.112 26.383 1.00 6.58 C -ANISOU 315 C ASP A 42 792 914 795 149 -59 -95 C -ATOM 316 O ASP A 42 9.266 29.523 25.358 1.00 6.72 O -ANISOU 316 O ASP A 42 884 809 862 175 106 -118 O -ATOM 317 CB ASP A 42 7.972 28.656 28.244 1.00 8.30 C -ANISOU 317 CB ASP A 42 1126 1125 902 279 132 58 C -ATOM 318 CG ASP A 42 8.364 27.792 29.427 1.00 10.00 C -ANISOU 318 CG ASP A 42 1403 1378 1018 388 203 187 C -ATOM 319 OD1 ASP A 42 9.515 27.668 29.789 1.00 13.13 O -ANISOU 319 OD1 ASP A 42 1610 1959 1420 348 -309 433 O -ATOM 320 OD2 ASP A 42 7.451 27.194 30.010 1.00 17.33 O -ANISOU 320 OD2 ASP A 42 1640 2819 2126 610 515 1480 O -ATOM 321 N VAL A 43 8.178 31.262 26.283 1.00 5.96 N -ANISOU 321 N VAL A 43 749 912 605 222 15 -124 N -ATOM 322 CA VAL A 43 7.977 31.877 24.986 1.00 6.18 C -ANISOU 322 CA VAL A 43 781 938 629 264 -61 -161 C -ATOM 323 C VAL A 43 9.316 32.292 24.369 1.00 5.96 C -ANISOU 323 C VAL A 43 776 831 656 260 -39 -159 C -ATOM 324 O VAL A 43 9.562 32.142 23.164 1.00 6.54 O -ANISOU 324 O VAL A 43 862 977 646 274 -29 -146 O -ATOM 325 CB VAL A 43 7.003 33.075 25.101 1.00 6.64 C -ANISOU 325 CB VAL A 43 742 1011 770 288 -7 -126 C -ATOM 326 CG1 VAL A 43 6.943 33.871 23.850 1.00 8.11 C -ANISOU 326 CG1 VAL A 43 916 1096 1068 346 28 89 C -ATOM 327 CG2 VAL A 43 5.611 32.545 25.437 1.00 7.48 C -ANISOU 327 CG2 VAL A 43 684 1225 934 311 -1 23 C -ATOM 328 N LYS A 44 10.234 32.840 25.181 1.00 5.81 N -ANISOU 328 N LYS A 44 777 803 625 204 -55 -130 N -ATOM 329 CA LYS A 44 11.550 33.168 24.719 1.00 6.25 C -ANISOU 329 CA LYS A 44 841 733 801 141 -76 -72 C -ATOM 330 C LYS A 44 12.255 31.928 24.178 1.00 5.71 C -ANISOU 330 C LYS A 44 700 741 728 98 -37 -49 C -ATOM 331 O LYS A 44 12.951 32.006 23.147 1.00 6.38 O -ANISOU 331 O LYS A 44 801 813 809 137 21 30 O -ATOM 332 CB LYS A 44 12.389 33.801 25.832 1.00 7.09 C -ANISOU 332 CB LYS A 44 854 873 965 57 -91 -127 C -ATOM 333 CG LYS A 44 11.921 35.191 26.217 1.00 8.04 C -ANISOU 333 CG LYS A 44 1257 864 933 98 -5 -167 C -ATOM 334 CD LYS A 44 12.730 35.765 27.336 1.00 11.92 C -ANISOU 334 CD LYS A 44 1988 1249 1292 322 -449 -479 C -ATOM 335 CE LYS A 44 12.388 37.180 27.704 1.00 12.69 C -ANISOU 335 CE LYS A 44 1986 1233 1602 -176 -110 -559 C -ATOM 336 NZ LYS A 44 13.226 37.553 28.904 1.00 21.77 N -ANISOU 336 NZ LYS A 44 3351 2486 2433 166 -1008 -1569 N -ATOM 337 N LYS A 45 12.151 30.776 24.846 1.00 5.78 N -ANISOU 337 N LYS A 45 799 767 632 148 28 -13 N -ATOM 338 CA LYS A 45 12.787 29.587 24.322 1.00 5.73 C -ANISOU 338 CA LYS A 45 674 774 729 135 37 -20 C -ATOM 339 C LYS A 45 12.286 29.265 22.928 1.00 5.80 C -ANISOU 339 C LYS A 45 672 742 790 147 0 -34 C -ATOM 340 O LYS A 45 13.067 28.886 22.013 1.00 6.08 O -ANISOU 340 O LYS A 45 748 879 685 249 63 -3 O -ATOM 341 CB LYS A 45 12.507 28.374 25.218 1.00 6.47 C -ANISOU 341 CB LYS A 45 816 715 925 89 62 75 C -ATOM 342 CG LYS A 45 13.066 28.492 26.632 1.00 6.67 C -ANISOU 342 CG LYS A 45 1000 826 707 125 165 -18 C -ATOM 343 CD LYS A 45 12.555 27.351 27.453 1.00 9.07 C -ANISOU 343 CD LYS A 45 1341 1191 913 173 372 218 C -ATOM 344 CE LYS A 45 12.805 27.573 28.954 1.00 11.81 C -ANISOU 344 CE LYS A 45 1782 1565 1140 -10 -237 467 C -ATOM 345 NZ LYS A 45 12.017 26.590 29.703 1.00 13.78 N -ANISOU 345 NZ LYS A 45 2388 1639 1210 345 838 347 N -ATOM 346 N ALA A 46 10.989 29.410 22.705 1.00 5.77 N -ANISOU 346 N ALA A 46 602 779 813 114 58 -125 N -ATOM 347 CA ALA A 46 10.426 29.120 21.397 1.00 5.90 C -ANISOU 347 CA ALA A 46 650 789 804 52 23 -152 C -ATOM 348 C ALA A 46 10.979 30.035 20.321 1.00 5.70 C -ANISOU 348 C ALA A 46 562 828 777 145 -36 -107 C -ATOM 349 O ALA A 46 11.232 29.600 19.200 1.00 6.14 O -ANISOU 349 O ALA A 46 716 899 717 133 14 -145 O -ATOM 350 CB ALA A 46 8.902 29.221 21.463 1.00 6.82 C -ANISOU 350 CB ALA A 46 639 1027 926 114 -9 -236 C -ATOM 351 N PHE A 47 11.187 31.312 20.652 1.00 5.83 N -ANISOU 351 N PHE A 47 683 829 701 152 0 -134 N -ATOM 352 CA PHE A 47 11.754 32.236 19.671 1.00 5.94 C -ANISOU 352 CA PHE A 47 735 813 707 139 -13 -20 C -ATOM 353 C PHE A 47 13.050 31.724 19.080 1.00 5.68 C -ANISOU 353 C PHE A 47 664 821 673 139 1 48 C -ATOM 354 O PHE A 47 13.289 31.773 17.889 1.00 6.22 O -ANISOU 354 O PHE A 47 888 815 659 251 67 35 O -ATOM 355 CB PHE A 47 12.045 33.595 20.368 1.00 6.06 C -ANISOU 355 CB PHE A 47 787 789 726 140 -60 21 C -ATOM 356 CG PHE A 47 12.817 34.542 19.487 1.00 5.99 C -ANISOU 356 CG PHE A 47 821 887 568 177 -4 5 C -ATOM 357 CD1 PHE A 47 12.179 35.256 18.483 1.00 6.19 C -ANISOU 357 CD1 PHE A 47 922 710 718 217 -67 -71 C -ATOM 358 CD2 PHE A 47 14.180 34.709 19.657 1.00 6.72 C -ANISOU 358 CD2 PHE A 47 879 979 694 -15 -110 73 C -ATOM 359 CE1 PHE A 47 12.850 36.099 17.678 1.00 6.69 C -ANISOU 359 CE1 PHE A 47 1192 783 567 189 -87 -17 C -ATOM 360 CE2 PHE A 47 14.902 35.528 18.807 1.00 7.58 C -ANISOU 360 CE2 PHE A 47 839 1166 874 -100 -102 170 C -ATOM 361 CZ PHE A 47 14.218 36.200 17.809 1.00 7.41 C -ANISOU 361 CZ PHE A 47 1156 1000 661 -31 -61 96 C -ATOM 362 N TYR A 48 13.969 31.294 19.999 1.00 6.14 N -ANISOU 362 N TYR A 48 669 989 675 212 58 156 N -ATOM 363 CA TYR A 48 15.304 30.930 19.547 1.00 6.63 C -ANISOU 363 CA TYR A 48 754 908 857 224 88 211 C -ATOM 364 C TYR A 48 15.270 29.692 18.696 1.00 7.10 C -ANISOU 364 C TYR A 48 833 1058 806 266 158 259 C -ATOM 365 O TYR A 48 16.182 29.532 17.858 1.00 8.66 O -ANISOU 365 O TYR A 48 1044 1060 1185 243 361 86 O -ATOM 366 CB TYR A 48 16.299 30.905 20.735 1.00 7.32 C -ANISOU 366 CB TYR A 48 610 1287 883 245 77 326 C -ATOM 367 CG TYR A 48 16.528 32.251 21.345 1.00 7.58 C -ANISOU 367 CG TYR A 48 778 1291 810 123 -18 120 C -ATOM 368 CD1 TYR A 48 17.316 33.198 20.701 1.00 7.96 C -ANISOU 368 CD1 TYR A 48 815 1351 858 117 -8 230 C -ATOM 369 CD2 TYR A 48 15.913 32.636 22.546 1.00 7.65 C -ANISOU 369 CD2 TYR A 48 760 1391 756 247 -24 331 C -ATOM 370 CE1 TYR A 48 17.500 34.454 21.245 1.00 8.92 C -ANISOU 370 CE1 TYR A 48 905 1480 1006 -126 -75 -85 C -ATOM 371 CE2 TYR A 48 16.065 33.873 23.093 1.00 8.27 C -ANISOU 371 CE2 TYR A 48 923 1343 877 350 22 101 C -ATOM 372 CZ TYR A 48 16.857 34.787 22.463 1.00 8.20 C -ANISOU 372 CZ TYR A 48 851 1430 833 174 -198 193 C -ATOM 373 OH TYR A 48 17.052 36.072 22.941 1.00 10.96 O -ANISOU 373 OH TYR A 48 1671 1390 1103 69 -148 -212 O -ATOM 374 N VAL A 49 14.299 28.805 18.887 1.00 7.51 N -ANISOU 374 N VAL A 49 1072 838 942 279 267 80 N -ATOM 375 CA VAL A 49 14.117 27.686 18.016 1.00 8.24 C -ANISOU 375 CA VAL A 49 1101 855 1173 272 148 73 C -ATOM 376 C VAL A 49 13.676 28.129 16.612 1.00 7.74 C -ANISOU 376 C VAL A 49 1053 780 1108 119 215 -96 C -ATOM 377 O VAL A 49 14.156 27.688 15.531 1.00 9.63 O -ANISOU 377 O VAL A 49 1325 1015 1320 278 551 -11 O -ATOM 378 CB VAL A 49 13.075 26.717 18.587 1.00 8.90 C -ANISOU 378 CB VAL A 49 1415 790 1177 326 317 98 C -ATOM 379 CG1 VAL A 49 12.703 25.642 17.603 1.00 9.63 C -ANISOU 379 CG1 VAL A 49 1299 1029 1330 101 40 99 C -ATOM 380 CG2 VAL A 49 13.622 26.081 19.879 1.00 10.27 C -ANISOU 380 CG2 VAL A 49 1925 892 1085 45 216 99 C -ATOM 381 N ILE A 50 12.700 29.040 16.529 1.00 6.50 N -ANISOU 381 N ILE A 50 780 677 1014 0 236 -12 N -ATOM 382 CA AILE A 50 12.087 29.545 15.259 0.50 7.48 C -ANISOU 382 CA AILE A 50 647 915 1280 -43 175 90 C -ATOM 383 CA BILE A 50 12.152 29.439 15.218 0.50 6.03 C -ANISOU 383 CA BILE A 50 712 635 942 -41 235 -359 C -ATOM 384 C ILE A 50 13.167 30.287 14.463 1.00 5.63 C -ANISOU 384 C ILE A 50 695 692 754 40 25 -47 C -ATOM 385 O ILE A 50 13.134 30.314 13.220 1.00 6.27 O -ANISOU 385 O ILE A 50 708 776 897 -11 -32 -41 O -ATOM 386 CB AILE A 50 10.861 30.508 15.329 0.50 6.93 C -ANISOU 386 CB AILE A 50 469 790 1372 -150 53 -90 C -ATOM 387 CB BILE A 50 10.785 30.057 15.614 0.50 5.70 C -ANISOU 387 CB BILE A 50 552 802 810 -127 59 -326 C -ATOM 388 CG1AILE A 50 9.748 29.929 16.161 0.50 6.60 C -ANISOU 388 CG1AILE A 50 653 757 1096 33 79 7 C -ATOM 389 CG1BILE A 50 9.906 28.964 16.175 0.50 5.49 C -ANISOU 389 CG1BILE A 50 557 768 762 -73 66 -226 C -ATOM 390 CG2AILE A 50 10.340 30.914 13.953 0.50 6.53 C -ANISOU 390 CG2AILE A 50 450 865 1167 -17 248 -124 C -ATOM 391 CG2BILE A 50 10.140 30.783 14.473 0.50 6.07 C -ANISOU 391 CG2BILE A 50 530 977 799 -147 134 -227 C -ATOM 392 CD1AILE A 50 9.177 28.610 15.711 0.50 6.82 C -ANISOU 392 CD1AILE A 50 714 712 1166 -112 312 -28 C -ATOM 393 CD1BILE A 50 8.673 29.502 16.923 0.50 6.89 C -ANISOU 393 CD1BILE A 50 554 1256 806 88 29 -8 C -ATOM 394 N ASP A 51 14.088 30.940 15.164 1.00 5.40 N -ANISOU 394 N ASP A 51 516 819 718 -47 65 -69 N -ATOM 395 CA ASP A 51 15.272 31.557 14.554 1.00 5.48 C -ANISOU 395 CA ASP A 51 601 816 664 -31 6 3 C -ATOM 396 C ASP A 51 16.254 30.461 14.132 1.00 5.80 C -ANISOU 396 C ASP A 51 671 878 653 -74 114 35 C -ATOM 397 O ASP A 51 17.243 30.174 14.803 1.00 6.51 O -ANISOU 397 O ASP A 51 694 1003 779 85 24 43 O -ATOM 398 CB ASP A 51 15.892 32.484 15.596 1.00 6.08 C -ANISOU 398 CB ASP A 51 676 893 742 -79 92 -89 C -ATOM 399 CG ASP A 51 17.231 33.029 15.135 1.00 5.94 C -ANISOU 399 CG ASP A 51 637 880 741 -34 9 0 C -ATOM 400 OD1 ASP A 51 17.484 33.086 13.930 1.00 6.26 O -ANISOU 400 OD1 ASP A 51 631 957 789 -80 13 67 O -ATOM 401 OD2 ASP A 51 18.025 33.412 16.064 1.00 7.31 O -ANISOU 401 OD2 ASP A 51 704 1165 908 -198 -68 -28 O -ATOM 402 N GLN A 52 15.958 29.849 13.008 1.00 5.82 N -ANISOU 402 N GLN A 52 795 771 647 70 69 110 N -ATOM 403 CA GLN A 52 16.651 28.612 12.593 1.00 6.39 C -ANISOU 403 CA GLN A 52 955 801 671 114 85 53 C -ATOM 404 C GLN A 52 18.122 28.819 12.271 1.00 7.21 C -ANISOU 404 C GLN A 52 924 1079 735 215 183 114 C -ATOM 405 O GLN A 52 18.892 27.891 12.414 1.00 8.34 O -ANISOU 405 O GLN A 52 1110 1079 979 393 186 174 O -ATOM 406 CB GLN A 52 15.957 27.959 11.440 1.00 7.44 C -ANISOU 406 CB GLN A 52 1118 855 854 61 128 -14 C -ATOM 407 CG GLN A 52 14.542 27.416 11.786 1.00 8.25 C -ANISOU 407 CG GLN A 52 1212 910 1012 -103 37 50 C -ATOM 408 CD GLN A 52 14.098 26.497 10.693 1.00 10.85 C -ANISOU 408 CD GLN A 52 1475 1020 1627 -33 -471 -77 C -ATOM 409 OE1 GLN A 52 14.665 25.450 10.461 1.00 16.50 O -ANISOU 409 OE1 GLN A 52 2113 1361 2793 380 -966 -931 O -ATOM 410 NE2 GLN A 52 13.089 26.946 9.965 1.00 9.79 N -ANISOU 410 NE2 GLN A 52 1253 1170 1297 -122 -89 47 N -ATOM 411 N ASP A 53 18.468 30.001 11.740 1.00 7.02 N -ANISOU 411 N ASP A 53 805 1081 783 272 199 122 N -ATOM 412 CA ASP A 53 19.883 30.273 11.443 1.00 8.12 C -ANISOU 412 CA ASP A 53 806 1254 1026 322 375 324 C -ATOM 413 C ASP A 53 20.650 30.921 12.581 1.00 8.74 C -ANISOU 413 C ASP A 53 702 1374 1246 228 193 306 C -ATOM 414 O ASP A 53 21.833 31.253 12.409 1.00 10.98 O -ANISOU 414 O ASP A 53 638 1691 1844 190 319 658 O -ATOM 415 CB ASP A 53 20.023 31.087 10.133 1.00 8.72 C -ANISOU 415 CB ASP A 53 1006 1182 1124 324 512 311 C -ATOM 416 CG ASP A 53 19.575 32.495 10.278 1.00 8.46 C -ANISOU 416 CG ASP A 53 806 1225 1183 260 386 378 C -ATOM 417 OD1 ASP A 53 19.106 32.900 11.388 1.00 8.11 O -ANISOU 417 OD1 ASP A 53 706 1245 1129 197 284 191 O -ATOM 418 OD2 ASP A 53 19.635 33.251 9.270 1.00 11.40 O -ANISOU 418 OD2 ASP A 53 1654 1413 1263 461 622 518 O -ATOM 419 N LYS A 54 20.040 31.090 13.735 1.00 8.10 N -ANISOU 419 N LYS A 54 630 1426 1022 88 68 362 N -ATOM 420 CA LYS A 54 20.738 31.618 14.921 1.00 9.06 C -ANISOU 420 CA LYS A 54 654 1593 1195 68 -126 243 C -ATOM 421 C LYS A 54 21.260 33.008 14.674 1.00 9.96 C -ANISOU 421 C LYS A 54 586 1666 1533 12 -128 378 C -ATOM 422 O LYS A 54 22.288 33.400 15.252 1.00 12.81 O -ANISOU 422 O LYS A 54 833 2079 1954 -209 -549 495 O -ATOM 423 CB LYS A 54 21.824 30.695 15.435 1.00 12.25 C -ANISOU 423 CB LYS A 54 1097 1960 1597 117 -316 758 C -ATOM 424 CG LYS A 54 21.332 29.263 15.536 1.00 12.47 C -ANISOU 424 CG LYS A 54 1299 1764 1675 438 75 543 C -ATOM 425 CD LYS A 54 20.059 29.030 16.320 1.00 10.47 C -ANISOU 425 CD LYS A 54 1163 1665 1149 231 -191 266 C -ATOM 426 CE LYS A 54 19.292 27.804 15.955 1.00 9.71 C -ANISOU 426 CE LYS A 54 1389 1341 959 471 36 83 C -ATOM 427 NZ LYS A 54 18.019 27.706 16.673 1.00 9.53 N -ANISOU 427 NZ LYS A 54 1174 1176 1273 357 6 -21 N -ATOM 428 N SER A 55 20.539 33.800 13.903 1.00 8.65 N -ANISOU 428 N SER A 55 575 1435 1276 -149 -138 151 N -ATOM 429 CA SER A 55 20.947 35.132 13.627 1.00 9.42 C -ANISOU 429 CA SER A 55 735 1597 1249 -263 -190 293 C -ATOM 430 C SER A 55 20.511 36.121 14.717 1.00 9.33 C -ANISOU 430 C SER A 55 905 1472 1167 -357 -410 268 C -ATOM 431 O SER A 55 20.962 37.245 14.696 1.00 12.53 O -ANISOU 431 O SER A 55 1722 1632 1406 -895 -537 328 O -ATOM 432 CB SER A 55 20.314 35.633 12.344 1.00 8.90 C -ANISOU 432 CB SER A 55 722 1572 1090 -280 9 214 C -ATOM 433 OG SER A 55 18.888 35.730 12.484 1.00 7.45 O -ANISOU 433 OG SER A 55 673 1187 970 -157 -98 98 O -ATOM 434 N GLY A 56 19.631 35.693 15.626 1.00 8.51 N -ANISOU 434 N GLY A 56 812 1245 1175 -289 -368 199 N -ATOM 435 CA GLY A 56 19.073 36.549 16.613 1.00 9.48 C -ANISOU 435 CA GLY A 56 1244 1236 1122 -366 -579 52 C -ATOM 436 C GLY A 56 17.755 37.196 16.245 1.00 7.63 C -ANISOU 436 C GLY A 56 1133 990 778 -345 -197 -86 C -ATOM 437 O GLY A 56 17.136 37.884 17.064 1.00 9.61 O -ANISOU 437 O GLY A 56 1571 1278 802 -388 -118 -209 O -ATOM 438 N PHE A 57 17.313 36.985 15.009 1.00 6.28 N -ANISOU 438 N PHE A 57 802 840 743 -54 -142 -42 N -ATOM 439 CA PHE A 57 16.042 37.523 14.522 1.00 6.07 C -ANISOU 439 CA PHE A 57 756 802 749 -42 -75 -82 C -ATOM 440 C PHE A 57 15.337 36.447 13.734 1.00 5.64 C -ANISOU 440 C PHE A 57 656 802 684 -49 -3 -116 C -ATOM 441 O PHE A 57 15.999 35.609 13.105 1.00 6.73 O -ANISOU 441 O PHE A 57 608 978 969 -33 -53 -279 O -ATOM 442 CB PHE A 57 16.242 38.735 13.610 1.00 6.62 C -ANISOU 442 CB PHE A 57 869 890 757 -111 -119 -46 C -ATOM 443 CG PHE A 57 16.849 39.915 14.266 1.00 6.68 C -ANISOU 443 CG PHE A 57 734 861 942 -72 -113 13 C -ATOM 444 CD1 PHE A 57 18.260 40.066 14.318 1.00 7.16 C -ANISOU 444 CD1 PHE A 57 760 813 1149 -83 -128 68 C -ATOM 445 CD2 PHE A 57 16.079 40.877 14.876 1.00 6.97 C -ANISOU 445 CD2 PHE A 57 764 823 1062 -10 -264 -80 C -ATOM 446 CE1 PHE A 57 18.812 41.188 14.933 1.00 8.02 C -ANISOU 446 CE1 PHE A 57 791 940 1317 -147 -226 -7 C -ATOM 447 CE2 PHE A 57 16.628 41.980 15.473 1.00 8.41 C -ANISOU 447 CE2 PHE A 57 879 847 1470 12 -468 -138 C -ATOM 448 CZ PHE A 57 17.996 42.135 15.482 1.00 9.20 C -ANISOU 448 CZ PHE A 57 985 752 1759 22 -622 -88 C -ATOM 449 N ILE A 58 14.009 36.502 13.731 1.00 5.48 N -ANISOU 449 N ILE A 58 660 741 683 20 32 -111 N -ATOM 450 CA ILE A 58 13.237 35.733 12.780 1.00 4.99 C -ANISOU 450 CA ILE A 58 589 640 667 8 13 -55 C -ATOM 451 C ILE A 58 13.059 36.606 11.552 1.00 5.47 C -ANISOU 451 C ILE A 58 727 657 694 -70 22 -109 C -ATOM 452 O ILE A 58 12.401 37.642 11.593 1.00 6.89 O -ANISOU 452 O ILE A 58 1005 834 778 162 90 70 O -ATOM 453 CB ILE A 58 11.883 35.291 13.357 1.00 5.60 C -ANISOU 453 CB ILE A 58 608 786 732 66 40 -22 C -ATOM 454 CG1 ILE A 58 12.084 34.420 14.594 1.00 5.71 C -ANISOU 454 CG1 ILE A 58 734 749 688 -21 3 -60 C -ATOM 455 CG2 ILE A 58 11.094 34.555 12.304 1.00 7.93 C -ANISOU 455 CG2 ILE A 58 739 1431 842 -315 -179 246 C -ATOM 456 CD1 ILE A 58 10.826 34.217 15.420 1.00 7.50 C -ANISOU 456 CD1 ILE A 58 983 1057 809 -206 109 -152 C -ATOM 457 N GLU A 59 13.745 36.219 10.467 1.00 5.68 N -ANISOU 457 N GLU A 59 846 648 662 -27 27 -3 N -ATOM 458 CA GLU A 59 13.636 36.908 9.182 1.00 6.15 C -ANISOU 458 CA GLU A 59 976 671 689 -91 71 96 C -ATOM 459 C GLU A 59 12.418 36.376 8.422 1.00 5.83 C -ANISOU 459 C GLU A 59 843 633 738 7 86 62 C -ATOM 460 O GLU A 59 11.816 35.371 8.775 1.00 5.99 O -ANISOU 460 O GLU A 59 892 644 741 -73 -45 123 O -ATOM 461 CB GLU A 59 14.909 36.770 8.371 1.00 6.49 C -ANISOU 461 CB GLU A 59 915 813 739 -100 15 103 C -ATOM 462 CG GLU A 59 16.158 37.414 8.950 1.00 7.81 C -ANISOU 462 CG GLU A 59 1029 915 1023 -275 -53 254 C -ATOM 463 CD GLU A 59 16.958 36.597 9.981 1.00 7.48 C -ANISOU 463 CD GLU A 59 816 1026 1000 -149 -16 84 C -ATOM 464 OE1 GLU A 59 16.807 35.362 10.006 1.00 7.31 O -ANISOU 464 OE1 GLU A 59 959 968 850 -22 -37 195 O -ATOM 465 OE2 GLU A 59 17.745 37.239 10.706 1.00 9.79 O -ANISOU 465 OE2 GLU A 59 1402 1102 1216 -321 -388 251 O -ATOM 466 N GLU A 60 12.104 37.050 7.314 1.00 6.66 N -ANISOU 466 N GLU A 60 836 755 940 13 8 289 N -ATOM 467 CA AGLU A 60 10.909 36.685 6.575 0.63 7.04 C -ANISOU 467 CA AGLU A 60 832 895 945 7 -3 431 C -ATOM 468 CA BGLU A 60 10.902 36.688 6.568 0.37 7.37 C -ANISOU 468 CA BGLU A 60 940 923 938 39 -75 351 C -ATOM 469 C GLU A 60 10.938 35.257 6.092 1.00 6.97 C -ANISOU 469 C GLU A 60 928 916 805 -78 -174 363 C -ATOM 470 O GLU A 60 9.897 34.586 6.096 1.00 7.98 O -ANISOU 470 O GLU A 60 825 1103 1104 -112 -227 465 O -ATOM 471 CB AGLU A 60 10.811 37.729 5.450 0.63 9.85 C -ANISOU 471 CB AGLU A 60 1001 1233 1507 281 26 847 C -ATOM 472 CB BGLU A 60 10.628 37.461 5.266 0.37 7.67 C -ANISOU 472 CB BGLU A 60 1081 937 897 -87 -68 378 C -ATOM 473 CG AGLU A 60 9.440 37.905 4.937 0.63 11.62 C -ANISOU 473 CG AGLU A 60 1476 1606 1334 -102 -717 516 C -ATOM 474 CG BGLU A 60 10.083 38.824 5.545 0.37 7.76 C -ANISOU 474 CG BGLU A 60 1356 674 919 -221 -459 229 C -ATOM 475 CD AGLU A 60 9.274 38.996 3.900 0.63 15.89 C -ANISOU 475 CD AGLU A 60 1745 2628 1667 85 -744 1245 C -ATOM 476 CD BGLU A 60 9.750 39.657 4.308 0.37 8.41 C -ANISOU 476 CD BGLU A 60 1434 1112 649 260 12 267 C -ATOM 477 OE1AGLU A 60 10.030 39.988 3.902 0.63 28.10 O -ANISOU 477 OE1AGLU A 60 2023 4676 3979 -1344 -1481 3731 O -ATOM 478 OE1BGLU A 60 9.165 39.062 3.353 0.37 17.86 O -ANISOU 478 OE1BGLU A 60 3229 1510 2048 -38 -2208 886 O -ATOM 479 OE2AGLU A 60 8.356 38.855 3.097 0.63 21.02 O -ANISOU 479 OE2AGLU A 60 3464 2176 2347 572 -1863 604 O -ATOM 480 OE2BGLU A 60 10.007 40.857 4.154 0.37 12.17 O -ANISOU 480 OE2BGLU A 60 2676 899 1050 518 216 377 O -ATOM 481 N ASP A 61 12.100 34.740 5.654 1.00 7.00 N -ANISOU 481 N ASP A 61 978 981 700 -90 -1 186 N -ATOM 482 CA ASP A 61 12.138 33.360 5.190 1.00 7.94 C -ANISOU 482 CA ASP A 61 1210 1098 708 -32 -222 -28 C -ATOM 483 C ASP A 61 11.811 32.338 6.299 1.00 7.27 C -ANISOU 483 C ASP A 61 1142 856 764 109 -241 33 C -ATOM 484 O ASP A 61 11.208 31.290 6.056 1.00 9.17 O -ANISOU 484 O ASP A 61 1728 883 872 -7 -599 -64 O -ATOM 485 CB ASP A 61 13.454 33.019 4.516 1.00 10.20 C -ANISOU 485 CB ASP A 61 1410 1505 960 141 9 -62 C -ATOM 486 CG ASP A 61 14.753 33.158 5.257 1.00 11.04 C -ANISOU 486 CG ASP A 61 1262 1742 1193 103 162 -271 C -ATOM 487 OD1 ASP A 61 14.746 33.713 6.352 1.00 9.80 O -ANISOU 487 OD1 ASP A 61 1069 1523 1133 200 -49 59 O -ATOM 488 OD2 ASP A 61 15.786 32.705 4.678 1.00 18.93 O -ANISOU 488 OD2 ASP A 61 1204 4085 1902 -6 282 -1253 O -ATOM 489 N GLU A 62 12.191 32.693 7.552 1.00 6.93 N -ANISOU 489 N GLU A 62 1121 790 721 -120 -282 97 N -ATOM 490 CA GLU A 62 11.865 31.869 8.730 1.00 7.06 C -ANISOU 490 CA GLU A 62 1158 629 894 -95 -389 163 C -ATOM 491 C GLU A 62 10.403 32.003 9.134 1.00 6.61 C -ANISOU 491 C GLU A 62 1105 610 797 -154 -376 132 C -ATOM 492 O GLU A 62 9.871 31.062 9.719 1.00 8.57 O -ANISOU 492 O GLU A 62 970 742 1545 -238 -556 488 O -ATOM 493 CB GLU A 62 12.802 32.249 9.864 1.00 6.08 C -ANISOU 493 CB GLU A 62 972 601 736 -58 -259 132 C -ATOM 494 CG GLU A 62 14.240 31.824 9.612 1.00 6.78 C -ANISOU 494 CG GLU A 62 1027 712 838 86 -309 -70 C -ATOM 495 CD GLU A 62 15.237 32.417 10.590 1.00 5.70 C -ANISOU 495 CD GLU A 62 814 733 618 51 -57 -64 C -ATOM 496 OE1 GLU A 62 14.869 33.378 11.324 1.00 6.19 O -ANISOU 496 OE1 GLU A 62 682 823 845 -2 -26 -204 O -ATOM 497 OE2 GLU A 62 16.419 31.995 10.591 1.00 6.59 O -ANISOU 497 OE2 GLU A 62 838 873 793 130 -31 -121 O -ATOM 498 N LEU A 63 9.760 33.139 8.854 1.00 6.70 N -ANISOU 498 N LEU A 63 1267 648 629 -66 -200 171 N -ATOM 499 CA LEU A 63 8.320 33.250 8.990 1.00 6.67 C -ANISOU 499 CA LEU A 63 1238 665 633 125 20 134 C -ATOM 500 C LEU A 63 7.622 32.396 7.947 1.00 6.02 C -ANISOU 500 C LEU A 63 943 566 777 162 119 153 C -ATOM 501 O LEU A 63 6.679 31.680 8.263 1.00 6.69 O -ANISOU 501 O LEU A 63 909 708 925 206 204 155 O -ATOM 502 CB LEU A 63 7.837 34.701 8.886 1.00 7.36 C -ANISOU 502 CB LEU A 63 1334 630 831 103 213 35 C -ATOM 503 CG LEU A 63 8.273 35.634 10.004 1.00 6.89 C -ANISOU 503 CG LEU A 63 939 733 945 39 -38 -12 C -ATOM 504 CD1 LEU A 63 7.846 37.057 9.643 1.00 9.06 C -ANISOU 504 CD1 LEU A 63 1405 796 1240 288 -29 -125 C -ATOM 505 CD2 LEU A 63 7.670 35.205 11.343 1.00 7.17 C -ANISOU 505 CD2 LEU A 63 833 1080 813 275 57 -79 C -ATOM 506 N LYS A 64 8.117 32.461 6.702 1.00 5.69 N -ANISOU 506 N LYS A 64 864 636 661 0 62 81 N -ATOM 507 CA LYS A 64 7.453 31.667 5.678 1.00 5.79 C -ANISOU 507 CA LYS A 64 726 709 765 73 -61 157 C -ATOM 508 C LYS A 64 7.451 30.183 6.038 1.00 5.47 C -ANISOU 508 C LYS A 64 837 594 646 4 56 112 C -ATOM 509 O LYS A 64 6.476 29.458 5.775 1.00 5.85 O -ANISOU 509 O LYS A 64 792 740 693 36 -56 110 O -ATOM 510 CB LYS A 64 8.165 31.896 4.323 1.00 6.81 C -ANISOU 510 CB LYS A 64 1183 764 641 -72 -100 265 C -ATOM 511 CG ALYS A 64 7.430 31.114 3.245 0.54 10.08 C -ANISOU 511 CG ALYS A 64 1407 1795 628 -480 -209 346 C -ATOM 512 CG BLYS A 64 7.628 31.116 3.148 0.46 9.12 C -ANISOU 512 CG BLYS A 64 1746 913 806 -544 3 130 C -ATOM 513 CD ALYS A 64 7.842 31.696 1.895 0.54 9.28 C -ANISOU 513 CD ALYS A 64 1698 1199 631 -375 -156 240 C -ATOM 514 CD BLYS A 64 8.476 31.167 1.885 0.46 8.58 C -ANISOU 514 CD BLYS A 64 1428 967 864 245 -31 147 C -ATOM 515 CE ALYS A 64 7.057 31.047 0.765 0.54 8.29 C -ANISOU 515 CE ALYS A 64 1370 1084 696 24 -54 -55 C -ATOM 516 CE BLYS A 64 8.023 30.295 0.741 0.46 9.02 C -ANISOU 516 CE BLYS A 64 1271 1372 784 152 -122 132 C -ATOM 517 NZ ALYS A 64 5.677 31.556 0.572 0.54 8.40 N -ANISOU 517 NZ ALYS A 64 1265 1265 661 107 204 379 N -ATOM 518 NZ BLYS A 64 8.950 30.387 -0.423 0.46 18.04 N -ANISOU 518 NZ BLYS A 64 3789 1643 1424 459 1275 15 N -ATOM 519 N LEU A 65 8.535 29.706 6.626 1.00 4.93 N -ANISOU 519 N LEU A 65 741 586 546 30 5 66 N -ATOM 520 CA LEU A 65 8.675 28.305 7.007 1.00 4.84 C -ANISOU 520 CA LEU A 65 634 620 584 92 42 79 C -ATOM 521 C LEU A 65 8.413 28.053 8.479 1.00 4.78 C -ANISOU 521 C LEU A 65 688 549 578 5 33 19 C -ATOM 522 O LEU A 65 8.785 27.012 9.034 1.00 5.51 O -ANISOU 522 O LEU A 65 790 614 688 98 20 100 O -ATOM 523 CB LEU A 65 10.051 27.777 6.548 1.00 5.55 C -ANISOU 523 CB LEU A 65 663 657 788 63 127 44 C -ATOM 524 CG LEU A 65 10.235 27.839 5.033 1.00 6.51 C -ANISOU 524 CG LEU A 65 867 747 858 100 229 116 C -ATOM 525 CD1 LEU A 65 11.585 27.283 4.661 1.00 8.47 C -ANISOU 525 CD1 LEU A 65 995 1064 1157 28 454 -22 C -ATOM 526 CD2 LEU A 65 9.144 27.056 4.304 1.00 9.13 C -ANISOU 526 CD2 LEU A 65 1051 1577 840 -36 62 -218 C -ATOM 527 N PHE A 66 7.676 28.978 9.118 1.00 4.79 N -ANISOU 527 N PHE A 66 737 550 534 20 9 37 N -ATOM 528 CA PHE A 66 7.347 28.900 10.525 1.00 4.79 C -ANISOU 528 CA PHE A 66 760 556 504 28 1 32 C -ATOM 529 C PHE A 66 6.778 27.539 10.924 1.00 4.68 C -ANISOU 529 C PHE A 66 680 573 525 124 10 -14 C -ATOM 530 O PHE A 66 7.130 26.988 11.985 1.00 4.93 O -ANISOU 530 O PHE A 66 794 551 529 0 26 50 O -ATOM 531 CB PHE A 66 6.334 30.027 10.832 1.00 5.32 C -ANISOU 531 CB PHE A 66 839 518 663 78 2 44 C -ATOM 532 CG PHE A 66 5.732 30.008 12.202 1.00 5.04 C -ANISOU 532 CG PHE A 66 729 502 683 99 6 69 C -ATOM 533 CD1 PHE A 66 6.406 30.464 13.307 1.00 6.54 C -ANISOU 533 CD1 PHE A 66 827 865 793 55 -68 -136 C -ATOM 534 CD2 PHE A 66 4.422 29.535 12.381 1.00 5.58 C -ANISOU 534 CD2 PHE A 66 747 597 775 75 -45 128 C -ATOM 535 CE1 PHE A 66 5.751 30.470 14.568 1.00 7.33 C -ANISOU 535 CE1 PHE A 66 1129 972 685 95 -108 -160 C -ATOM 536 CE2 PHE A 66 3.819 29.525 13.605 1.00 6.65 C -ANISOU 536 CE2 PHE A 66 856 835 835 130 122 78 C -ATOM 537 CZ PHE A 66 4.486 29.990 14.672 1.00 7.10 C -ANISOU 537 CZ PHE A 66 1037 834 829 279 150 -39 C -ATOM 538 N LEU A 67 5.831 27.030 10.128 1.00 4.56 N -ANISOU 538 N LEU A 67 730 484 519 109 23 19 N -ATOM 539 CA LEU A 67 5.154 25.796 10.512 1.00 4.63 C -ANISOU 539 CA LEU A 67 691 539 530 58 107 14 C -ATOM 540 C LEU A 67 6.098 24.580 10.517 1.00 4.48 C -ANISOU 540 C LEU A 67 693 506 502 42 -40 -36 C -ATOM 541 O LEU A 67 5.796 23.600 11.195 1.00 4.80 O -ANISOU 541 O LEU A 67 808 479 538 50 13 26 O -ATOM 542 CB LEU A 67 3.948 25.492 9.613 1.00 4.73 C -ANISOU 542 CB LEU A 67 706 548 545 39 58 62 C -ATOM 543 CG LEU A 67 2.854 26.583 9.622 1.00 5.38 C -ANISOU 543 CG LEU A 67 715 601 730 58 13 2 C -ATOM 544 CD1 LEU A 67 1.782 26.188 8.607 1.00 6.58 C -ANISOU 544 CD1 LEU A 67 762 864 874 156 -95 30 C -ATOM 545 CD2 LEU A 67 2.259 26.772 10.990 1.00 5.78 C -ANISOU 545 CD2 LEU A 67 689 620 888 50 147 -70 C -ATOM 546 N GLN A 68 7.194 24.645 9.784 1.00 4.46 N -ANISOU 546 N GLN A 68 757 511 428 83 91 22 N -ATOM 547 CA GLN A 68 8.123 23.515 9.744 1.00 5.08 C -ANISOU 547 CA GLN A 68 923 524 484 138 92 58 C -ATOM 548 C GLN A 68 8.769 23.256 11.091 1.00 5.16 C -ANISOU 548 C GLN A 68 749 639 572 121 100 41 C -ATOM 549 O GLN A 68 9.288 22.146 11.319 1.00 6.55 O -ANISOU 549 O GLN A 68 998 737 755 238 105 136 O -ATOM 550 CB GLN A 68 9.193 23.682 8.675 1.00 5.45 C -ANISOU 550 CB GLN A 68 900 563 608 181 161 24 C -ATOM 551 CG GLN A 68 8.664 23.583 7.233 1.00 5.91 C -ANISOU 551 CG GLN A 68 1051 619 575 147 129 -33 C -ATOM 552 CD GLN A 68 9.838 23.354 6.325 1.00 6.24 C -ANISOU 552 CD GLN A 68 1117 604 648 14 170 -24 C -ATOM 553 OE1 GLN A 68 10.632 24.213 6.092 1.00 10.26 O -ANISOU 553 OE1 GLN A 68 1831 800 1269 -391 793 -326 O -ATOM 554 NE2 GLN A 68 9.954 22.128 5.821 1.00 5.59 N -ANISOU 554 NE2 GLN A 68 791 704 629 39 88 -123 N -ATOM 555 N ASN A 69 8.784 24.235 11.982 1.00 5.13 N -ANISOU 555 N ASN A 69 719 655 573 62 21 103 N -ATOM 556 CA ASN A 69 9.307 24.022 13.341 1.00 5.11 C -ANISOU 556 CA ASN A 69 689 698 554 -13 -9 118 C -ATOM 557 C ASN A 69 8.388 23.123 14.157 1.00 5.28 C -ANISOU 557 C ASN A 69 840 633 533 -19 -19 87 C -ATOM 558 O ASN A 69 8.799 22.592 15.200 1.00 7.03 O -ANISOU 558 O ASN A 69 1026 918 728 -78 -137 280 O -ATOM 559 CB ASN A 69 9.484 25.358 14.036 1.00 6.71 C -ANISOU 559 CB ASN A 69 1071 834 647 -220 -188 177 C -ATOM 560 CG ASN A 69 10.475 26.244 13.320 1.00 8.40 C -ANISOU 560 CG ASN A 69 973 1130 1087 -418 -466 446 C -ATOM 561 OD1 ASN A 69 11.674 26.019 13.440 1.00 15.12 O -ANISOU 561 OD1 ASN A 69 1025 2293 2429 -578 -664 1700 O -ATOM 562 ND2 ASN A 69 10.002 27.222 12.614 1.00 7.07 N -ANISOU 562 ND2 ASN A 69 991 819 878 -274 -227 258 N -ATOM 563 N PHE A 70 7.136 22.986 13.733 1.00 4.87 N -ANISOU 563 N PHE A 70 784 579 488 14 53 99 N -ATOM 564 CA PHE A 70 6.128 22.181 14.398 1.00 5.18 C -ANISOU 564 CA PHE A 70 777 633 559 -49 89 36 C -ATOM 565 C PHE A 70 5.932 20.848 13.711 1.00 5.62 C -ANISOU 565 C PHE A 70 803 734 597 -102 27 74 C -ATOM 566 O PHE A 70 5.636 19.848 14.365 1.00 8.34 O -ANISOU 566 O PHE A 70 1808 738 624 -402 2 112 O -ATOM 567 CB PHE A 70 4.804 22.992 14.443 1.00 5.54 C -ANISOU 567 CB PHE A 70 699 813 593 -79 21 61 C -ATOM 568 CG PHE A 70 4.971 24.281 15.245 1.00 5.17 C -ANISOU 568 CG PHE A 70 650 723 590 9 42 51 C -ATOM 569 CD1 PHE A 70 5.427 25.432 14.635 1.00 5.86 C -ANISOU 569 CD1 PHE A 70 792 774 661 98 137 79 C -ATOM 570 CD2 PHE A 70 4.742 24.310 16.605 1.00 5.67 C -ANISOU 570 CD2 PHE A 70 786 808 560 18 30 95 C -ATOM 571 CE1 PHE A 70 5.651 26.577 15.336 1.00 6.36 C -ANISOU 571 CE1 PHE A 70 761 734 920 80 58 166 C -ATOM 572 CE2 PHE A 70 4.955 25.461 17.332 1.00 5.92 C -ANISOU 572 CE2 PHE A 70 830 855 563 134 -38 -23 C -ATOM 573 CZ PHE A 70 5.427 26.611 16.699 1.00 6.37 C -ANISOU 573 CZ PHE A 70 797 751 873 65 79 -69 C -ATOM 574 N SER A 71 6.109 20.766 12.404 1.00 5.37 N -ANISOU 574 N SER A 71 901 540 597 3 72 31 N -ATOM 575 CA SER A 71 6.159 19.522 11.676 1.00 5.87 C -ANISOU 575 CA SER A 71 981 614 635 26 95 -41 C -ATOM 576 C SER A 71 6.977 19.747 10.421 1.00 5.77 C -ANISOU 576 C SER A 71 896 557 737 53 118 -16 C -ATOM 577 O SER A 71 6.622 20.646 9.669 1.00 6.04 O -ANISOU 577 O SER A 71 1047 559 690 48 157 -43 O -ATOM 578 CB SER A 71 4.769 19.027 11.291 1.00 6.84 C -ANISOU 578 CB SER A 71 1024 755 819 -115 150 -66 C -ATOM 579 OG SER A 71 4.893 17.887 10.476 1.00 9.70 O -ANISOU 579 OG SER A 71 1491 854 1340 -118 -138 -304 O -ATOM 580 N PRO A 72 7.996 18.948 10.140 1.00 5.99 N -ANISOU 580 N PRO A 72 959 629 686 59 163 21 N -ATOM 581 CA PRO A 72 8.796 19.255 8.932 1.00 6.36 C -ANISOU 581 CA PRO A 72 915 661 839 38 125 -101 C -ATOM 582 C PRO A 72 8.013 19.226 7.643 1.00 5.83 C -ANISOU 582 C PRO A 72 964 537 714 52 162 -73 C -ATOM 583 O PRO A 72 8.388 19.894 6.694 1.00 6.51 O -ANISOU 583 O PRO A 72 996 631 847 40 248 -26 O -ATOM 584 CB APRO A 72 9.880 18.197 8.981 0.56 6.82 C -ANISOU 584 CB APRO A 72 834 893 866 60 90 -95 C -ATOM 585 CB BPRO A 72 9.920 18.217 8.979 0.44 7.17 C -ANISOU 585 CB BPRO A 72 810 772 1141 41 146 115 C -ATOM 586 CG APRO A 72 9.303 17.072 9.765 0.56 7.38 C -ANISOU 586 CG APRO A 72 863 725 1216 154 172 -24 C -ATOM 587 CG BPRO A 72 10.098 17.842 10.427 0.44 7.89 C -ANISOU 587 CG BPRO A 72 823 1011 1162 -41 -62 69 C -ATOM 588 CD APRO A 72 8.460 17.747 10.858 0.56 7.94 C -ANISOU 588 CD APRO A 72 1091 821 1104 357 267 113 C -ATOM 589 CD BPRO A 72 8.642 17.860 10.902 0.44 8.73 C -ANISOU 589 CD BPRO A 72 1021 1076 1219 331 179 338 C -ATOM 590 N SER A 73 6.949 18.424 7.611 1.00 5.61 N -ANISOU 590 N SER A 73 862 512 758 60 191 -32 N -ATOM 591 CA SER A 73 6.145 18.285 6.413 1.00 6.41 C -ANISOU 591 CA SER A 73 903 677 854 77 27 -154 C -ATOM 592 C SER A 73 5.016 19.314 6.305 1.00 6.92 C -ANISOU 592 C SER A 73 1016 683 931 138 -11 -179 C -ATOM 593 O SER A 73 4.260 19.291 5.344 1.00 9.05 O -ANISOU 593 O SER A 73 1348 1029 1062 333 -237 -274 O -ATOM 594 CB SER A 73 5.551 16.881 6.324 1.00 7.71 C -ANISOU 594 CB SER A 73 1057 645 1227 102 -136 -140 C -ATOM 595 OG SER A 73 4.779 16.586 7.489 1.00 10.19 O -ANISOU 595 OG SER A 73 1501 980 1390 -324 160 -95 O -ATOM 596 N ALA A 74 4.894 20.215 7.290 1.00 6.59 N -ANISOU 596 N ALA A 74 1014 609 883 136 29 -107 N -ATOM 597 CA ALA A 74 3.879 21.262 7.191 1.00 6.95 C -ANISOU 597 CA ALA A 74 1071 622 947 181 108 -73 C -ATOM 598 C ALA A 74 4.148 22.203 6.036 1.00 6.90 C -ANISOU 598 C ALA A 74 1109 590 922 151 26 -151 C -ATOM 599 O ALA A 74 5.263 22.388 5.565 1.00 7.52 O -ANISOU 599 O ALA A 74 1082 786 988 76 33 12 O -ATOM 600 CB ALA A 74 3.903 22.092 8.474 1.00 8.36 C -ANISOU 600 CB ALA A 74 1320 933 924 433 158 -136 C -ATOM 601 N ARG A 75 3.050 22.819 5.581 1.00 6.68 N -ANISOU 601 N ARG A 75 1139 510 889 103 22 -92 N -ATOM 602 CA ARG A 75 3.158 23.721 4.443 1.00 6.85 C -ANISOU 602 CA ARG A 75 1215 612 776 98 -29 -138 C -ATOM 603 C ARG A 75 3.930 25.000 4.781 1.00 6.03 C -ANISOU 603 C ARG A 75 1105 531 654 101 13 -37 C -ATOM 604 O ARG A 75 3.954 25.465 5.919 1.00 5.96 O -ANISOU 604 O ARG A 75 1045 591 628 25 62 -37 O -ATOM 605 CB ARG A 75 1.771 24.094 3.917 1.00 6.88 C -ANISOU 605 CB ARG A 75 1177 614 823 115 -89 -153 C -ATOM 606 CG ARG A 75 0.925 24.962 4.846 1.00 6.33 C -ANISOU 606 CG ARG A 75 1149 458 799 1 -107 -85 C -ATOM 607 CD ARG A 75 -0.405 25.283 4.230 1.00 6.54 C -ANISOU 607 CD ARG A 75 1048 573 863 -36 -99 -138 C -ATOM 608 NE ARG A 75 -1.233 26.130 5.047 1.00 6.51 N -ANISOU 608 NE ARG A 75 891 624 958 -53 -95 -28 N -ATOM 609 CZ ARG A 75 -1.173 27.461 5.080 1.00 5.62 C -ANISOU 609 CZ ARG A 75 752 563 819 -25 -201 21 C -ATOM 610 NH1 ARG A 75 -0.278 28.131 4.335 1.00 6.01 N -ANISOU 610 NH1 ARG A 75 938 529 816 -31 -19 -13 N -ATOM 611 NH2 ARG A 75 -2.028 28.147 5.841 1.00 5.99 N -ANISOU 611 NH2 ARG A 75 758 550 969 -80 -15 70 N -ATOM 612 N ALA A 76 4.474 25.587 3.726 1.00 6.64 N -ANISOU 612 N ALA A 76 1237 615 671 188 60 -120 N -ATOM 613 CA ALA A 76 4.926 26.998 3.797 1.00 5.83 C -ANISOU 613 CA ALA A 76 949 639 627 110 169 27 C -ATOM 614 C ALA A 76 3.720 27.881 3.987 1.00 5.25 C -ANISOU 614 C ALA A 76 865 615 513 26 6 6 C -ATOM 615 O ALA A 76 2.637 27.628 3.458 1.00 6.11 O -ANISOU 615 O ALA A 76 1061 593 666 66 -75 -72 O -ATOM 616 CB ALA A 76 5.649 27.405 2.519 1.00 7.94 C -ANISOU 616 CB ALA A 76 1277 1036 703 272 270 138 C -ATOM 617 N LEU A 77 3.915 28.988 4.666 1.00 5.10 N -ANISOU 617 N LEU A 77 772 579 588 79 -31 8 N -ATOM 618 CA LEU A 77 2.952 30.084 4.633 1.00 5.06 C -ANISOU 618 CA LEU A 77 847 559 514 66 30 54 C -ATOM 619 C LEU A 77 2.992 30.701 3.222 1.00 5.26 C -ANISOU 619 C LEU A 77 739 670 590 86 -37 45 C -ATOM 620 O LEU A 77 4.004 30.742 2.577 1.00 6.45 O -ANISOU 620 O LEU A 77 926 809 717 113 81 150 O -ATOM 621 CB LEU A 77 3.278 31.134 5.683 1.00 5.11 C -ANISOU 621 CB LEU A 77 753 550 638 112 -22 -1 C -ATOM 622 CG LEU A 77 3.249 30.663 7.127 1.00 5.84 C -ANISOU 622 CG LEU A 77 798 771 650 211 -36 -20 C -ATOM 623 CD1 LEU A 77 3.423 31.865 8.021 1.00 7.02 C -ANISOU 623 CD1 LEU A 77 954 1006 708 180 -19 -211 C -ATOM 624 CD2 LEU A 77 2.010 29.870 7.469 1.00 6.74 C -ANISOU 624 CD2 LEU A 77 1040 731 788 105 65 89 C -ATOM 625 N THR A 78 1.794 31.187 2.799 1.00 5.26 N -ANISOU 625 N THR A 78 860 531 608 41 -80 -23 N -ATOM 626 CA THR A 78 1.781 31.908 1.547 1.00 5.61 C -ANISOU 626 CA THR A 78 892 598 641 97 -87 -14 C -ATOM 627 C THR A 78 2.535 33.231 1.723 1.00 5.66 C -ANISOU 627 C THR A 78 920 605 626 22 -73 63 C -ATOM 628 O THR A 78 2.814 33.682 2.849 1.00 5.53 O -ANISOU 628 O THR A 78 901 625 576 -26 -21 -3 O -ATOM 629 CB THR A 78 0.353 32.202 1.121 1.00 6.04 C -ANISOU 629 CB THR A 78 1033 585 678 46 -210 -13 C -ATOM 630 OG1 THR A 78 -0.224 33.127 2.067 1.00 6.19 O -ANISOU 630 OG1 THR A 78 935 620 797 104 -289 -19 O -ATOM 631 CG2 THR A 78 -0.501 30.946 0.969 1.00 7.10 C -ANISOU 631 CG2 THR A 78 1082 710 907 -72 -243 -53 C -ATOM 632 N ASP A 79 2.915 33.865 0.618 1.00 6.10 N -ANISOU 632 N ASP A 79 1125 615 578 -9 -2 -19 N -ATOM 633 CA ASP A 79 3.530 35.166 0.726 1.00 5.96 C -ANISOU 633 CA ASP A 79 990 679 595 -7 83 12 C -ATOM 634 C ASP A 79 2.622 36.150 1.450 1.00 5.72 C -ANISOU 634 C ASP A 79 1032 507 636 -22 -52 35 C -ATOM 635 O ASP A 79 3.117 36.981 2.239 1.00 6.31 O -ANISOU 635 O ASP A 79 1088 603 708 7 0 -81 O -ATOM 636 CB ASP A 79 3.868 35.704 -0.680 1.00 7.32 C -ANISOU 636 CB ASP A 79 1244 815 722 -60 164 32 C -ATOM 637 CG ASP A 79 5.009 34.948 -1.370 1.00 9.57 C -ANISOU 637 CG ASP A 79 1701 951 986 -117 506 -128 C -ATOM 638 OD1 ASP A 79 5.743 34.152 -0.708 1.00 10.26 O -ANISOU 638 OD1 ASP A 79 1567 1056 1276 83 607 -135 O -ATOM 639 OD2 ASP A 79 5.131 35.216 -2.601 1.00 12.25 O -ANISOU 639 OD2 ASP A 79 2096 1650 908 148 654 -151 O -ATOM 640 N ALA A 80 1.314 36.077 1.241 1.00 5.76 N -ANISOU 640 N ALA A 80 1051 557 580 68 -65 15 N -ATOM 641 CA ALA A 80 0.384 36.944 1.941 1.00 5.84 C -ANISOU 641 CA ALA A 80 1059 563 598 56 -94 68 C -ATOM 642 C ALA A 80 0.412 36.702 3.446 1.00 5.48 C -ANISOU 642 C ALA A 80 884 539 661 43 -106 -8 C -ATOM 643 O ALA A 80 0.456 37.646 4.243 1.00 5.56 O -ANISOU 643 O ALA A 80 921 504 685 82 -104 -9 O -ATOM 644 CB ALA A 80 -1.022 36.775 1.394 1.00 7.06 C -ANISOU 644 CB ALA A 80 1097 722 865 66 -283 80 C -ATOM 645 N GLU A 81 0.350 35.433 3.860 1.00 5.14 N -ANISOU 645 N GLU A 81 839 442 671 38 -159 20 N -ATOM 646 CA GLU A 81 0.391 35.100 5.267 1.00 5.16 C -ANISOU 646 CA GLU A 81 740 508 712 52 -96 -8 C -ATOM 647 C GLU A 81 1.712 35.551 5.900 1.00 4.79 C -ANISOU 647 C GLU A 81 828 378 615 25 -132 4 C -ATOM 648 O GLU A 81 1.728 36.058 7.015 1.00 5.39 O -ANISOU 648 O GLU A 81 750 557 741 33 -58 -69 O -ATOM 649 CB GLU A 81 0.220 33.584 5.460 1.00 5.17 C -ANISOU 649 CB GLU A 81 742 421 800 61 -112 34 C -ATOM 650 CG GLU A 81 -1.175 33.054 5.229 1.00 5.42 C -ANISOU 650 CG GLU A 81 743 534 784 35 -117 15 C -ATOM 651 CD GLU A 81 -1.231 31.523 5.086 1.00 5.04 C -ANISOU 651 CD GLU A 81 779 559 578 -8 -67 69 C -ATOM 652 OE1 GLU A 81 -0.222 30.907 4.721 1.00 5.64 O -ANISOU 652 OE1 GLU A 81 755 523 863 24 47 32 O -ATOM 653 OE2 GLU A 81 -2.347 30.960 5.286 1.00 5.90 O -ANISOU 653 OE2 GLU A 81 715 616 910 -46 -52 51 O -ATOM 654 N THR A 82 2.800 35.345 5.173 1.00 4.73 N -ANISOU 654 N THR A 82 767 460 572 65 -88 -20 N -ATOM 655 CA THR A 82 4.113 35.694 5.683 1.00 4.97 C -ANISOU 655 CA THR A 82 798 508 581 0 -70 63 C -ATOM 656 C THR A 82 4.202 37.196 5.971 1.00 4.85 C -ANISOU 656 C THR A 82 705 545 592 11 -61 -15 C -ATOM 657 O THR A 82 4.668 37.632 7.022 1.00 5.30 O -ANISOU 657 O THR A 82 768 595 650 8 -94 11 O -ATOM 658 CB THR A 82 5.201 35.276 4.678 1.00 5.53 C -ANISOU 658 CB THR A 82 777 538 788 90 -3 9 C -ATOM 659 OG1 THR A 82 5.152 33.852 4.485 1.00 6.09 O -ANISOU 659 OG1 THR A 82 936 549 829 93 -60 -73 O -ATOM 660 CG2 THR A 82 6.575 35.621 5.145 1.00 6.81 C -ANISOU 660 CG2 THR A 82 883 733 973 44 -59 -161 C -ATOM 661 N LYS A 83 3.791 37.990 4.981 1.00 5.30 N -ANISOU 661 N LYS A 83 892 485 635 15 -135 30 N -ATOM 662 CA ALYS A 83 3.858 39.423 5.149 0.62 5.85 C -ANISOU 662 CA ALYS A 83 1004 455 765 -6 -101 45 C -ATOM 663 CA BLYS A 83 3.904 39.434 5.159 0.38 5.95 C -ANISOU 663 CA BLYS A 83 1025 501 735 18 -106 66 C -ATOM 664 C LYS A 83 2.907 39.953 6.179 1.00 5.59 C -ANISOU 664 C LYS A 83 948 465 711 63 -258 69 C -ATOM 665 O LYS A 83 3.200 40.986 6.824 1.00 5.95 O -ANISOU 665 O LYS A 83 1018 496 747 -4 -189 -1 O -ATOM 666 CB ALYS A 83 3.521 40.103 3.798 0.62 9.46 C -ANISOU 666 CB ALYS A 83 2281 575 738 219 -110 58 C -ATOM 667 CB BLYS A 83 3.748 40.174 3.818 0.38 7.70 C -ANISOU 667 CB BLYS A 83 1676 470 778 -235 -119 136 C -ATOM 668 CG ALYS A 83 4.681 40.143 2.880 0.62 10.85 C -ANISOU 668 CG ALYS A 83 2469 805 848 -43 111 8 C -ATOM 669 CG BLYS A 83 4.848 40.115 2.827 0.38 11.84 C -ANISOU 669 CG BLYS A 83 2303 1268 928 62 326 117 C -ATOM 670 CD ALYS A 83 5.655 41.207 3.305 0.62 12.39 C -ANISOU 670 CD ALYS A 83 2656 1108 942 -268 -395 268 C -ATOM 671 CD BLYS A 83 6.244 40.459 3.278 0.38 18.00 C -ANISOU 671 CD BLYS A 83 2163 2364 2314 -783 864 -330 C -ATOM 672 CE ALYS A 83 6.457 41.719 2.150 0.62 12.73 C -ANISOU 672 CE ALYS A 83 1904 1674 1260 -238 -332 219 C -ATOM 673 CE BLYS A 83 6.723 41.813 2.791 0.38 15.23 C -ANISOU 673 CE BLYS A 83 1292 2520 1976 113 93 855 C -ATOM 674 NZ ALYS A 83 7.399 40.701 1.677 0.62 17.68 N -ANISOU 674 NZ ALYS A 83 3765 1981 972 681 25 284 N -ATOM 675 NZ BLYS A 83 8.171 41.866 2.496 0.38 13.00 N -ANISOU 675 NZ BLYS A 83 1241 2175 1525 194 114 1313 N -ATOM 676 N ALA A 84 1.746 39.331 6.359 1.00 5.57 N -ANISOU 676 N ALA A 84 924 474 717 72 -207 -38 N -ATOM 677 CA ALA A 84 0.849 39.738 7.385 1.00 6.10 C -ANISOU 677 CA ALA A 84 951 522 844 47 -235 -37 C -ATOM 678 C ALA A 84 1.423 39.479 8.794 1.00 5.26 C -ANISOU 678 C ALA A 84 673 551 776 12 -108 -58 C -ATOM 679 O ALA A 84 1.324 40.287 9.703 1.00 6.01 O -ANISOU 679 O ALA A 84 849 595 838 88 -145 -108 O -ATOM 680 CB ALA A 84 -0.503 39.024 7.240 1.00 6.73 C -ANISOU 680 CB ALA A 84 795 778 982 131 -230 -67 C -ATOM 681 N PHE A 85 2.066 38.308 8.942 1.00 5.19 N -ANISOU 681 N PHE A 85 741 501 728 7 -66 0 N -ATOM 682 CA PHE A 85 2.738 37.916 10.187 1.00 5.22 C -ANISOU 682 CA PHE A 85 781 510 691 70 -36 34 C -ATOM 683 C PHE A 85 3.804 38.954 10.520 1.00 4.96 C -ANISOU 683 C PHE A 85 728 557 600 130 -25 -18 C -ATOM 684 O PHE A 85 3.897 39.470 11.626 1.00 5.69 O -ANISOU 684 O PHE A 85 814 619 729 42 -67 -52 O -ATOM 685 CB PHE A 85 3.264 36.497 9.990 1.00 5.69 C -ANISOU 685 CB PHE A 85 935 512 716 89 -11 -30 C -ATOM 686 CG PHE A 85 3.712 35.722 11.179 1.00 5.09 C -ANISOU 686 CG PHE A 85 673 527 733 36 31 67 C -ATOM 687 CD1 PHE A 85 3.832 36.228 12.428 1.00 6.54 C -ANISOU 687 CD1 PHE A 85 1118 632 734 146 102 50 C -ATOM 688 CD2 PHE A 85 3.957 34.349 10.987 1.00 5.71 C -ANISOU 688 CD2 PHE A 85 703 595 873 90 -76 28 C -ATOM 689 CE1 PHE A 85 4.208 35.371 13.494 1.00 7.72 C -ANISOU 689 CE1 PHE A 85 1402 940 590 345 97 190 C -ATOM 690 CE2 PHE A 85 4.360 33.553 12.030 1.00 6.47 C -ANISOU 690 CE2 PHE A 85 806 632 1019 203 3 140 C -ATOM 691 CZ PHE A 85 4.495 34.058 13.288 1.00 6.68 C -ANISOU 691 CZ PHE A 85 903 827 809 141 61 228 C -ATOM 692 N LEU A 86 4.645 39.264 9.506 1.00 5.28 N -ANISOU 692 N LEU A 86 734 598 672 26 -45 -58 N -ATOM 693 CA LEU A 86 5.712 40.252 9.702 1.00 5.78 C -ANISOU 693 CA LEU A 86 716 713 766 10 -81 -70 C -ATOM 694 C LEU A 86 5.139 41.594 10.113 1.00 5.48 C -ANISOU 694 C LEU A 86 736 642 703 -93 -100 -73 C -ATOM 695 O LEU A 86 5.608 42.218 11.076 1.00 6.66 O -ANISOU 695 O LEU A 86 857 822 852 -104 -103 -177 O -ATOM 696 CB LEU A 86 6.522 40.391 8.402 1.00 6.02 C -ANISOU 696 CB LEU A 86 698 703 885 47 29 9 C -ATOM 697 CG LEU A 86 7.645 41.433 8.498 1.00 7.05 C -ANISOU 697 CG LEU A 86 800 950 930 -105 35 -41 C -ATOM 698 CD1 LEU A 86 8.689 41.066 9.532 1.00 8.30 C -ANISOU 698 CD1 LEU A 86 750 1226 1177 -90 -70 31 C -ATOM 699 CD2 LEU A 86 8.256 41.655 7.134 1.00 9.52 C -ANISOU 699 CD2 LEU A 86 1146 1314 1157 -202 290 -12 C -ATOM 700 N ALA A 87 4.134 42.099 9.387 1.00 5.76 N -ANISOU 700 N ALA A 87 790 585 814 -24 -1 -134 N -ATOM 701 CA ALA A 87 3.633 43.442 9.673 1.00 6.33 C -ANISOU 701 CA ALA A 87 976 536 893 -72 -81 -23 C -ATOM 702 C ALA A 87 3.035 43.540 11.054 1.00 6.35 C -ANISOU 702 C ALA A 87 867 632 914 -71 -23 -206 C -ATOM 703 O ALA A 87 3.165 44.585 11.713 1.00 8.29 O -ANISOU 703 O ALA A 87 1229 679 1242 -168 128 -295 O -ATOM 704 CB ALA A 87 2.599 43.843 8.634 1.00 7.18 C -ANISOU 704 CB ALA A 87 1214 554 960 73 -142 6 C -ATOM 705 N ASP A 88 2.357 42.477 11.486 1.00 6.03 N -ANISOU 705 N ASP A 88 754 654 881 -41 -2 -167 N -ATOM 706 CA ASP A 88 1.768 42.529 12.820 1.00 7.01 C -ANISOU 706 CA ASP A 88 904 722 1039 -14 150 -249 C -ATOM 707 C ASP A 88 2.797 42.538 13.915 1.00 7.24 C -ANISOU 707 C ASP A 88 1029 817 907 -205 197 -272 C -ATOM 708 O ASP A 88 2.568 43.194 14.909 1.00 11.26 O -ANISOU 708 O ASP A 88 1748 1397 1132 -116 241 -487 O -ATOM 709 CB ASP A 88 0.838 41.318 12.967 1.00 7.40 C -ANISOU 709 CB ASP A 88 763 835 1216 -6 107 -81 C -ATOM 710 CG ASP A 88 0.054 41.419 14.228 1.00 12.74 C -ANISOU 710 CG ASP A 88 2087 801 1951 -98 1042 -12 C -ATOM 711 OD1 ASP A 88 -0.743 42.373 14.417 1.00 13.81 O -ANISOU 711 OD1 ASP A 88 1473 1922 1854 280 427 -476 O -ATOM 712 OD2 ASP A 88 0.162 40.524 15.032 1.00 22.67 O -ANISOU 712 OD2 ASP A 88 5008 1117 2490 676 2398 309 O -ATOM 713 N GLY A 89 3.905 41.792 13.723 1.00 7.00 N -ANISOU 713 N GLY A 89 1012 970 678 -264 7 -177 N -ATOM 714 CA GLY A 89 4.878 41.656 14.770 1.00 8.18 C -ANISOU 714 CA GLY A 89 1177 1131 799 -385 -92 32 C -ATOM 715 C GLY A 89 5.985 42.656 14.774 1.00 6.80 C -ANISOU 715 C GLY A 89 988 912 682 -133 -19 -90 C -ATOM 716 O GLY A 89 6.642 42.866 15.824 1.00 6.67 O -ANISOU 716 O GLY A 89 919 869 746 -18 -99 -69 O -ATOM 717 N ASP A 90 6.284 43.276 13.653 1.00 6.64 N -ANISOU 717 N ASP A 90 876 865 782 -169 -81 -36 N -ATOM 718 CA ASP A 90 7.492 44.090 13.495 1.00 5.78 C -ANISOU 718 CA ASP A 90 736 711 748 -30 -71 42 C -ATOM 719 C ASP A 90 7.242 45.523 13.985 1.00 6.16 C -ANISOU 719 C ASP A 90 711 742 887 29 -183 15 C -ATOM 720 O ASP A 90 7.125 46.492 13.242 1.00 7.37 O -ANISOU 720 O ASP A 90 990 766 1042 125 -166 76 O -ATOM 721 CB ASP A 90 7.964 44.088 12.060 1.00 6.11 C -ANISOU 721 CB ASP A 90 854 698 770 -77 -120 39 C -ATOM 722 CG ASP A 90 9.241 44.862 11.862 1.00 5.88 C -ANISOU 722 CG ASP A 90 679 747 809 56 -134 61 C -ATOM 723 OD1 ASP A 90 9.950 45.096 12.874 1.00 6.49 O -ANISOU 723 OD1 ASP A 90 749 766 950 61 -175 128 O -ATOM 724 OD2 ASP A 90 9.526 45.234 10.708 1.00 7.19 O -ANISOU 724 OD2 ASP A 90 773 1008 951 -39 -131 133 O -ATOM 725 N LYS A 91 7.115 45.639 15.313 1.00 6.56 N -ANISOU 725 N LYS A 91 952 709 831 140 -57 -55 N -ATOM 726 CA ALYS A 91 6.816 46.897 15.992 0.50 7.23 C -ANISOU 726 CA ALYS A 91 1081 826 840 270 -121 -32 C -ATOM 727 CA BLYS A 91 6.757 46.943 15.871 0.50 8.71 C -ANISOU 727 CA BLYS A 91 1074 844 1393 305 67 -211 C -ATOM 728 C LYS A 91 7.893 47.939 15.862 1.00 7.40 C -ANISOU 728 C LYS A 91 1173 680 959 223 -174 -76 C -ATOM 729 O LYS A 91 7.592 49.106 16.076 1.00 8.58 O -ANISOU 729 O LYS A 91 1395 817 1047 308 -85 -108 O -ATOM 730 CB ALYS A 91 6.452 46.596 17.461 0.50 10.35 C -ANISOU 730 CB ALYS A 91 2026 1064 844 64 157 -78 C -ATOM 731 CB BLYS A 91 6.166 46.675 17.266 0.50 10.01 C -ANISOU 731 CB BLYS A 91 1252 928 1623 434 474 -134 C -ATOM 732 CG ALYS A 91 5.068 45.977 17.634 0.50 11.88 C -ANISOU 732 CG ALYS A 91 2259 821 1433 -110 518 8 C -ATOM 733 CG BLYS A 91 4.828 45.958 17.228 0.50 11.27 C -ANISOU 733 CG BLYS A 91 1380 1422 1479 259 561 -708 C -ATOM 734 CD ALYS A 91 4.146 46.070 16.419 0.50 19.64 C -ANISOU 734 CD ALYS A 91 2284 2602 2575 151 -312 -1279 C -ATOM 735 CD BLYS A 91 3.683 46.574 16.421 0.50 14.81 C -ANISOU 735 CD BLYS A 91 1306 1947 2372 596 242 -1028 C -ATOM 736 CE ALYS A 91 2.755 45.458 16.542 0.50 19.51 C -ANISOU 736 CE ALYS A 91 2230 2297 2888 466 -22 -611 C -ATOM 737 CE BLYS A 91 2.348 45.781 16.590 0.50 14.32 C -ANISOU 737 CE BLYS A 91 1266 2417 1758 701 618 -646 C -ATOM 738 NZ ALYS A 91 2.171 45.953 17.819 0.50 20.12 N -ANISOU 738 NZ ALYS A 91 2196 2709 2741 1446 -264 -278 N -ATOM 739 NZ BLYS A 91 1.288 46.509 15.811 0.50 12.25 N -ANISOU 739 NZ BLYS A 91 1355 2073 1228 -153 414 -338 N -ATOM 740 N ASP A 92 9.142 47.569 15.574 1.00 7.96 N -ANISOU 740 N ASP A 92 1061 708 1255 176 -292 -158 N -ATOM 741 CA ASP A 92 10.207 48.551 15.415 1.00 8.64 C -ANISOU 741 CA ASP A 92 1047 799 1439 54 -375 -188 C -ATOM 742 C ASP A 92 10.563 48.774 13.956 1.00 9.47 C -ANISOU 742 C ASP A 92 1161 769 1669 -14 -325 123 C -ATOM 743 O ASP A 92 11.394 49.664 13.657 1.00 12.51 O -ANISOU 743 O ASP A 92 1659 951 2144 -266 -191 202 O -ATOM 744 CB ASP A 92 11.436 48.235 16.260 1.00 9.68 C -ANISOU 744 CB ASP A 92 1184 1063 1431 3 -351 -352 C -ATOM 745 CG ASP A 92 12.183 47.011 15.931 1.00 10.36 C -ANISOU 745 CG ASP A 92 1092 1126 1719 192 -628 -400 C -ATOM 746 OD1 ASP A 92 11.980 46.421 14.863 1.00 7.93 O -ANISOU 746 OD1 ASP A 92 721 911 1381 -77 -123 -68 O -ATOM 747 OD2 ASP A 92 13.075 46.669 16.772 1.00 15.53 O -ANISOU 747 OD2 ASP A 92 1895 2021 1984 702 -1008 -477 O -ATOM 748 N GLY A 93 9.942 48.099 13.014 1.00 8.64 N -ANISOU 748 N GLY A 93 1169 775 1339 82 -120 180 N -ATOM 749 CA GLY A 93 10.092 48.437 11.632 1.00 9.55 C -ANISOU 749 CA GLY A 93 1230 942 1457 266 -34 250 C -ATOM 750 C GLY A 93 11.350 48.035 10.922 1.00 11.29 C -ANISOU 750 C GLY A 93 1603 1086 1600 356 258 594 C -ATOM 751 O GLY A 93 11.576 48.504 9.822 1.00 20.04 O -ANISOU 751 O GLY A 93 3239 2359 2017 1666 1168 1292 O -ATOM 752 N ASP A 94 12.170 47.172 11.523 1.00 8.29 N -ANISOU 752 N ASP A 94 1045 802 1302 21 -73 249 N -ATOM 753 CA ASP A 94 13.413 46.765 10.927 1.00 9.04 C -ANISOU 753 CA ASP A 94 1014 1094 1325 -196 79 364 C -ATOM 754 C ASP A 94 13.294 45.609 9.941 1.00 8.58 C -ANISOU 754 C ASP A 94 984 1038 1239 -15 68 344 C -ATOM 755 O ASP A 94 14.288 45.146 9.394 1.00 10.44 O -ANISOU 755 O ASP A 94 1017 1607 1344 -135 187 216 O -ATOM 756 CB ASP A 94 14.515 46.439 11.961 1.00 9.30 C -ANISOU 756 CB ASP A 94 834 1109 1590 -184 7 189 C -ATOM 757 CG ASP A 94 14.219 45.201 12.768 1.00 7.80 C -ANISOU 757 CG ASP A 94 723 1043 1195 -31 -84 1 C -ATOM 758 OD1 ASP A 94 13.083 44.624 12.591 1.00 6.81 O -ANISOU 758 OD1 ASP A 94 651 886 1049 -48 -49 139 O -ATOM 759 OD2 ASP A 94 15.083 44.777 13.546 1.00 8.30 O -ANISOU 759 OD2 ASP A 94 655 1188 1312 52 -99 134 O -ATOM 760 N GLY A 95 12.083 45.147 9.660 1.00 7.59 N -ANISOU 760 N GLY A 95 896 1028 960 124 -15 340 N -ATOM 761 CA GLY A 95 11.880 44.113 8.669 1.00 7.59 C -ANISOU 761 CA GLY A 95 959 1132 791 56 56 286 C -ATOM 762 C GLY A 95 12.059 42.691 9.183 1.00 6.69 C -ANISOU 762 C GLY A 95 717 1059 766 57 -8 166 C -ATOM 763 O GLY A 95 12.008 41.757 8.398 1.00 7.42 O -ANISOU 763 O GLY A 95 929 1104 787 -12 23 93 O -ATOM 764 N MET A 96 12.212 42.549 10.495 1.00 6.24 N -ANISOU 764 N MET A 96 764 859 747 14 -19 137 N -ATOM 765 CA AMET A 96 12.496 41.285 11.151 0.64 6.15 C -ANISOU 765 CA AMET A 96 813 832 690 -73 0 185 C -ATOM 766 CA BMET A 96 12.345 41.200 11.067 0.36 6.11 C -ANISOU 766 CA BMET A 96 673 845 806 76 18 176 C -ATOM 767 C MET A 96 11.762 41.222 12.470 1.00 5.44 C -ANISOU 767 C MET A 96 576 760 731 -22 -27 48 C -ATOM 768 O MET A 96 11.263 42.269 12.948 1.00 6.19 O -ANISOU 768 O MET A 96 795 765 791 45 -38 30 O -ATOM 769 CB AMET A 96 13.995 41.087 11.426 0.64 9.52 C -ANISOU 769 CB AMET A 96 991 1425 1202 612 477 778 C -ATOM 770 CB BMET A 96 13.793 40.735 10.898 0.36 7.44 C -ANISOU 770 CB BMET A 96 836 1206 787 195 142 188 C -ATOM 771 CG AMET A 96 14.915 41.313 10.294 0.64 7.61 C -ANISOU 771 CG AMET A 96 748 1181 964 -38 114 241 C -ATOM 772 CG BMET A 96 14.797 41.691 11.545 0.36 8.59 C -ANISOU 772 CG BMET A 96 804 1502 958 -276 -140 851 C -ATOM 773 SD AMET A 96 16.626 41.076 10.772 0.64 8.20 S -ANISOU 773 SD AMET A 96 733 923 1458 -108 -219 242 S -ATOM 774 SD BMET A 96 16.471 41.410 10.941 0.36 12.94 S -ANISOU 774 SD BMET A 96 902 1431 2584 -8 -162 427 S -ATOM 775 CE AMET A 96 17.084 42.551 11.642 0.64 8.69 C -ANISOU 775 CE AMET A 96 838 797 1665 -167 260 136 C -ATOM 776 CE BMET A 96 17.315 42.823 11.675 0.36 15.09 C -ANISOU 776 CE BMET A 96 1399 1704 2630 -964 131 893 C -ATOM 777 N ILE A 97 11.733 40.058 13.096 1.00 5.69 N -ANISOU 777 N ILE A 97 793 662 707 69 16 29 N -ATOM 778 CA AILE A 97 11.135 39.972 14.431 0.38 5.93 C -ANISOU 778 CA AILE A 97 722 860 672 148 27 87 C -ATOM 779 CA BILE A 97 11.105 39.903 14.411 0.62 5.34 C -ANISOU 779 CA BILE A 97 686 678 664 111 48 20 C -ATOM 780 C ILE A 97 12.180 39.534 15.434 1.00 5.29 C -ANISOU 780 C ILE A 97 657 734 620 82 51 1 C -ATOM 781 O ILE A 97 12.835 38.492 15.296 1.00 5.90 O -ANISOU 781 O ILE A 97 816 750 674 124 -15 8 O -ATOM 782 CB AILE A 97 9.959 38.980 14.386 0.38 7.05 C -ANISOU 782 CB AILE A 97 584 1117 976 105 10 181 C -ATOM 783 CB BILE A 97 10.004 38.807 14.375 0.62 5.81 C -ANISOU 783 CB BILE A 97 767 680 760 33 -23 50 C -ATOM 784 CG1AILE A 97 8.827 39.632 13.567 0.38 6.35 C -ANISOU 784 CG1AILE A 97 871 759 782 22 -180 6 C -ATOM 785 CG1BILE A 97 8.905 39.074 13.337 0.62 5.62 C -ANISOU 785 CG1BILE A 97 781 614 741 43 -20 -160 C -ATOM 786 CG2AILE A 97 9.468 38.540 15.741 0.38 6.11 C -ANISOU 786 CG2AILE A 97 676 681 963 284 59 175 C -ATOM 787 CG2BILE A 97 9.387 38.666 15.768 0.62 7.45 C -ANISOU 787 CG2BILE A 97 887 1152 792 -207 -14 287 C -ATOM 788 CD1AILE A 97 7.665 38.699 13.330 0.38 8.80 C -ANISOU 788 CD1AILE A 97 1000 1280 1061 -247 -439 78 C -ATOM 789 CD1BILE A 97 8.118 40.369 13.542 0.62 6.71 C -ANISOU 789 CD1BILE A 97 794 856 900 146 -232 -236 C -ATOM 790 N GLY A 98 12.354 40.365 16.453 1.00 5.63 N -ANISOU 790 N GLY A 98 789 711 638 127 82 59 N -ATOM 791 CA GLY A 98 13.281 40.058 17.536 1.00 6.12 C -ANISOU 791 CA GLY A 98 765 858 702 -54 37 16 C -ATOM 792 C GLY A 98 12.521 39.381 18.704 1.00 5.73 C -ANISOU 792 C GLY A 98 732 804 640 9 51 17 C -ATOM 793 O GLY A 98 11.300 39.242 18.701 1.00 6.08 O -ANISOU 793 O GLY A 98 704 950 656 95 53 10 O -ATOM 794 N VAL A 99 13.279 38.968 19.727 1.00 6.14 N -ANISOU 794 N VAL A 99 692 983 657 -24 -18 18 N -ATOM 795 CA VAL A 99 12.678 38.150 20.771 1.00 6.40 C -ANISOU 795 CA VAL A 99 776 1046 610 -51 -31 58 C -ATOM 796 C VAL A 99 11.573 38.873 21.493 1.00 6.41 C -ANISOU 796 C VAL A 99 749 1066 622 37 -88 61 C -ATOM 797 O VAL A 99 10.512 38.304 21.772 1.00 7.03 O -ANISOU 797 O VAL A 99 799 1071 800 -71 79 30 O -ATOM 798 CB VAL A 99 13.750 37.606 21.750 1.00 6.79 C -ANISOU 798 CB VAL A 99 768 1165 649 121 -61 -19 C -ATOM 799 CG1 VAL A 99 14.509 38.669 22.520 1.00 8.15 C -ANISOU 799 CG1 VAL A 99 992 1345 760 -15 -192 16 C -ATOM 800 CG2 VAL A 99 13.116 36.576 22.684 1.00 7.80 C -ANISOU 800 CG2 VAL A 99 983 1215 765 126 -36 186 C -ATOM 801 N ASP A 100 11.762 40.159 21.806 1.00 6.95 N -ANISOU 801 N ASP A 100 844 1105 694 -33 131 -32 N -ATOM 802 CA ASP A 100 10.736 40.893 22.533 1.00 7.44 C -ANISOU 802 CA ASP A 100 921 1198 706 33 115 -130 C -ATOM 803 C ASP A 100 9.469 41.080 21.669 1.00 7.09 C -ANISOU 803 C ASP A 100 937 1058 699 0 172 25 C -ATOM 804 O ASP A 100 8.357 41.007 22.174 1.00 7.83 O -ANISOU 804 O ASP A 100 882 1251 841 21 218 -70 O -ATOM 805 CB ASP A 100 11.266 42.243 23.034 1.00 9.46 C -ANISOU 805 CB ASP A 100 1101 1369 1122 -59 235 -506 C -ATOM 806 CG ASP A 100 12.324 42.101 24.123 1.00 11.97 C -ANISOU 806 CG ASP A 100 1600 2129 820 -548 267 -458 C -ATOM 807 OD1 ASP A 100 12.413 41.039 24.767 1.00 11.87 O -ANISOU 807 OD1 ASP A 100 1294 2239 978 -192 -14 -417 O -ATOM 808 OD2 ASP A 100 12.993 43.136 24.238 1.00 17.85 O -ANISOU 808 OD2 ASP A 100 2209 2663 1908 -1116 -331 -319 O -ATOM 809 N GLU A 101 9.653 41.304 20.377 1.00 6.76 N -ANISOU 809 N GLU A 101 818 991 760 56 150 17 N -ATOM 810 CA GLU A 101 8.527 41.415 19.460 1.00 6.54 C -ANISOU 810 CA GLU A 101 791 879 814 150 181 43 C -ATOM 811 C GLU A 101 7.774 40.099 19.370 1.00 6.58 C -ANISOU 811 C GLU A 101 670 969 859 140 170 111 C -ATOM 812 O GLU A 101 6.541 40.071 19.333 1.00 7.34 O -ANISOU 812 O GLU A 101 815 960 1015 81 149 169 O -ATOM 813 CB GLU A 101 8.970 41.825 18.056 1.00 6.18 C -ANISOU 813 CB GLU A 101 869 732 747 125 130 -53 C -ATOM 814 CG GLU A 101 9.334 43.291 17.942 1.00 6.30 C -ANISOU 814 CG GLU A 101 881 726 786 144 101 3 C -ATOM 815 CD GLU A 101 10.022 43.595 16.644 1.00 5.61 C -ANISOU 815 CD GLU A 101 664 697 771 65 -9 -78 C -ATOM 816 OE1 GLU A 101 10.671 42.734 16.048 1.00 7.73 O -ANISOU 816 OE1 GLU A 101 1242 781 915 191 328 125 O -ATOM 817 OE2 GLU A 101 9.932 44.770 16.193 1.00 7.73 O -ANISOU 817 OE2 GLU A 101 1111 729 1095 166 263 60 O -ATOM 818 N PHE A 102 8.490 38.997 19.355 1.00 6.45 N -ANISOU 818 N PHE A 102 780 853 818 66 153 110 N -ATOM 819 CA PHE A 102 7.870 37.683 19.301 1.00 6.33 C -ANISOU 819 CA PHE A 102 703 868 834 70 116 97 C -ATOM 820 C PHE A 102 7.015 37.438 20.556 1.00 6.55 C -ANISOU 820 C PHE A 102 718 963 807 132 115 119 C -ATOM 821 O PHE A 102 5.856 37.065 20.475 1.00 7.39 O -ANISOU 821 O PHE A 102 747 1046 1016 81 183 171 O -ATOM 822 CB PHE A 102 8.961 36.633 19.154 1.00 6.58 C -ANISOU 822 CB PHE A 102 705 912 885 105 37 112 C -ATOM 823 CG PHE A 102 8.505 35.213 19.048 1.00 6.62 C -ANISOU 823 CG PHE A 102 660 935 921 61 98 -4 C -ATOM 824 CD1 PHE A 102 8.080 34.662 17.845 1.00 7.73 C -ANISOU 824 CD1 PHE A 102 854 1136 948 47 29 -31 C -ATOM 825 CD2 PHE A 102 8.557 34.390 20.154 1.00 6.84 C -ANISOU 825 CD2 PHE A 102 755 918 926 134 99 112 C -ATOM 826 CE1 PHE A 102 7.760 33.297 17.768 1.00 8.93 C -ANISOU 826 CE1 PHE A 102 1045 1184 1165 -48 195 -349 C -ATOM 827 CE2 PHE A 102 8.214 33.045 20.087 1.00 8.12 C -ANISOU 827 CE2 PHE A 102 863 918 1305 129 124 205 C -ATOM 828 CZ PHE A 102 7.845 32.543 18.903 1.00 8.97 C -ANISOU 828 CZ PHE A 102 971 991 1446 -30 409 -48 C -ATOM 829 N ALA A 103 7.615 37.719 21.709 1.00 7.10 N -ANISOU 829 N ALA A 103 770 1094 835 36 104 173 N -ATOM 830 CA ALA A 103 6.870 37.544 22.939 1.00 8.38 C -ANISOU 830 CA ALA A 103 824 1537 822 33 127 329 C -ATOM 831 C ALA A 103 5.661 38.450 22.982 1.00 7.86 C -ANISOU 831 C ALA A 103 873 1398 717 -11 129 128 C -ATOM 832 O ALA A 103 4.594 38.044 23.466 1.00 8.50 O -ANISOU 832 O ALA A 103 832 1549 847 -60 149 113 O -ATOM 833 CB ALA A 103 7.779 37.768 24.141 1.00 9.77 C -ANISOU 833 CB ALA A 103 1011 1772 928 -51 28 309 C -ATOM 834 N ALA A 104 5.773 39.675 22.498 1.00 8.42 N -ANISOU 834 N ALA A 104 866 1366 969 48 252 72 N -ATOM 835 CA ALA A 104 4.671 40.643 22.527 1.00 9.17 C -ANISOU 835 CA ALA A 104 1020 1308 1157 189 291 -124 C -ATOM 836 C ALA A 104 3.483 40.159 21.714 1.00 8.44 C -ANISOU 836 C ALA A 104 940 1199 1069 259 242 67 C -ATOM 837 O ALA A 104 2.342 40.421 22.084 1.00 10.98 O -ANISOU 837 O ALA A 104 1002 1776 1392 344 212 -150 O -ATOM 838 CB ALA A 104 5.081 41.998 22.078 1.00 10.27 C -ANISOU 838 CB ALA A 104 1289 1298 1317 160 328 -35 C -ATOM 839 N MET A 105 3.712 39.477 20.576 1.00 8.06 N -ANISOU 839 N MET A 105 1055 1132 875 368 189 224 N -ATOM 840 CA AMET A 105 2.620 38.983 19.770 0.67 9.11 C -ANISOU 840 CA AMET A 105 1069 1549 844 641 -11 92 C -ATOM 841 CA BMET A 105 2.617 38.980 19.753 0.33 10.14 C -ANISOU 841 CA BMET A 105 1339 1752 761 414 -52 211 C -ATOM 842 C MET A 105 1.863 37.849 20.484 1.00 8.62 C -ANISOU 842 C MET A 105 1143 1245 886 365 -235 -66 C -ATOM 843 O MET A 105 0.676 37.668 20.283 1.00 12.94 O -ANISOU 843 O MET A 105 1360 1389 2169 178 -772 111 O -ATOM 844 CB AMET A 105 3.115 38.384 18.453 0.67 13.06 C -ANISOU 844 CB AMET A 105 1697 2730 537 551 -136 175 C -ATOM 845 CB BMET A 105 2.878 38.283 18.402 0.33 8.26 C -ANISOU 845 CB BMET A 105 1090 625 1422 -508 163 -94 C -ATOM 846 CG AMET A 105 3.360 39.287 17.323 0.67 11.23 C -ANISOU 846 CG AMET A 105 2104 1230 934 -559 56 -90 C -ATOM 847 CG BMET A 105 4.274 37.968 18.034 0.33 8.84 C -ANISOU 847 CG BMET A 105 1041 1284 1034 -344 10 -283 C -ATOM 848 SD AMET A 105 3.792 38.492 15.786 0.67 10.24 S -ANISOU 848 SD AMET A 105 1501 1536 854 -654 23 -143 S -ATOM 849 SD BMET A 105 4.926 38.233 16.372 0.33 8.93 S -ANISOU 849 SD BMET A 105 1220 1119 1054 -142 104 -274 S -ATOM 850 CE AMET A 105 5.419 37.807 16.156 0.67 12.20 C -ANISOU 850 CE AMET A 105 1715 1991 928 -393 -29 80 C -ATOM 851 CE BMET A 105 3.402 38.489 15.421 0.33 18.29 C -ANISOU 851 CE BMET A 105 2450 3349 1149 1438 -656 -1155 C -ATOM 852 N ILE A 106 2.592 37.086 21.239 1.00 8.50 N -ANISOU 852 N ILE A 106 887 1275 1067 246 -209 38 N -ATOM 853 CA ILE A 106 2.062 35.882 21.863 1.00 8.14 C -ANISOU 853 CA ILE A 106 833 1098 1160 88 -173 -88 C -ATOM 854 C ILE A 106 1.383 36.162 23.176 1.00 7.78 C -ANISOU 854 C ILE A 106 862 929 1165 148 -81 -95 C -ATOM 855 O ILE A 106 0.395 35.494 23.510 1.00 9.36 O -ANISOU 855 O ILE A 106 815 1117 1626 -51 2 -79 O -ATOM 856 CB ILE A 106 3.215 34.854 22.047 1.00 7.60 C -ANISOU 856 CB ILE A 106 775 968 1145 67 -182 -205 C -ATOM 857 CG1 ILE A 106 3.626 34.400 20.662 1.00 8.85 C -ANISOU 857 CG1 ILE A 106 879 1293 1190 88 -268 -407 C -ATOM 858 CG2 ILE A 106 2.843 33.713 22.930 1.00 8.21 C -ANISOU 858 CG2 ILE A 106 800 892 1429 95 -14 -127 C -ATOM 859 CD1 ILE A 106 4.981 33.670 20.597 1.00 9.45 C -ANISOU 859 CD1 ILE A 106 937 1504 1151 101 -121 -409 C -ATOM 860 N LYS A 107 1.959 37.083 23.925 1.00 7.78 N -ANISOU 860 N LYS A 107 835 1125 995 -38 172 -63 N -ATOM 861 CA LYS A 107 1.468 37.427 25.265 1.00 7.84 C -ANISOU 861 CA LYS A 107 821 1219 940 119 157 -136 C -ATOM 862 C LYS A 107 0.575 38.689 25.292 1.00 8.04 C -ANISOU 862 C LYS A 107 1053 1210 793 127 32 -127 C -ATOM 863 O LYS A 107 0.216 39.106 26.328 1.00 13.30 O -ANISOU 863 O LYS A 107 2038 1874 1142 828 458 -4 O -ATOM 864 CB LYS A 107 2.675 37.474 26.184 1.00 9.45 C -ANISOU 864 CB LYS A 107 1177 1432 980 355 142 -61 C -ATOM 865 CG LYS A 107 3.471 36.175 26.330 1.00 9.76 C -ANISOU 865 CG LYS A 107 1183 1637 890 366 0 35 C -ATOM 866 CD LYS A 107 2.680 34.975 26.794 1.00 19.51 C -ANISOU 866 CD LYS A 107 3066 1796 2552 970 1576 1117 C -ATOM 867 CE ALYS A 107 1.959 35.187 28.071 0.53 18.08 C -ANISOU 867 CE ALYS A 107 2061 1725 3083 1113 1619 819 C -ATOM 868 CE BLYS A 107 2.151 35.140 28.200 0.47 20.84 C -ANISOU 868 CE BLYS A 107 3980 2155 1782 711 804 1440 C -ATOM 869 NZ ALYS A 107 1.479 33.920 28.697 0.53 9.17 N -ANISOU 869 NZ ALYS A 107 1385 1433 665 322 -14 -11 N -ATOM 870 NZ BLYS A 107 3.276 35.064 29.180 0.47 23.81 N -ANISOU 870 NZ BLYS A 107 3199 2463 3386 1301 371 -1926 N -ATOM 871 N ALA A 108 0.166 39.151 24.125 1.00 10.08 N -ANISOU 871 N ALA A 108 1264 1577 987 285 -13 -109 N -ATOM 872 CA ALA A 108 -0.696 40.304 24.011 1.00 10.56 C -ANISOU 872 CA ALA A 108 1092 1517 1403 244 -65 -160 C -ATOM 873 C ALA A 108 -1.929 40.222 24.914 1.00 9.40 C -ANISOU 873 C ALA A 108 1119 1264 1190 220 -68 -52 C -ATOM 874 O ALA A 108 -2.327 41.299 25.441 1.00 11.25 O -ANISOU 874 O ALA A 108 1390 1417 1469 172 334 -8 O -ATOM 875 CB ALA A 108 -1.122 40.462 22.528 1.00 11.69 C -ANISOU 875 CB ALA A 108 981 2065 1395 288 114 131 C -ATOM 876 OXT ALA A 108 -2.534 39.147 24.987 1.00 12.46 O -ANISOU 876 OXT ALA A 108 1306 1501 1928 34 118 -405 O -TER 877 ALA A 108 -HETATM 878 CA CA A 110 17.153 34.014 11.880 1.00 5.67 CA -ANISOU 878 CA CA A 110 574 856 725 25 32 -19 CA -HETATM 879 CA CA A 111 11.520 44.191 14.302 1.00 5.60 CA -ANISOU 879 CA CA A 111 598 718 812 31 -92 60 CA -HETATM 880 N NH4 A 200 17.205 34.073 7.423 1.00 8.52 N -ANISOU 880 N NH4 A 200 1107 1304 826 400 173 -15 N -HETATM 881 C FMT A 150 0.543 36.728 30.783 1.00 8.35 C -ANISOU 881 C FMT A 150 1255 876 1042 93 13 14 C -HETATM 882 O1 FMT A 150 -0.031 37.145 32.124 1.00 13.52 O -ANISOU 882 O1 FMT A 150 2045 1752 1339 294 162 -19 O -HETATM 883 O2 FMT A 150 1.508 37.792 30.198 1.00 13.59 O -ANISOU 883 O2 FMT A 150 1938 1420 1804 60 317 108 O -HETATM 884 C FMT A 151 0.767 33.924 -2.279 1.00 8.67 C -ANISOU 884 C FMT A 151 1631 1083 582 196 -46 72 C -HETATM 885 O1 FMT A 151 2.218 33.182 -2.070 1.00 11.53 O -ANISOU 885 O1 FMT A 151 1742 1480 1160 83 -34 -25 O -HETATM 886 O2 FMT A 151 0.268 34.803 -1.195 1.00 9.62 O -ANISOU 886 O2 FMT A 151 1770 1019 866 192 -343 -22 O -HETATM 887 O HOH A 201 13.527 43.258 15.138 1.00 8.43 O -ANISOU 887 O HOH A 201 665 1274 1264 118 -173 242 O -HETATM 888 O HOH A 202 5.424 27.358 7.374 1.00 5.75 O -ANISOU 888 O HOH A 202 903 738 544 -101 -1 73 O -HETATM 889 O HOH A 203 5.494 42.448 18.329 1.00 7.26 O -ANISOU 889 O HOH A 203 923 909 928 169 97 -27 O -HETATM 890 O HOH A 204 11.508 29.242 11.126 1.00 6.65 O -ANISOU 890 O HOH A 204 856 780 889 -101 -110 259 O -HETATM 891 O HOH A 205 -1.000 39.908 3.441 1.00 7.27 O -ANISOU 891 O HOH A 205 1210 696 855 260 -140 42 O -HETATM 892 O HOH A 206 -11.408 32.786 13.184 1.00 8.37 O -ANISOU 892 O HOH A 206 851 1210 1121 142 -212 -131 O -HETATM 893 O HOH A 207 1.395 15.133 16.638 1.00 8.25 O -ANISOU 893 O HOH A 207 1535 760 839 -359 -82 -63 O -HETATM 894 O HOH A 208 -9.351 35.761 15.188 1.00 8.74 O -ANISOU 894 O HOH A 208 950 1271 1098 220 -130 -148 O -HETATM 895 O HOH A 209 4.514 18.955 21.061 1.00 10.07 O -ANISOU 895 O HOH A 209 1373 1457 996 -603 236 -257 O -HETATM 896 O HOH A 210 7.925 45.135 8.520 1.00 9.61 O -ANISOU 896 O HOH A 210 1358 1155 1138 339 -413 -58 O -HETATM 897 O HOH A 211 -1.154 23.529 8.235 1.00 9.80 O -ANISOU 897 O HOH A 211 1253 1073 1397 30 58 32 O -HETATM 898 O HOH A 212 17.352 31.209 8.158 1.00 10.59 O -ANISOU 898 O HOH A 212 1692 1264 1067 601 193 -108 O -HETATM 899 O HOH A 213 12.280 42.673 19.507 1.00 10.45 O -ANISOU 899 O HOH A 213 974 1565 1432 189 138 78 O -HETATM 900 O HOH A 214 -4.135 29.554 12.053 1.00 8.46 O -ANISOU 900 O HOH A 214 1230 892 1093 -56 154 94 O -HETATM 901 O HOH A 215 -6.746 29.397 13.032 1.00 10.76 O -ANISOU 901 O HOH A 215 1260 1267 1562 264 87 -152 O -HETATM 902 O HOH A 216 0.209 22.680 24.105 1.00 9.00 O -ANISOU 902 O HOH A 216 1401 1079 941 375 -91 -27 O -HETATM 903 O HOH A 217 -1.808 18.145 11.920 1.00 8.11 O -ANISOU 903 O HOH A 217 1464 732 885 -213 -185 -31 O -HETATM 904 O HOH A 218 -7.791 25.659 7.093 1.00 8.19 O -ANISOU 904 O HOH A 218 1036 1092 984 -46 -152 -98 O -HETATM 905 O HOH A 219 -3.807 27.369 13.969 1.00 10.44 O -ANISOU 905 O HOH A 219 1455 828 1684 -137 -545 28 O -HETATM 906 O HOH A 220 9.913 20.122 13.134 1.00 10.19 O -ANISOU 906 O HOH A 220 1594 992 1285 220 -49 326 O -HETATM 907 O HOH A 221 18.313 31.502 17.908 1.00 10.50 O -ANISOU 907 O HOH A 221 1050 1801 1139 -25 76 4 O -HETATM 908 O HOH A 222 -2.404 29.129 24.492 1.00 10.82 O -ANISOU 908 O HOH A 222 1712 1262 1139 -69 -106 -11 O -HETATM 909 O HOH A 223 0.828 39.176 -0.819 1.00 10.92 O -ANISOU 909 O HOH A 223 1817 974 1360 277 340 58 O -HETATM 910 O HOH A 224 13.418 39.620 7.306 1.00 10.31 O -ANISOU 910 O HOH A 224 1803 863 1250 -268 -30 2 O -HETATM 911 O HOH A 225 5.246 50.214 16.984 1.00 13.38 O -ANISOU 911 O HOH A 225 2379 1699 1004 1189 386 344 O -HETATM 912 O HOH A 226 0.584 39.926 28.952 1.00 14.52 O -ANISOU 912 O HOH A 226 2844 1400 1273 638 -360 -522 O -HETATM 913 O HOH A 227 -7.070 29.236 17.734 1.00 13.69 O -ANISOU 913 O HOH A 227 1052 1215 2936 67 191 -209 O -HETATM 914 O HOH A 228 12.573 25.303 7.625 1.00 11.48 O -ANISOU 914 O HOH A 228 1054 1708 1600 158 -72 302 O -HETATM 915 O HOH A 229 -6.083 33.746 7.574 1.00 10.90 O -ANISOU 915 O HOH A 229 1667 1324 1150 316 -70 -98 O -HETATM 916 O HOH A 230 0.453 21.951 6.657 1.00 15.47 O -ANISOU 916 O HOH A 230 2289 942 2646 158 864 455 O -HETATM 917 O HOH A 231 13.818 44.094 17.677 1.00 11.85 O -ANISOU 917 O HOH A 231 1206 2138 1160 -233 -254 307 O -HETATM 918 O HOH A 232 14.305 36.504 4.657 1.00 15.35 O -ANISOU 918 O HOH A 232 1673 2523 1635 -346 171 613 O -HETATM 919 O HOH A 233 17.175 46.165 14.493 1.00 17.56 O -ANISOU 919 O HOH A 233 1447 1227 3997 -150 -1246 -113 O -HETATM 920 O HOH A 234 0.645 25.960 27.349 1.00 17.75 O -ANISOU 920 O HOH A 234 4009 1573 1161 -169 -52 315 O -HETATM 921 O HOH A 235 5.197 28.190 31.035 1.00 11.48 O -ANISOU 921 O HOH A 235 1657 1428 1277 196 -170 201 O -HETATM 922 O HOH A 236 2.239 17.362 10.017 1.00 13.30 O -ANISOU 922 O HOH A 236 1563 2195 1295 -672 -322 116 O -HETATM 923 O HOH A 237 -3.318 36.426 13.650 1.00 14.93 O -ANISOU 923 O HOH A 237 1794 1593 2287 825 -379 63 O -HETATM 924 O HOH A 238 -2.885 40.665 27.996 1.00 13.91 O -ANISOU 924 O HOH A 238 2982 1373 929 -659 4 -281 O -HETATM 925 O HOH A 239 20.295 35.792 8.779 1.00 14.03 O -ANISOU 925 O HOH A 239 1378 1890 2062 63 -61 245 O -HETATM 926 O HOH A 240 -6.414 27.667 15.300 1.00 13.05 O -ANISOU 926 O HOH A 240 2112 1356 1490 270 -330 -321 O -HETATM 927 O HOH A 241 17.882 37.894 21.224 1.00 13.52 O -ANISOU 927 O HOH A 241 1660 2180 1297 -438 -258 363 O -HETATM 928 O HOH A 242 -8.844 23.821 8.850 1.00 13.56 O -ANISOU 928 O HOH A 242 1238 1725 2189 -254 -375 713 O -HETATM 929 O HOH A 243 17.389 24.628 10.092 1.00 15.65 O -ANISOU 929 O HOH A 243 3223 1010 1714 317 743 136 O -HETATM 930 O HOH A 244 7.886 41.287 24.837 1.00 21.56 O -ANISOU 930 O HOH A 244 1592 5326 1273 -527 271 -710 O -HETATM 931 O HOH A 245 4.462 24.075 1.216 1.00 19.37 O -ANISOU 931 O HOH A 245 3928 2359 1072 699 -22 -774 O -HETATM 932 O HOH A 246 -0.208 35.432 9.130 1.00 13.38 O -ANISOU 932 O HOH A 246 1589 1358 2138 -59 201 459 O -HETATM 933 O HOH A 247 11.928 30.396 3.259 1.00 14.56 O -ANISOU 933 O HOH A 247 1876 1929 1729 -402 -296 102 O -HETATM 934 O HOH A 248 0.792 17.241 12.292 1.00 9.51 O -ANISOU 934 O HOH A 248 1547 711 1356 -164 -295 65 O -HETATM 935 O HOH A 249 8.385 33.745 -1.764 1.00 13.25 O -ANISOU 935 O HOH A 249 1389 2612 1032 241 -153 -363 O -HETATM 936 O HOH A 250 0.698 23.394 26.644 1.00 18.56 O -ANISOU 936 O HOH A 250 3790 1974 1289 1017 -558 -179 O -HETATM 937 O HOH A 251 20.169 32.715 6.738 1.00 13.45 O -ANISOU 937 O HOH A 251 2080 1502 1529 750 609 205 O -HETATM 938 O HOH A 252 23.463 37.924 13.342 1.00 13.71 O -ANISOU 938 O HOH A 252 1759 1390 2060 -135 -10 -408 O -HETATM 939 O HOH A 253 14.449 40.735 26.510 1.00 15.33 O -ANISOU 939 O HOH A 253 1378 2766 1683 -203 -173 56 O -HETATM 940 O HOH A 254 8.626 18.996 15.181 1.00 19.91 O -ANISOU 940 O HOH A 254 2331 2400 2833 1143 1234 1392 O -HETATM 941 O HOH A 255 11.222 45.041 20.834 1.00 17.27 O -ANISOU 941 O HOH A 255 2808 2091 1662 -29 60 -167 O -HETATM 942 O HOH A 256 -4.998 16.758 17.908 1.00 19.13 O -ANISOU 942 O HOH A 256 2024 2208 3036 -776 -928 -152 O -HETATM 943 O HOH A 257 11.497 42.246 5.702 1.00 21.04 O -ANISOU 943 O HOH A 257 2004 4611 1379 -763 -281 1131 O -HETATM 944 O HOH A 258 15.913 36.323 25.382 1.00 18.90 O -ANISOU 944 O HOH A 258 2955 2979 1247 -430 325 104 O -HETATM 945 O HOH A 259 -4.729 31.155 24.590 1.00 20.74 O -ANISOU 945 O HOH A 259 2657 3466 1757 408 -113 -115 O -HETATM 946 O HOH A 260 2.863 43.020 18.770 1.00 18.01 O -ANISOU 946 O HOH A 260 1071 2097 3675 208 -252 -735 O -HETATM 947 O HOH A 261 -2.735 35.732 8.277 1.00 16.32 O -ANISOU 947 O HOH A 261 1968 1417 2817 -453 -592 577 O -HETATM 948 O HOH A 262 -7.081 27.343 21.991 1.00 21.05 O -ANISOU 948 O HOH A 262 1791 3640 2568 1234 263 180 O -HETATM 949 O HOH A 263 -3.015 36.500 5.563 1.00 18.80 O -ANISOU 949 O HOH A 263 2119 2243 2782 179 -192 825 O -HETATM 950 O HOH A 264 2.020 46.639 13.013 1.00 16.16 O -ANISOU 950 O HOH A 264 1895 1250 2994 -429 886 -863 O -HETATM 951 O HOH A 265 -10.045 27.165 6.409 1.00 14.97 O -ANISOU 951 O HOH A 265 1602 1903 2184 148 -427 -36 O -HETATM 952 O HOH A 266 3.329 39.247 -0.205 1.00 21.47 O -ANISOU 952 O HOH A 266 2361 811 4984 263 -1705 -220 O -HETATM 953 O HOH A 267 -2.334 36.497 24.182 1.00 18.76 O -ANISOU 953 O HOH A 267 2374 1795 2959 -545 1044 -880 O -HETATM 954 O HOH A 268 10.437 40.026 26.350 1.00 20.38 O -ANISOU 954 O HOH A 268 3749 1981 2014 126 688 342 O -HETATM 955 O HOH A 269 15.945 31.937 2.166 1.00 17.65 O -ANISOU 955 O HOH A 269 1196 3526 1984 -177 339 -781 O -HETATM 956 O HOH A 270 11.572 32.713 1.532 1.00 17.31 O -ANISOU 956 O HOH A 270 2761 1980 1835 -568 -657 396 O -HETATM 957 O HOH A 271 12.725 25.895 31.980 1.00 15.35 O -ANISOU 957 O HOH A 271 2494 1891 1449 655 404 -128 O -HETATM 958 O HOH A 272 -2.705 34.010 20.984 1.00 14.57 O -ANISOU 958 O HOH A 272 2282 1517 1739 427 10 13 O -HETATM 959 O HOH A 273 11.020 20.655 19.731 1.00 16.06 O -ANISOU 959 O HOH A 273 1238 2757 2105 145 379 576 O -HETATM 960 O HOH A 274 -3.419 39.016 4.402 1.00 16.43 O -ANISOU 960 O HOH A 274 1972 1290 2979 -50 587 -24 O -HETATM 961 O HOH A 275 11.089 22.491 16.675 1.00 20.16 O -ANISOU 961 O HOH A 275 1881 2352 3429 257 -965 -100 O -HETATM 962 O HOH A 276 -2.053 38.131 27.937 1.00 18.20 O -ANISOU 962 O HOH A 276 2677 2029 2210 -35 -28 -363 O -HETATM 963 O HOH A 277 4.150 37.670 -3.612 1.00 20.46 O -ANISOU 963 O HOH A 277 2004 3336 2434 285 165 1726 O -HETATM 964 O HOH A 278 -7.544 28.866 10.483 1.00 17.04 O -ANISOU 964 O HOH A 278 2959 1622 1894 -291 262 -49 O -HETATM 965 O HOH A 279 9.983 46.431 18.601 1.00 18.94 O -ANISOU 965 O HOH A 279 3391 1688 2118 46 -276 -531 O -HETATM 966 O HOH A 280 -3.623 37.098 10.915 1.00 19.24 O -ANISOU 966 O HOH A 280 2230 2880 2200 1033 -169 287 O -HETATM 967 O HOH A 281 10.380 24.984 24.549 1.00 20.45 O -ANISOU 967 O HOH A 281 1767 2370 3634 -346 188 -1084 O -HETATM 968 O HOH A 282 -10.006 30.643 12.105 1.00 30.64 O -ANISOU 968 O HOH A 282 2332 4208 5101 1594 -1872 -3089 O -HETATM 969 O HOH A 283 -6.445 29.112 23.927 1.00 20.43 O -ANISOU 969 O HOH A 283 2909 3011 1843 -457 377 -63 O -HETATM 970 O HOH A 284 1.552 27.365 0.997 1.00 31.63 O -ANISOU 970 O HOH A 284 6337 3980 1701 1321 -1970 -674 O -HETATM 971 O HOH A 285 8.600 26.992 24.272 1.00 24.51 O -ANISOU 971 O HOH A 285 4374 1685 3253 504 -1766 -684 O -HETATM 972 O HOH A 286 16.259 25.997 15.353 1.00 16.43 O -ANISOU 972 O HOH A 286 1592 1826 2826 481 -379 -989 O -HETATM 973 O HOH A 287 3.543 13.437 17.503 1.00 20.34 O -ANISOU 973 O HOH A 287 2458 2324 2948 904 -1382 -853 O -HETATM 974 O HOH A 288 6.519 44.555 20.048 1.00 15.63 O -ANISOU 974 O HOH A 288 2139 1737 2063 -311 746 -392 O -HETATM 975 O HOH A 289 15.546 47.848 16.317 1.00 20.80 O -ANISOU 975 O HOH A 289 2017 2932 2953 -61 -575 -297 O -HETATM 976 O HOH A 290 9.990 26.345 32.346 1.00 20.98 O -ANISOU 976 O HOH A 290 3150 2536 2287 1297 681 800 O -HETATM 977 O HOH A 291 20.230 36.669 19.972 1.00 23.42 O -ANISOU 977 O HOH A 291 1645 5270 1983 -1165 114 -10 O -HETATM 978 O HOH A 292 5.050 18.696 2.172 1.00 34.09 O -ANISOU 978 O HOH A 292 2238 7446 3268 1946 1237 1906 O -HETATM 979 O HOH A 293 17.068 36.045 5.392 1.00 26.22 O -ANISOU 979 O HOH A 293 3429 3801 2733 269 549 -733 O -HETATM 980 O HOH A 294 -7.982 21.677 14.715 1.00 21.18 O -ANISOU 980 O HOH A 294 1192 3131 3726 -350 -168 -302 O -HETATM 981 O HOH A 295 19.475 39.203 9.954 1.00 28.69 O -ANISOU 981 O HOH A 295 3888 3518 3496 -1579 394 849 O -HETATM 982 O HOH A 296 12.516 45.420 23.196 1.00 24.76 O -ANISOU 982 O HOH A 296 3394 3101 2913 -1422 -940 -344 O -HETATM 983 O HOH A 297 4.399 45.631 21.449 1.00 23.46 O -ANISOU 983 O HOH A 297 3846 3076 1992 1698 581 -94 O -HETATM 984 O HOH A 298 9.241 26.488 0.541 1.00 20.92 O -ANISOU 984 O HOH A 298 3049 2917 1985 265 516 -315 O -HETATM 985 O HOH A 299 -4.470 33.902 23.181 1.00 23.26 O -ANISOU 985 O HOH A 299 3632 3451 1752 1351 805 443 O -HETATM 986 O HOH A 300 8.655 44.547 21.592 1.00 21.25 O -ANISOU 986 O HOH A 300 2231 3351 2493 206 347 -683 O -HETATM 987 O HOH A 301 -1.163 35.441 26.540 1.00 17.04 O -ANISOU 987 O HOH A 301 2213 1400 2862 140 282 45 O -HETATM 988 O HOH A 302 -0.675 44.210 10.175 1.00 27.89 O -ANISOU 988 O HOH A 302 2750 1194 6655 152 1330 422 O -HETATM 989 O HOH A 303 7.342 16.398 13.960 1.00 20.75 O -ANISOU 989 O HOH A 303 3684 2283 1918 335 523 438 O -HETATM 990 O HOH A 304 2.925 21.065 1.760 1.00 25.10 O -ANISOU 990 O HOH A 304 4267 2999 2271 1586 500 -370 O -HETATM 991 O HOH A 305 5.589 15.822 12.286 1.00 22.53 O -ANISOU 991 O HOH A 305 3210 1319 4034 466 1226 627 O -HETATM 992 O HOH A 306 1.313 30.594 32.173 1.00 25.01 O -ANISOU 992 O HOH A 306 5636 2556 1313 -514 797 -363 O -HETATM 993 O HOH A 307 9.443 45.414 6.363 1.00 24.46 O -ANISOU 993 O HOH A 307 2162 5199 1935 478 -392 859 O -HETATM 994 O HOH A 308 18.302 32.809 4.888 1.00 39.47 O -ANISOU 994 O HOH A 308 3052 7163 4780 1825 2121 -1175 O -HETATM 995 O HOH A 309 -8.246 30.310 3.117 1.00 29.87 O -ANISOU 995 O HOH A 309 2507 4046 4795 284 -1364 1247 O -HETATM 996 O HOH A 310 -8.472 25.903 15.890 1.00 25.55 O -ANISOU 996 O HOH A 310 2062 5116 2530 -302 662 207 O -HETATM 997 O HOH A 311 -4.716 24.818 23.377 1.00 44.90 O -ANISOU 997 O HOH A 311 5985 5309 5766 -1142 3986 1709 O -HETATM 998 O HOH A 312 11.907 35.674 30.836 1.00 30.71 O -ANISOU 998 O HOH A 312 6425 2641 2603 -659 -1861 477 O -HETATM 999 O HOH A 313 3.133 29.496 -0.949 1.00 35.81 O -ANISOU 999 O HOH A 313 5521 5510 2575 1334 418 -1422 O -HETATM 1000 O HOH A 314 2.232 22.903 0.529 1.00 25.78 O -ANISOU 1000 O HOH A 314 3612 3050 3132 110 221 1228 O -HETATM 1001 O HOH A 315 15.445 38.281 26.861 1.00 22.45 O -ANISOU 1001 O HOH A 315 2408 3859 2264 498 603 843 O -HETATM 1002 O HOH A 316 -2.558 24.588 1.688 1.00 18.50 O -ANISOU 1002 O HOH A 316 2670 2817 1544 265 -46 76 O -HETATM 1003 O HOH A 317 -9.368 31.673 6.265 1.00 31.70 O -ANISOU 1003 O HOH A 317 2457 5404 4185 630 496 -35 O -HETATM 1004 O HOH A 318 16.858 45.905 9.015 1.00 19.90 O -ANISOU 1004 O HOH A 318 1422 3969 2172 -512 175 228 O -HETATM 1005 O HOH A 319 6.810 20.828 4.216 1.00 18.69 O -ANISOU 1005 O HOH A 319 2526 2402 2172 612 723 335 O -HETATM 1006 O HOH A 320 -9.061 29.784 16.131 1.00 27.97 O -ANISOU 1006 O HOH A 320 2889 3840 3901 802 1591 -142 O -HETATM 1007 O HOH A 321 14.066 33.740 30.624 1.00 23.07 O -ANISOU 1007 O HOH A 321 3208 2514 3045 356 -1053 132 O -HETATM 1008 O HOH A 322 12.766 40.638 29.405 1.00 35.95 O -ANISOU 1008 O HOH A 322 6432 3966 3261 749 1092 1138 O -HETATM 1009 O HOH A 323 -2.541 34.224 -1.225 1.00 36.79 O -ANISOU 1009 O HOH A 323 3112 8506 2360 -2586 -1213 1763 O -HETATM 1010 O HOH A 324 4.855 10.416 23.951 1.00 40.33 O -ANISOU 1010 O HOH A 324 6319 2913 6092 -2090 2072 667 O -HETATM 1011 O HOH A 325 10.920 28.636 1.019 1.00 31.90 O -ANISOU 1011 O HOH A 325 3425 4404 4291 -1896 -860 -476 O -HETATM 1012 O HOH A 326 2.498 15.088 6.391 1.00 21.99 O -ANISOU 1012 O HOH A 326 2191 1937 4227 -112 475 -440 O -HETATM 1013 O HOH A 327 -6.105 31.794 -1.101 1.00 39.90 O -ANISOU 1013 O HOH A 327 3971 6983 4206 -2330 -2241 -79 O -HETATM 1014 O HOH A 328 -5.617 15.415 25.420 1.00 32.15 O -ANISOU 1014 O HOH A 328 1660 5306 5249 598 889 571 O -HETATM 1015 O HOH A 329 11.438 51.916 15.034 1.00 31.96 O -ANISOU 1015 O HOH A 329 5421 2549 4175 -1459 -555 207 O -HETATM 1016 O HOH A 330 14.070 49.934 12.877 1.00 25.03 O -ANISOU 1016 O HOH A 330 2615 2723 4173 -202 392 -568 O -HETATM 1017 O HOH A 331 -3.673 22.172 26.276 1.00 27.32 O -ANISOU 1017 O HOH A 331 3104 5702 1574 -799 1160 -580 O -HETATM 1018 O HOH A 332 6.275 15.373 9.214 1.00 28.98 O -ANISOU 1018 O HOH A 332 3450 5843 1720 459 612 37 O -HETATM 1019 O HOH A 333 10.394 34.603 2.359 1.00 28.12 O -ANISOU 1019 O HOH A 333 4040 2937 3708 -10 -1466 1387 O -HETATM 1020 O HOH A 334 6.006 13.658 23.344 1.00 38.41 O -ANISOU 1020 O HOH A 334 7261 4688 2644 1062 2123 2 O -HETATM 1021 O HOH A 335 -1.615 22.342 27.918 1.00 39.60 O -ANISOU 1021 O HOH A 335 4995 4068 5983 -1938 1213 1123 O -HETATM 1022 O HOH A 336 -10.204 28.740 4.120 1.00 27.41 O -ANISOU 1022 O HOH A 336 2580 4216 3619 1195 -87 688 O -HETATM 1023 O HOH A 337 9.246 14.545 12.216 1.00 29.98 O -ANISOU 1023 O HOH A 337 4048 4187 3154 338 -523 1436 O -HETATM 1024 O HOH A 338 6.698 14.173 20.182 1.00 34.17 O -ANISOU 1024 O HOH A 338 2445 4950 5588 472 -1455 943 O -HETATM 1025 O HOH A 339 5.385 38.898 -1.814 1.00 38.97 O -ANISOU 1025 O HOH A 339 4925 4482 5401 1624 -1560 1630 O -HETATM 1026 O HOH A 340 8.469 49.083 19.613 1.00 38.74 O -ANISOU 1026 O HOH A 340 5387 6297 3036 835 -1714 824 O -HETATM 1027 O HOH A 341 -4.821 19.673 27.578 1.00 42.12 O -ANISOU 1027 O HOH A 341 5292 6718 3994 -1189 1701 2122 O -HETATM 1028 O HOH A 342 -0.347 44.492 19.791 1.00 41.43 O -ANISOU 1028 O HOH A 342 2191 7574 5975 -513 -1362 377 O -HETATM 1029 O HOH A 343 6.896 27.777 -0.953 1.00 31.45 O -ANISOU 1029 O HOH A 343 5356 3040 3552 -274 -825 -1019 O -HETATM 1030 O HOH A 344 3.699 25.298 31.775 1.00 30.50 O -ANISOU 1030 O HOH A 344 3146 3546 4898 -431 1186 -136 O -HETATM 1031 O HOH A 345 -0.637 44.668 17.166 1.00 27.18 O -ANISOU 1031 O HOH A 345 1583 5082 3660 -141 296 1409 O -HETATM 1032 O HOH A 346 2.148 44.247 20.844 1.00 26.22 O -ANISOU 1032 O HOH A 346 3113 4649 2198 1562 -69 -1008 O -HETATM 1033 O HOH A 347 12.881 47.632 19.548 1.00 29.69 O -ANISOU 1033 O HOH A 347 2465 6527 2290 1695 -692 -1261 O -HETATM 1034 O HOH A 348 13.003 47.817 7.278 1.00 35.81 O -ANISOU 1034 O HOH A 348 6479 4033 3093 2580 333 732 O -HETATM 1035 O HOH A 349 7.054 34.633 1.803 1.00 30.01 O -ANISOU 1035 O HOH A 349 3910 4890 2601 2500 703 10 O -HETATM 1036 O HOH A 350 9.566 41.930 0.037 1.00 38.56 O -ANISOU 1036 O HOH A 350 4441 5102 5107 -979 1212 -3165 O -HETATM 1037 O HOH A 351 10.082 52.260 16.836 1.00 39.90 O -ANISOU 1037 O HOH A 351 4795 4638 5727 -166 -117 -2827 O -HETATM 1038 O HOH A 352 -5.486 19.928 24.616 1.00 37.08 O -ANISOU 1038 O HOH A 352 2834 7247 4006 -852 1124 2752 O -HETATM 1039 O HOH A 353 2.922 12.164 19.992 1.00 23.99 O -ANISOU 1039 O HOH A 353 2547 2538 4031 290 567 -175 O -HETATM 1040 O HOH A 354 5.822 38.406 0.373 1.00 30.18 O -ANISOU 1040 O HOH A 354 5028 3316 3123 1908 -400 -366 O -HETATM 1041 O HOH A 355 -4.326 36.143 -0.056 1.00 29.15 O -ANISOU 1041 O HOH A 355 4234 2844 3997 -1459 -921 1141 O -HETATM 1042 O HOH A 356 17.171 38.617 5.518 1.00 46.91 O -ANISOU 1042 O HOH A 356 8342 5040 4443 624 2887 894 O -HETATM 1043 O HOH A 357 -9.505 22.143 12.707 1.00 34.75 O -ANISOU 1043 O HOH A 357 3042 5760 4402 -661 -1310 1607 O -HETATM 1044 O HOH A 358 15.762 40.264 6.275 1.00 33.76 O -ANISOU 1044 O HOH A 358 3455 3860 5510 622 1762 2236 O -HETATM 1045 O HOH A 359 2.739 22.067 29.879 1.00 42.65 O -ANISOU 1045 O HOH A 359 6975 3688 5543 965 -165 -2241 O -HETATM 1046 O HOH A 360 -5.828 36.544 2.570 1.00 39.35 O -ANISOU 1046 O HOH A 360 6179 3772 5001 1202 -649 672 O -HETATM 1047 O HOH A 361 16.251 48.952 8.974 1.00 46.44 O -ANISOU 1047 O HOH A 361 5005 5154 7485 -2322 1137 1344 O -HETATM 1048 O HOH A 362 -5.360 22.899 21.082 1.00 19.02 O -ANISOU 1048 O HOH A 362 2060 2450 2716 -218 15 932 O -HETATM 1049 O HOH A 363 23.641 30.968 10.348 1.00 14.46 O -ANISOU 1049 O HOH A 363 1349 1450 2695 -14 796 -304 O -HETATM 1050 O HOH A 364 2.407 21.572 27.657 1.00 16.60 O -ANISOU 1050 O HOH A 364 1986 1619 2703 55 -971 128 O -HETATM 1051 O HOH A 365 -4.030 35.316 3.875 1.00 30.49 O -ANISOU 1051 O HOH A 365 2820 2696 6069 519 -247 386 O -HETATM 1052 O HOH A 366 0.904 41.810 17.563 1.00 19.65 O -ANISOU 1052 O HOH A 366 2086 2621 2759 276 -539 -171 O -HETATM 1053 O HOH A 367 7.024 25.264 24.843 1.00 18.73 O -ANISOU 1053 O HOH A 367 2597 2214 2307 -552 235 34 O -HETATM 1054 O HOH A 368 -0.918 42.053 9.538 1.00 20.02 O -ANISOU 1054 O HOH A 368 1802 3573 2231 -117 -122 99 O -HETATM 1055 O HOH A 369 13.933 23.788 5.614 1.00 35.92 O -ANISOU 1055 O HOH A 369 2134 6479 5034 -236 -1446 2327 O -HETATM 1056 O HOH A 370 -5.275 14.237 23.171 1.00 23.83 O -ANISOU 1056 O HOH A 370 3308 3386 2362 -1619 46 71 O -HETATM 1057 O HOH A 371 0.607 49.428 16.790 1.00 29.75 O -ANISOU 1057 O HOH A 371 5912 2310 3082 -51 -65 765 O -HETATM 1058 O HOH A 372 7.917 44.277 24.521 1.00 40.62 O -ANISOU 1058 O HOH A 372 4609 6416 4408 2065 -608 -2336 O -HETATM 1059 O HOH A 373 4.319 49.911 19.263 1.00 38.91 O -ANISOU 1059 O HOH A 373 6107 6418 2260 285 966 -1457 O -HETATM 1060 O HOH A 374 1.588 19.042 4.938 1.00 37.20 O -ANISOU 1060 O HOH A 374 2257 5589 6288 -560 -1217 -2551 O -HETATM 1061 O HOH A 375 10.617 41.028 30.951 1.00 38.39 O -ANISOU 1061 O HOH A 375 4910 3949 5728 -468 1427 -1013 O -HETATM 1062 O HOH A 376 -6.844 20.506 21.175 1.00 43.51 O -ANISOU 1062 O HOH A 376 7753 5734 3043 957 -826 950 O -HETATM 1063 O HOH A 377 -0.783 47.599 18.622 1.00 37.52 O -ANISOU 1063 O HOH A 377 3311 5321 5624 -67 1291 213 O -HETATM 1064 O HOH A 378 8.192 24.720 30.804 1.00 29.55 O -ANISOU 1064 O HOH A 378 4989 3128 3111 1347 -127 -339 O -HETATM 1065 O HOH A 379 13.960 33.633 1.056 1.00 40.50 O -ANISOU 1065 O HOH A 379 4102 4874 6413 -2011 464 -1058 O -HETATM 1066 O HOH A 380 -5.244 26.781 24.449 1.00 45.53 O -ANISOU 1066 O HOH A 380 7336 5210 4752 -1389 -102 412 O -HETATM 1067 O HOH A 381 -7.231 28.450 0.130 1.00 36.12 O -ANISOU 1067 O HOH A 381 4216 5495 4015 -942 -2394 -579 O -HETATM 1068 O HOH A 382 -10.027 30.438 9.295 1.00 40.64 O -ANISOU 1068 O HOH A 382 5948 4941 4553 254 3024 796 O -HETATM 1069 O HOH A 383 7.559 38.160 -1.352 1.00 41.14 O -ANISOU 1069 O HOH A 383 5192 4545 5893 73 2809 -1490 O -HETATM 1070 O HOH A 384 8.579 44.240 3.164 1.00 48.68 O -ANISOU 1070 O HOH A 384 6347 4456 7693 3466 5 -628 O -HETATM 1071 O HOH A 385 -9.822 26.179 10.561 1.00 27.53 O -ANISOU 1071 O HOH A 385 1368 4039 5055 226 -268 -63 O -HETATM 1072 O HOH A 386 -1.328 34.166 29.837 1.00 43.94 O -ANISOU 1072 O HOH A 386 2838 8741 5118 1225 -936 1511 O -HETATM 1073 O HOH A 387 9.648 28.610 32.348 1.00 45.42 O -ANISOU 1073 O HOH A 387 7710 6195 3354 524 -587 1226 O -HETATM 1074 O HOH A 388 -10.258 28.422 14.318 1.00 38.51 O -ANISOU 1074 O HOH A 388 1662 8198 4771 -299 -252 693 O -HETATM 1075 O HOH A 389 -0.170 46.029 13.021 1.00 36.39 O -ANISOU 1075 O HOH A 389 5160 3664 5002 -1269 1545 -898 O -HETATM 1076 O HOH A 390 -3.264 26.955 31.202 1.00 39.35 O -ANISOU 1076 O HOH A 390 7156 4824 2972 -1756 755 220 O -HETATM 1077 O HOH A 391 19.861 36.882 24.411 1.00 46.81 O -ANISOU 1077 O HOH A 391 5741 4677 7369 -2316 -1809 -1740 O -HETATM 1078 O HOH A 392 6.847 36.896 1.862 1.00 32.88 O -ANISOU 1078 O HOH A 392 3512 6090 2890 -170 -735 1147 O -HETATM 1079 O HOH A 393 9.318 36.123 -1.181 1.00 47.29 O -ANISOU 1079 O HOH A 393 5894 7449 4627 -422 -3427 -851 O -HETATM 1080 O HOH A 394 17.244 25.683 18.693 1.00 25.38 O -ANISOU 1080 O HOH A 394 3865 2626 3152 833 1769 427 O -HETATM 1081 O HOH A 395 0.123 27.596 -1.213 1.00 54.28 O -ANISOU 1081 O HOH A 395 4578 7518 8527 -1827 1535 120 O -HETATM 1082 O HOH A 396 0.432 47.976 21.724 1.00 40.79 O -ANISOU 1082 O HOH A 396 5991 3875 5633 -1561 -989 -1240 O -HETATM 1083 O HOH A 397 -6.635 15.335 20.459 1.00 42.98 O -ANISOU 1083 O HOH A 397 3645 6347 6339 1366 2504 1248 O -HETATM 1084 O HOH A 398 -6.617 16.073 23.084 1.00 38.05 O -ANISOU 1084 O HOH A 398 4101 4387 5968 1416 2297 -353 O -HETATM 1085 O HOH A 399 -6.810 36.320 7.280 1.00 44.85 O -ANISOU 1085 O HOH A 399 5607 4722 6711 705 1418 603 O -HETATM 1086 O HOH A 400 3.851 9.987 20.867 1.00 29.63 O -ANISOU 1086 O HOH A 400 4103 4076 3081 1830 -42 737 O -HETATM 1087 O HOH A 401 14.263 46.258 6.163 1.00 47.71 O -ANISOU 1087 O HOH A 401 5296 6608 6222 -695 2312 752 O -HETATM 1088 O HOH A 402 -2.786 25.893 26.306 1.00 47.51 O -ANISOU 1088 O HOH A 402 4515 5888 7647 -974 3906 -470 O -HETATM 1089 O HOH A 403 21.376 34.580 20.347 1.00 36.76 O -ANISOU 1089 O HOH A 403 5139 4569 4258 878 2120 1719 O -HETATM 1090 O HOH A 404 10.450 18.319 16.933 1.00 45.59 O -ANISOU 1090 O HOH A 404 5686 5562 6076 -279 -787 1850 O -HETATM 1091 O HOH A 405 8.491 41.020 27.037 1.00 34.02 O -ANISOU 1091 O HOH A 405 3209 4565 5151 1302 2080 2093 O -HETATM 1092 O HOH A 406 18.657 27.479 19.594 1.00 31.58 O -ANISOU 1092 O HOH A 406 5312 1775 4911 589 -2738 390 O -HETATM 1093 O HOH A 407 -7.657 23.673 22.401 1.00 41.10 O -ANISOU 1093 O HOH A 407 2600 6256 6760 852 1896 317 O -HETATM 1094 O HOH A 408 14.849 49.907 10.724 1.00 33.58 O -ANISOU 1094 O HOH A 408 3317 4671 4771 -290 337 412 O -HETATM 1095 O HOH A 409 -10.365 24.592 18.461 1.00 47.58 O -ANISOU 1095 O HOH A 409 6230 4571 7277 2538 -2320 -2007 O -HETATM 1096 O HOH A 410 -1.423 29.150 32.136 1.00 36.85 O -ANISOU 1096 O HOH A 410 4673 5428 3900 1463 -147 -90 O -HETATM 1097 O HOH A 411 15.217 43.507 7.331 1.00 44.94 O -ANISOU 1097 O HOH A 411 5805 6457 4814 -680 2377 792 O -CONECT 1 2 3 4 -CONECT 2 1 -CONECT 3 1 -CONECT 4 1 -CONECT 400 878 -CONECT 417 878 -CONECT 433 878 -CONECT 441 878 -CONECT 464 878 -CONECT 496 878 -CONECT 497 878 -CONECT 723 879 -CONECT 746 879 -CONECT 758 879 -CONECT 768 879 -CONECT 816 879 -CONECT 817 879 -CONECT 878 400 417 433 441 -CONECT 878 464 496 497 -CONECT 879 723 746 758 768 -CONECT 879 816 817 887 -CONECT 881 882 883 -CONECT 882 881 -CONECT 883 881 -CONECT 884 885 886 -CONECT 885 884 -CONECT 886 884 -CONECT 887 879 -MASTER 285 0 6 8 0 0 14 6 1096 1 28 9 -END |