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Diffstat (limited to 'plip/test/pdb/1vfy.pdb')
| -rw-r--r-- | plip/test/pdb/1vfy.pdb | 1054 |
1 files changed, 0 insertions, 1054 deletions
diff --git a/plip/test/pdb/1vfy.pdb b/plip/test/pdb/1vfy.pdb deleted file mode 100644 index d5caebd..0000000 --- a/plip/test/pdb/1vfy.pdb +++ /dev/null @@ -1,1054 +0,0 @@ -HEADER TRANSPORT PROTEIN 26-APR-99 1VFY -TITLE PHOSPHATIDYLINOSITOL-3-PHOSPHATE BINDING FYVE DOMAIN OF -TITLE 2 VPS27P PROTEIN FROM SACCHAROMYCES CEREVISIAE -COMPND MOL_ID: 1; -COMPND 2 MOLECULE: PHOSPHATIDYLINOSITOL-3-PHOSPHATE BINDING FYVE -COMPND 3 DOMAIN OF PROTEIN VPS27; -COMPND 4 CHAIN: A; -COMPND 5 FRAGMENT: 163-229, FYVE DOMAIN; -COMPND 6 ENGINEERED: YES; -COMPND 7 MUTATION: YES -SOURCE MOL_ID: 1; -SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; -SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST; -SOURCE 4 ORGANISM_TAXID: 4932; -SOURCE 5 CELLULAR_LOCATION: CYTOPLASM, ENDOSOMAL MEMBRANES; -SOURCE 6 GENE: VPS27; -SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); -SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008; -SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21; -SOURCE 10 EXPRESSION_SYSTEM_VARIANT: DE3; -SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; -SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PGEX-2T -KEYWDS FYVE DOMAIN, ENDOSOME MATURATION, INTRACELLULAR TRAFFICKING, -KEYWDS 2 TRANSPORT PROTEIN -EXPDTA X-RAY DIFFRACTION -AUTHOR J.H.HURLEY,S.MISRA -REVDAT 4 24-FEB-09 1VFY 1 VERSN -REVDAT 3 25-NOV-03 1VFY 1 SOURCE JRNL REMARK MASTER -REVDAT 2 22-DEC-99 1VFY 1 JRNL HEADER DBREF -REVDAT 1 06-MAY-99 1VFY 0 -JRNL AUTH S.MISRA,J.H.HURLEY -JRNL TITL CRYSTAL STRUCTURE OF A PHOSPHATIDYLINOSITOL -JRNL TITL 2 3-PHOSPHATE-SPECIFIC MEMBRANE-TARGETING MOTIF, THE -JRNL TITL 3 FYVE DOMAIN OF VPS27P. -JRNL REF CELL(CAMBRIDGE,MASS.) V. 97 657 1999 -JRNL REFN ISSN 0092-8674 -JRNL PMID 10367894 -JRNL DOI 10.1016/S0092-8674(00)80776-X -REMARK 1 -REMARK 2 -REMARK 2 RESOLUTION. 1.15 ANGSTROMS. -REMARK 3 -REMARK 3 REFINEMENT. -REMARK 3 PROGRAM : CNS 0.5 -REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- -REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, -REMARK 3 : READ,RICE,SIMONSON,WARREN -REMARK 3 -REMARK 3 REFINEMENT TARGET : NULL -REMARK 3 -REMARK 3 DATA USED IN REFINEMENT. -REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.15 -REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 -REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 -REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL -REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL -REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 85.4 -REMARK 3 NUMBER OF REFLECTIONS : 20972 -REMARK 3 -REMARK 3 FIT TO DATA USED IN REFINEMENT. -REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT -REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM -REMARK 3 R VALUE (WORKING SET) : 0.174 -REMARK 3 FREE R VALUE : 0.181 -REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000 -REMARK 3 FREE R VALUE TEST SET COUNT : 977 -REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL -REMARK 3 -REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. -REMARK 3 TOTAL NUMBER OF BINS USED : 10 -REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.15 -REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.19 -REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 69.20 -REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1609 -REMARK 3 BIN R VALUE (WORKING SET) : 0.2130 -REMARK 3 BIN FREE R VALUE : 0.2480 -REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.80 -REMARK 3 BIN FREE R VALUE TEST SET COUNT : 67 -REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL -REMARK 3 -REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. -REMARK 3 PROTEIN ATOMS : 532 -REMARK 3 NUCLEIC ACID ATOMS : 0 -REMARK 3 HETEROGEN ATOMS : 2 -REMARK 3 SOLVENT ATOMS : 109 -REMARK 3 -REMARK 3 B VALUES. -REMARK 3 FROM WILSON PLOT (A**2) : NULL -REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.60 -REMARK 3 OVERALL ANISOTROPIC B VALUE. -REMARK 3 B11 (A**2) : 0.11900 -REMARK 3 B22 (A**2) : 0.78600 -REMARK 3 B33 (A**2) : -0.90000 -REMARK 3 B12 (A**2) : 0.17600 -REMARK 3 B13 (A**2) : 0.53700 -REMARK 3 B23 (A**2) : 1.79500 -REMARK 3 -REMARK 3 ESTIMATED COORDINATE ERROR. -REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.12 -REMARK 3 ESD FROM SIGMAA (A) : 0.08 -REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00 -REMARK 3 -REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. -REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.13 -REMARK 3 ESD FROM C-V SIGMAA (A) : 0.07 -REMARK 3 -REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. -REMARK 3 BOND LENGTHS (A) : 0.012 -REMARK 3 BOND ANGLES (DEGREES) : 1.77 -REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.70 -REMARK 3 IMPROPER ANGLES (DEGREES) : 1.03 -REMARK 3 -REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED -REMARK 3 -REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA -REMARK 3 MAIN-CHAIN BOND (A**2) : 1.570 ; NULL -REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.200 ; NULL -REMARK 3 SIDE-CHAIN BOND (A**2) : 3.430 ; NULL -REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.860 ; NULL -REMARK 3 -REMARK 3 BULK SOLVENT MODELING. -REMARK 3 METHOD USED : FLAT MODEL -REMARK 3 KSOL : 0.41 -REMARK 3 BSOL : 46.40 -REMARK 3 -REMARK 3 NCS MODEL : NULL -REMARK 3 -REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT -REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL -REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL -REMARK 3 -REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM -REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM -REMARK 3 PARAMETER FILE 3 : PARAM19.ION -REMARK 3 PARAMETER FILE 4 : NULL -REMARK 3 TOPOLOGY FILE 1 : GENERATE_9.MTF -REMARK 3 TOPOLOGY FILE 2 : NULL -REMARK 3 TOPOLOGY FILE 3 : NULL -REMARK 3 TOPOLOGY FILE 4 : NULL -REMARK 3 -REMARK 3 OTHER REFINEMENT REMARKS: NULL -REMARK 4 -REMARK 4 1VFY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 -REMARK 100 -REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-APR-99. -REMARK 100 THE RCSB ID CODE IS RCSB000947. -REMARK 200 -REMARK 200 EXPERIMENTAL DETAILS -REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION -REMARK 200 DATE OF DATA COLLECTION : 15-FEB-99 -REMARK 200 TEMPERATURE (KELVIN) : 95 -REMARK 200 PH : 5.6 -REMARK 200 NUMBER OF CRYSTALS USED : 1 -REMARK 200 -REMARK 200 SYNCHROTRON (Y/N) : Y -REMARK 200 RADIATION SOURCE : NSLS -REMARK 200 BEAMLINE : X9B -REMARK 200 X-RAY GENERATOR MODEL : NULL -REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M -REMARK 200 WAVELENGTH OR RANGE (A) : 1.2830,1.2822,1.2320 -REMARK 200 MONOCHROMATOR : NULL -REMARK 200 OPTICS : NULL -REMARK 200 -REMARK 200 DETECTOR TYPE : CCD -REMARK 200 DETECTOR MANUFACTURER : ADSC -REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO -REMARK 200 DATA SCALING SOFTWARE : SCALEPACK -REMARK 200 -REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20972 -REMARK 200 RESOLUTION RANGE HIGH (A) : 1.150 -REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 -REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 -REMARK 200 -REMARK 200 OVERALL. -REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4 -REMARK 200 DATA REDUNDANCY : 3.800 -REMARK 200 R MERGE (I) : 0.06500 -REMARK 200 R SYM (I) : 0.06500 -REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.6000 -REMARK 200 -REMARK 200 IN THE HIGHEST RESOLUTION SHELL. -REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 -REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07 -REMARK 200 COMPLETENESS FOR SHELL (%) : 82.3 -REMARK 200 DATA REDUNDANCY IN SHELL : 3.40 -REMARK 200 R MERGE FOR SHELL (I) : 0.01100 -REMARK 200 R SYM FOR SHELL (I) : 0.01100 -REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.000 -REMARK 200 -REMARK 200 DIFFRACTION PROTOCOL: MAD -REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD -REMARK 200 SOFTWARE USED: SOLVE -REMARK 200 STARTING MODEL: NULL -REMARK 200 -REMARK 200 REMARK: NULL -REMARK 280 -REMARK 280 CRYSTAL -REMARK 280 SOLVENT CONTENT, VS (%): 38.00 -REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16 -REMARK 280 -REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M -REMARK 280 SODIUM ACETATE PH 4.6, 15% PEG 4000, PH 5.6 -REMARK 290 -REMARK 290 CRYSTALLOGRAPHIC SYMMETRY -REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 -REMARK 290 -REMARK 290 SYMOP SYMMETRY -REMARK 290 NNNMMM OPERATOR -REMARK 290 1555 X,Y,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 -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 465 -REMARK 465 MISSING RESIDUES -REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE -REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN -REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) -REMARK 465 -REMARK 465 M RES C SSSEQI -REMARK 465 ASP A 163 -REMARK 465 SER A 164 -REMARK 465 LYS A 165 -REMARK 465 THR A 166 -REMARK 465 PRO A 167 -REMARK 465 ALA A 168 -REMARK 500 -REMARK 500 GEOMETRY AND STEREOCHEMISTRY -REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT -REMARK 500 -REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. -REMARK 500 -REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE -REMARK 500 OG SER A 173 O HOH A 10 1.91 -REMARK 500 O HOH A 48 O HOH A 103 1.94 -REMARK 500 O HOH A 79 O HOH A 94 2.08 -REMARK 500 O HOH A 9 O HOH A 42 2.08 -REMARK 500 OD1 ASP A 223 O HOH A 31 2.14 -REMARK 500 -REMARK 500 REMARK: NULL -REMARK 500 -REMARK 500 GEOMETRY AND STEREOCHEMISTRY -REMARK 500 SUBTOPIC: CLOSE CONTACTS -REMARK 500 -REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC -REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 -REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A -REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 -REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE -REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. -REMARK 500 -REMARK 500 DISTANCE CUTOFF: -REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS -REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS -REMARK 500 -REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE -REMARK 500 O HOH A 59 O HOH A 60 1445 2.05 -REMARK 500 O HOH A 1 O HOH A 6 1455 2.15 -REMARK 500 -REMARK 500 REMARK: NULL -REMARK 500 -REMARK 500 GEOMETRY AND STEREOCHEMISTRY -REMARK 500 SUBTOPIC: TORSION ANGLES -REMARK 500 -REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: -REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; -REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). -REMARK 500 -REMARK 500 STANDARD TABLE: -REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) -REMARK 500 -REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- -REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 -REMARK 500 -REMARK 500 M RES CSSEQI PSI PHI -REMARK 500 ASN A 187 83.91 -154.10 -REMARK 500 SER A 204 44.21 -152.38 -REMARK 500 -REMARK 500 REMARK: NULL -REMARK 525 -REMARK 525 SOLVENT -REMARK 525 -REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT -REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST -REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT -REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE -REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; -REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE -REMARK 525 NUMBER; I=INSERTION CODE): -REMARK 525 -REMARK 525 M RES CSSEQI -REMARK 525 HOH A 48 DISTANCE = 5.05 ANGSTROMS -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 ZN A 301 ZN -REMARK 620 N RES CSSEQI ATOM -REMARK 620 1 CYS A 176 SG -REMARK 620 2 CYS A 179 SG 108.2 -REMARK 620 3 CYS A 200 SG 113.2 115.8 -REMARK 620 4 HIS A 203 ND1 114.1 109.1 96.1 -REMARK 620 N 1 2 3 -REMARK 620 -REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL -REMARK 620 ZN A 300 ZN -REMARK 620 N RES CSSEQI ATOM -REMARK 620 1 CYS A 192 SG -REMARK 620 2 CYS A 195 SG 103.6 -REMARK 620 3 CYS A 222 SG 115.6 116.2 -REMARK 620 4 CYS A 225 SG 106.1 112.8 102.4 -REMARK 620 N 1 2 3 -REMARK 800 -REMARK 800 SITE -REMARK 800 SITE_IDENTIFIER: ZNA -REMARK 800 EVIDENCE_CODE: AUTHOR -REMARK 800 SITE_DESCRIPTION: ZINC ION A LIGANDING RESIDUES -REMARK 800 SITE_IDENTIFIER: ZNB -REMARK 800 EVIDENCE_CODE: AUTHOR -REMARK 800 SITE_DESCRIPTION: ZINC ION B LIGANDING RESIDUES -REMARK 800 SITE_IDENTIFIER: POS -REMARK 800 EVIDENCE_CODE: AUTHOR -REMARK 800 SITE_DESCRIPTION: RKHHCR MOTIF ; PUTATIVE PI3P BINDING SITE -REMARK 800 SITE_IDENTIFIER: AC1 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 300 -REMARK 800 SITE_IDENTIFIER: AC2 -REMARK 800 EVIDENCE_CODE: SOFTWARE -REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301 -DBREF 1VFY A 163 230 UNP P40343 VPS27_YEAST 163 230 -SEQADV 1VFY GLU A 230 UNP P40343 ASP 230 ENGINEERED -SEQRES 1 A 73 ASP SER LYS THR PRO ALA ASP TRP ILE ASP SER ASP ALA -SEQRES 2 A 73 CYS MET ILE CYS SER LYS LYS PHE SER LEU LEU ASN ARG -SEQRES 3 A 73 LYS HIS HIS CYS ARG SER CYS GLY GLY VAL PHE CYS GLN -SEQRES 4 A 73 GLU HIS SER SER ASN SER ILE PRO LEU PRO ASP LEU GLY -SEQRES 5 A 73 ILE TYR GLU PRO VAL ARG VAL CYS ASP SER CYS PHE GLU -SEQRES 6 A 73 ASP TYR GLU PHE ILE VAL THR ASP -HET ZN A 300 1 -HET ZN A 301 1 -HETNAM ZN ZINC ION -FORMUL 2 ZN 2(ZN 2+) -FORMUL 4 HOH *109(H2 O) -HELIX 1 1 GLN A 201 HIS A 203 5 3 -HELIX 2 2 PRO A 211 LEU A 213 5 3 -HELIX 3 3 ASP A 223 VAL A 233 1 11 -SHEET 1 A 2 ASN A 206 ILE A 208 0 -SHEET 2 A 2 VAL A 219 VAL A 221 -1 N VAL A 221 O ASN A 206 -LINK SG CYS A 176 ZN ZN A 301 1555 1555 2.34 -LINK SG CYS A 179 ZN ZN A 301 1555 1555 2.31 -LINK SG CYS A 192 ZN ZN A 300 1555 1555 2.37 -LINK SG CYS A 195 ZN ZN A 300 1555 1555 2.37 -LINK SG CYS A 200 ZN ZN A 301 1555 1555 2.33 -LINK ND1 HIS A 203 ZN ZN A 301 1555 1555 2.14 -LINK SG CYS A 222 ZN ZN A 300 1555 1555 2.33 -LINK SG CYS A 225 ZN ZN A 300 1555 1555 2.35 -SITE 1 ZNA 4 CYS A 176 CYS A 179 CYS A 200 HIS A 203 -SITE 1 ZNB 4 CYS A 192 CYS A 195 CYS A 222 CYS A 225 -SITE 1 POS 7 ARG A 188 LYS A 189 HIS A 190 HIS A 191 -SITE 2 POS 7 CYS A 192 ARG A 193 ARG A 220 -SITE 1 AC1 4 CYS A 192 CYS A 195 CYS A 222 CYS A 225 -SITE 1 AC2 4 CYS A 176 CYS A 179 CYS A 200 HIS A 203 -CRYST1 24.090 26.570 31.610 111.79 92.70 105.70 P 1 1 -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 0.041511 0.011668 0.007217 0.00000 -SCALE2 0.000000 0.039095 0.017026 0.00000 -SCALE3 0.000000 0.000000 0.034544 0.00000 -ATOM 1 N ASP A 169 7.887 17.852 47.781 1.00 18.09 N -ATOM 2 CA ASP A 169 9.275 17.917 47.212 1.00 16.84 C -ATOM 3 C ASP A 169 9.383 17.094 45.931 1.00 9.03 C -ATOM 4 O ASP A 169 9.425 17.684 44.892 1.00 12.14 O -ATOM 5 CB ASP A 169 10.316 17.476 48.223 1.00 27.95 C -ATOM 6 CG ASP A 169 11.709 17.957 47.846 1.00 25.30 C -ATOM 7 OD1 ASP A 169 11.867 19.181 47.597 1.00 30.03 O -ATOM 8 OD2 ASP A 169 12.634 17.118 47.800 1.00 37.73 O -ATOM 9 N TRP A 170 9.435 15.768 45.983 1.00 9.21 N -ATOM 10 CA TRP A 170 9.470 15.019 44.727 1.00 7.79 C -ATOM 11 C TRP A 170 8.087 14.982 44.070 1.00 8.32 C -ATOM 12 O TRP A 170 7.047 14.927 44.756 1.00 8.38 O -ATOM 13 CB TRP A 170 9.950 13.593 44.982 1.00 9.26 C -ATOM 14 CG TRP A 170 11.423 13.433 45.264 1.00 8.90 C -ATOM 15 CD1 TRP A 170 12.286 14.383 45.694 1.00 11.52 C -ATOM 16 CD2 TRP A 170 12.185 12.220 45.141 1.00 9.02 C -ATOM 17 NE1 TRP A 170 13.556 13.840 45.853 1.00 11.26 N -ATOM 18 CE2 TRP A 170 13.511 12.519 45.521 1.00 10.65 C -ATOM 19 CE3 TRP A 170 11.867 10.920 44.748 1.00 13.23 C -ATOM 20 CZ2 TRP A 170 14.521 11.557 45.523 1.00 11.59 C -ATOM 21 CZ3 TRP A 170 12.866 9.967 44.750 1.00 14.05 C -ATOM 22 CH2 TRP A 170 14.180 10.293 45.137 1.00 11.18 C -ATOM 23 N ILE A 171 8.064 15.036 42.737 1.00 6.81 N -ATOM 24 CA ILE A 171 6.823 14.892 41.990 1.00 6.58 C -ATOM 25 C ILE A 171 6.959 13.578 41.212 1.00 6.19 C -ATOM 26 O ILE A 171 7.948 12.869 41.370 1.00 7.51 O -ATOM 27 CB ILE A 171 6.571 16.073 41.029 1.00 6.25 C -ATOM 28 CG1 ILE A 171 7.744 16.256 40.070 1.00 8.25 C -ATOM 29 CG2 ILE A 171 6.370 17.358 41.848 1.00 8.23 C -ATOM 30 CD1 ILE A 171 7.453 17.222 38.943 1.00 19.47 C -ATOM 31 N ASP A 172 5.959 13.227 40.420 1.00 6.16 N -ATOM 32 CA ASP A 172 6.070 12.058 39.570 1.00 6.80 C -ATOM 33 C ASP A 172 5.394 12.348 38.230 1.00 6.37 C -ATOM 34 O ASP A 172 4.529 13.235 38.082 1.00 6.23 O -ATOM 35 CB ASP A 172 5.421 10.837 40.227 1.00 7.86 C -ATOM 36 CG ASP A 172 6.051 9.523 39.789 1.00 14.11 C -ATOM 37 OD1 ASP A 172 6.906 9.481 38.861 1.00 9.81 O -ATOM 38 OD2 ASP A 172 5.674 8.503 40.397 1.00 17.66 O -ATOM 39 N SER A 173 5.862 11.615 37.217 1.00 6.83 N -ATOM 40 CA SER A 173 5.280 11.702 35.884 1.00 8.03 C -ATOM 41 C SER A 173 5.711 10.463 35.128 1.00 8.71 C -ATOM 42 O SER A 173 6.599 9.708 35.580 1.00 8.86 O -ATOM 43 CB SER A 173 5.771 12.935 35.149 1.00 7.20 C -ATOM 44 OG SER A 173 5.046 13.081 33.951 1.00 12.07 O -ATOM 45 N ASP A 174 5.049 10.238 33.998 1.00 8.89 N -ATOM 46 CA ASP A 174 5.382 9.096 33.161 1.00 9.00 C -ATOM 47 C ASP A 174 6.435 9.383 32.084 1.00 8.66 C -ATOM 48 O ASP A 174 6.805 8.462 31.332 1.00 8.74 O -ATOM 49 CB ASP A 174 4.104 8.504 32.542 1.00 12.61 C -ATOM 50 CG ASP A 174 3.421 9.435 31.592 1.00 12.82 C -ATOM 51 OD1 ASP A 174 3.852 10.580 31.399 1.00 18.53 O -ATOM 52 OD2 ASP A 174 2.401 8.986 31.015 1.00 21.51 O -ATOM 53 N ALA A 175 6.937 10.609 32.011 1.00 9.08 N -ATOM 54 CA ALA A 175 7.913 10.948 30.983 1.00 8.25 C -ATOM 55 C ALA A 175 8.933 11.944 31.505 1.00 8.05 C -ATOM 56 O ALA A 175 8.689 12.666 32.472 1.00 7.53 O -ATOM 57 CB ALA A 175 7.177 11.526 29.749 1.00 10.62 C -ATOM 58 N CYS A 176 10.092 11.966 30.872 1.00 7.64 N -ATOM 59 CA CYS A 176 11.168 12.872 31.233 1.00 7.20 C -ATOM 60 C CYS A 176 10.713 14.313 31.069 1.00 8.99 C -ATOM 61 O CYS A 176 10.135 14.684 30.029 1.00 10.70 O -ATOM 62 CB CYS A 176 12.381 12.628 30.348 1.00 7.60 C -ATOM 63 SG CYS A 176 13.775 13.781 30.615 1.00 8.16 S -ATOM 64 N MET A 177 10.985 15.140 32.068 1.00 9.14 N -ATOM 65 CA MET A 177 10.564 16.540 32.001 1.00 9.57 C -ATOM 66 C MET A 177 11.317 17.351 30.943 1.00 13.74 C -ATOM 67 O MET A 177 10.811 18.401 30.493 1.00 16.85 O -ATOM 68 CB MET A 177 10.722 17.186 33.370 1.00 11.73 C -ATOM 69 CG MET A 177 9.740 16.636 34.349 1.00 11.14 C -ATOM 70 SD MET A 177 9.932 17.448 35.905 1.00 13.67 S -ATOM 71 CE MET A 177 8.653 18.685 35.787 1.00 20.85 C -ATOM 72 N ILE A 178 12.476 16.871 30.510 1.00 12.91 N -ATOM 73 CA ILE A 178 13.226 17.597 29.501 1.00 12.63 C -ATOM 74 C ILE A 178 12.849 17.148 28.093 1.00 14.40 C -ATOM 75 O ILE A 178 12.416 17.967 27.262 1.00 17.65 O -ATOM 76 CB ILE A 178 14.747 17.406 29.697 1.00 14.99 C -ATOM 77 CG1 ILE A 178 15.209 18.079 30.993 1.00 14.19 C -ATOM 78 CG2 ILE A 178 15.515 17.961 28.499 1.00 17.45 C -ATOM 79 CD1 ILE A 178 14.840 19.529 31.101 1.00 19.37 C -ATOM 80 N CYS A 179 12.942 15.853 27.825 1.00 11.66 N -ATOM 81 CA CYS A 179 12.671 15.379 26.478 1.00 11.05 C -ATOM 82 C CYS A 179 11.329 14.755 26.190 1.00 13.12 C -ATOM 83 O CYS A 179 11.034 14.414 25.035 1.00 15.44 O -ATOM 84 CB CYS A 179 13.773 14.423 26.033 1.00 12.68 C -ATOM 85 SG CYS A 179 13.873 12.870 26.965 1.00 10.34 S -ATOM 86 N SER A 180 10.526 14.573 27.235 1.00 11.13 N -ATOM 87 CA SER A 180 9.192 14.025 27.113 1.00 11.84 C -ATOM 88 C SER A 180 9.095 12.577 26.657 1.00 12.02 C -ATOM 89 O SER A 180 8.015 12.107 26.339 1.00 13.89 O -ATOM 90 CB SER A 180 8.345 14.922 26.202 1.00 16.99 C -ATOM 91 OG SER A 180 8.156 16.212 26.770 1.00 21.08 O -ATOM 92 N LYS A 181 10.210 11.858 26.652 1.00 10.20 N -ATOM 93 CA LYS A 181 10.192 10.450 26.293 1.00 11.65 C -ATOM 94 C LYS A 181 9.590 9.691 27.476 1.00 9.55 C -ATOM 95 O LYS A 181 9.858 9.985 28.659 1.00 9.53 O -ATOM 96 CB LYS A 181 11.604 9.965 25.955 1.00 9.48 C -ATOM 97 CG LYS A 181 12.081 10.520 24.621 1.00 12.97 C -ATOM 98 CD LYS A 181 13.459 10.040 24.235 1.00 12.13 C -ATOM 99 CE LYS A 181 13.906 10.713 22.946 1.00 16.33 C -ATOM 100 NZ LYS A 181 15.240 10.221 22.553 1.00 22.59 N -ATOM 101 N LYS A 182 8.725 8.730 27.176 1.00 9.30 N -ATOM 102 CA LYS A 182 8.048 7.972 28.215 1.00 8.67 C -ATOM 103 C LYS A 182 8.927 6.913 28.832 1.00 8.04 C -ATOM 104 O LYS A 182 9.632 6.185 28.127 1.00 8.12 O -ATOM 105 CB LYS A 182 6.799 7.328 27.627 1.00 10.54 C -ATOM 106 CG LYS A 182 5.923 6.600 28.633 1.00 17.74 C -ATOM 107 CD LYS A 182 4.713 5.968 27.956 1.00 19.68 C -ATOM 108 CE LYS A 182 3.414 6.352 28.633 1.00 30.63 C -ATOM 109 NZ LYS A 182 3.262 5.658 29.931 1.00 33.39 N -ATOM 110 N PHE A 183 8.892 6.813 30.148 1.00 8.01 N -ATOM 111 CA PHE A 183 9.743 5.843 30.810 1.00 6.91 C -ATOM 112 C PHE A 183 9.273 4.420 30.583 1.00 8.20 C -ATOM 113 O PHE A 183 8.076 4.180 30.483 1.00 9.02 O -ATOM 114 CB PHE A 183 9.791 6.106 32.322 1.00 7.34 C -ATOM 115 CG PHE A 183 10.256 7.487 32.681 1.00 7.05 C -ATOM 116 CD1 PHE A 183 11.533 7.918 32.317 1.00 6.60 C -ATOM 117 CD2 PHE A 183 9.440 8.347 33.409 1.00 8.01 C -ATOM 118 CE1 PHE A 183 11.980 9.176 32.677 1.00 6.91 C -ATOM 119 CE2 PHE A 183 9.885 9.609 33.779 1.00 8.15 C -ATOM 120 CZ PHE A 183 11.139 10.014 33.417 1.00 7.28 C -ATOM 121 N SER A 184 10.218 3.479 30.552 1.00 7.75 N -ATOM 122 CA SER A 184 9.883 2.061 30.422 1.00 6.79 C -ATOM 123 C SER A 184 11.102 1.326 30.968 1.00 7.40 C -ATOM 124 O SER A 184 12.081 1.951 31.390 1.00 8.09 O -ATOM 125 CB SER A 184 9.669 1.689 28.946 1.00 10.99 C -ATOM 126 OG SER A 184 10.916 1.500 28.305 1.00 13.91 O -ATOM 127 N LEU A 185 11.071 -0.004 30.973 1.00 8.27 N -ATOM 128 CA LEU A 185 12.231 -0.730 31.442 1.00 8.66 C -ATOM 129 C LEU A 185 13.480 -0.419 30.621 1.00 9.88 C -ATOM 130 O LEU A 185 14.588 -0.579 31.135 1.00 10.97 O -ATOM 131 CB LEU A 185 11.981 -2.241 31.434 1.00 11.19 C -ATOM 132 CG LEU A 185 10.889 -2.724 32.390 1.00 11.54 C -ATOM 133 CD1 LEU A 185 10.739 -4.242 32.270 1.00 15.41 C -ATOM 134 CD2 LEU A 185 11.252 -2.305 33.792 1.00 15.29 C -ATOM 135 N LEU A 186 13.304 -0.008 29.366 1.00 8.63 N -ATOM 136 CA LEU A 186 14.443 0.329 28.499 1.00 9.63 C -ATOM 137 C LEU A 186 14.871 1.809 28.587 1.00 10.10 C -ATOM 138 O LEU A 186 15.825 2.219 27.914 1.00 12.23 O -ATOM 139 CB LEU A 186 14.133 -0.022 27.037 1.00 10.62 C -ATOM 140 CG LEU A 186 13.939 -1.521 26.756 1.00 15.06 C -ATOM 141 CD1 LEU A 186 13.636 -1.725 25.265 1.00 17.75 C -ATOM 142 CD2 LEU A 186 15.184 -2.289 27.131 1.00 19.92 C -ATOM 143 N ASN A 187 14.141 2.622 29.358 1.00 8.14 N -ATOM 144 CA ASN A 187 14.519 4.031 29.571 1.00 8.00 C -ATOM 145 C ASN A 187 13.891 4.355 30.926 1.00 6.44 C -ATOM 146 O ASN A 187 12.786 4.892 31.037 1.00 7.18 O -ATOM 147 CB ASN A 187 13.974 4.923 28.470 1.00 10.02 C -ATOM 148 CG ASN A 187 14.668 6.263 28.418 1.00 9.47 C -ATOM 149 OD1 ASN A 187 15.743 6.442 29.015 1.00 9.22 O -ATOM 150 ND2 ASN A 187 14.075 7.210 27.708 1.00 9.23 N -ATOM 151 N ARG A 188 14.611 4.006 31.964 1.00 6.62 N -ATOM 152 CA ARG A 188 14.054 4.089 33.300 1.00 6.70 C -ATOM 153 C ARG A 188 13.879 5.474 33.875 1.00 6.00 C -ATOM 154 O ARG A 188 14.545 6.433 33.489 1.00 6.97 O -ATOM 155 CB ARG A 188 14.881 3.229 34.244 1.00 8.55 C -ATOM 156 CG ARG A 188 14.754 1.760 33.905 1.00 11.77 C -ATOM 157 CD ARG A 188 15.620 0.938 34.737 1.00 20.30 C -ATOM 158 NE ARG A 188 15.479 -0.474 34.392 1.00 20.56 N -ATOM 159 CZ ARG A 188 15.283 -1.412 35.300 1.00 11.56 C -ATOM 160 NH1 ARG A 188 15.198 -1.069 36.574 1.00 11.90 N -ATOM 161 NH2 ARG A 188 15.205 -2.687 34.933 1.00 12.54 N -ATOM 162 N LYS A 189 12.944 5.556 34.809 1.00 7.40 N -ATOM 163 CA LYS A 189 12.623 6.784 35.518 1.00 6.72 C -ATOM 164 C LYS A 189 13.672 7.112 36.589 1.00 6.05 C -ATOM 165 O LYS A 189 14.161 6.217 37.284 1.00 8.03 O -ATOM 166 CB LYS A 189 11.275 6.591 36.206 1.00 6.93 C -ATOM 167 CG LYS A 189 10.811 7.762 37.069 1.00 8.19 C -ATOM 168 CD LYS A 189 9.445 7.466 37.712 1.00 10.43 C -ATOM 169 CE LYS A 189 8.328 7.361 36.690 1.00 9.20 C -ATOM 170 NZ LYS A 189 7.009 7.114 37.366 1.00 10.16 N -ATOM 171 N HIS A 190 14.000 8.399 36.714 1.00 6.00 N -ATOM 172 CA HIS A 190 14.900 8.816 37.780 1.00 5.54 C -ATOM 173 C HIS A 190 14.474 10.173 38.308 1.00 5.57 C -ATOM 174 O HIS A 190 14.035 11.037 37.549 1.00 9.33 O -ATOM 175 CB HIS A 190 16.334 8.958 37.295 1.00 7.15 C -ATOM 176 CG HIS A 190 16.897 7.719 36.696 1.00 7.28 C -ATOM 177 ND1 HIS A 190 17.297 6.648 37.460 1.00 9.42 N -ATOM 178 CD2 HIS A 190 17.080 7.374 35.405 1.00 7.67 C -ATOM 179 CE1 HIS A 190 17.704 5.683 36.652 1.00 7.62 C -ATOM 180 NE2 HIS A 190 17.586 6.094 35.401 1.00 8.78 N -ATOM 181 N HIS A 191 14.614 10.377 39.601 1.00 4.89 N -ATOM 182 CA HIS A 191 14.353 11.682 40.178 1.00 6.19 C -ATOM 183 C HIS A 191 15.638 12.493 40.362 1.00 5.59 C -ATOM 184 O HIS A 191 16.706 11.944 40.690 1.00 5.56 O -ATOM 185 CB HIS A 191 13.717 11.523 41.574 1.00 5.97 C -ATOM 186 CG HIS A 191 12.261 11.206 41.540 1.00 5.68 C -ATOM 187 ND1 HIS A 191 11.764 9.921 41.395 1.00 7.63 N -ATOM 188 CD2 HIS A 191 11.184 12.028 41.592 1.00 7.42 C -ATOM 189 CE1 HIS A 191 10.443 9.977 41.355 1.00 8.67 C -ATOM 190 NE2 HIS A 191 10.068 11.239 41.470 1.00 7.81 N -ATOM 191 N CYS A 192 15.514 13.808 40.191 1.00 4.92 N -ATOM 192 CA CYS A 192 16.589 14.741 40.535 1.00 4.78 C -ATOM 193 C CYS A 192 16.465 14.967 42.058 1.00 4.40 C -ATOM 194 O CYS A 192 15.407 15.370 42.557 1.00 5.76 O -ATOM 195 CB CYS A 192 16.397 16.066 39.824 1.00 4.98 C -ATOM 196 SG CYS A 192 17.613 17.288 40.404 1.00 4.80 S -ATOM 197 N ARG A 193 17.526 14.697 42.797 1.00 4.69 N -ATOM 198 CA ARG A 193 17.500 14.873 44.255 1.00 5.24 C -ATOM 199 C ARG A 193 17.494 16.342 44.669 1.00 5.44 C -ATOM 200 O ARG A 193 17.176 16.659 45.828 1.00 6.02 O -ATOM 201 CB ARG A 193 18.682 14.161 44.895 1.00 5.16 C -ATOM 202 CG ARG A 193 18.431 12.666 45.167 1.00 7.17 C -ATOM 203 CD ARG A 193 18.151 11.832 43.909 1.00 6.74 C -ATOM 204 NE ARG A 193 18.053 10.430 44.323 1.00 7.72 N -ATOM 205 CZ ARG A 193 17.702 9.417 43.542 1.00 8.79 C -ATOM 206 NH1 ARG A 193 17.399 9.625 42.278 1.00 7.49 N -ATOM 207 NH2 ARG A 193 17.677 8.171 44.015 1.00 9.31 N -ATOM 208 N SER A 194 17.827 17.243 43.765 1.00 4.70 N -ATOM 209 CA SER A 194 17.793 18.669 44.065 1.00 6.19 C -ATOM 210 C SER A 194 16.403 19.299 43.831 1.00 6.12 C -ATOM 211 O SER A 194 15.860 19.927 44.758 1.00 9.35 O -ATOM 212 CB SER A 194 18.827 19.396 43.206 1.00 6.78 C -ATOM 213 OG SER A 194 18.754 20.809 43.306 1.00 10.28 O -ATOM 214 N CYS A 195 15.822 19.120 42.647 1.00 4.94 N -ATOM 215 CA CYS A 195 14.548 19.773 42.362 1.00 6.16 C -ATOM 216 C CYS A 195 13.337 18.859 42.468 1.00 5.23 C -ATOM 217 O CYS A 195 12.189 19.354 42.456 1.00 6.66 O -ATOM 218 CB CYS A 195 14.599 20.464 40.980 1.00 6.83 C -ATOM 219 SG CYS A 195 14.589 19.297 39.585 1.00 6.21 S -ATOM 220 N GLY A 196 13.529 17.551 42.571 1.00 5.90 N -ATOM 221 CA GLY A 196 12.401 16.631 42.723 1.00 5.92 C -ATOM 222 C GLY A 196 11.716 16.198 41.438 1.00 5.44 C -ATOM 223 O GLY A 196 10.791 15.389 41.515 1.00 5.76 O -ATOM 224 N GLY A 197 12.133 16.750 40.300 1.00 5.70 N -ATOM 225 CA GLY A 197 11.555 16.365 39.023 1.00 5.61 C -ATOM 226 C GLY A 197 11.966 14.961 38.589 1.00 4.52 C -ATOM 227 O GLY A 197 12.816 14.322 39.215 1.00 5.68 O -ATOM 228 N VAL A 198 11.352 14.481 37.510 1.00 5.96 N -ATOM 229 CA VAL A 198 11.698 13.163 36.929 1.00 6.50 C -ATOM 230 C VAL A 198 12.323 13.335 35.556 1.00 5.98 C -ATOM 231 O VAL A 198 11.875 14.164 34.752 1.00 5.85 O -ATOM 232 CB VAL A 198 10.505 12.178 36.828 1.00 7.47 C -ATOM 233 CG1 VAL A 198 10.093 11.729 38.233 1.00 8.92 C -ATOM 234 CG2 VAL A 198 9.344 12.805 36.069 1.00 9.54 C -ATOM 235 N PHE A 199 13.373 12.544 35.337 1.00 6.09 N -ATOM 236 CA PHE A 199 14.215 12.666 34.158 1.00 5.07 C -ATOM 237 C PHE A 199 14.705 11.311 33.702 1.00 6.37 C -ATOM 238 O PHE A 199 14.787 10.373 34.481 1.00 6.55 O -ATOM 239 CB PHE A 199 15.463 13.534 34.481 1.00 5.84 C -ATOM 240 CG PHE A 199 15.102 14.888 35.014 1.00 5.33 C -ATOM 241 CD1 PHE A 199 14.893 15.091 36.361 1.00 6.65 C -ATOM 242 CD2 PHE A 199 14.887 15.928 34.151 1.00 7.26 C -ATOM 243 CE1 PHE A 199 14.468 16.337 36.834 1.00 5.10 C -ATOM 244 CE2 PHE A 199 14.465 17.167 34.600 1.00 6.90 C -ATOM 245 CZ PHE A 199 14.257 17.382 35.928 1.00 5.44 C -ATOM 246 N CYS A 200 15.012 11.210 32.410 1.00 6.92 N -ATOM 247 CA CYS A 200 15.636 9.997 31.899 1.00 7.08 C -ATOM 248 C CYS A 200 17.154 10.081 32.252 1.00 5.98 C -ATOM 249 O CYS A 200 17.669 11.131 32.691 1.00 7.16 O -ATOM 250 CB CYS A 200 15.461 9.893 30.381 1.00 8.39 C -ATOM 251 SG CYS A 200 16.399 11.158 29.437 1.00 8.01 S -ATOM 252 N GLN A 201 17.878 8.990 32.048 1.00 6.29 N -ATOM 253 CA GLN A 201 19.307 8.936 32.312 1.00 6.48 C -ATOM 254 C GLN A 201 20.071 9.990 31.514 1.00 7.08 C -ATOM 255 O GLN A 201 20.979 10.643 32.033 1.00 7.26 O -ATOM 256 CB GLN A 201 19.836 7.546 31.945 1.00 7.79 C -ATOM 257 CG GLN A 201 21.333 7.442 31.839 1.00 9.51 C -ATOM 258 CD GLN A 201 22.009 7.655 33.164 1.00 15.44 C -ATOM 259 OE1 GLN A 201 21.452 7.354 34.218 1.00 16.08 O -ATOM 260 NE2 GLN A 201 23.245 8.162 33.115 1.00 20.70 N -ATOM 261 N GLU A 202 19.704 10.166 30.242 1.00 7.64 N -ATOM 262 CA GLU A 202 20.428 11.109 29.418 1.00 8.07 C -ATOM 263 C GLU A 202 20.371 12.524 29.992 1.00 9.70 C -ATOM 264 O GLU A 202 21.287 13.325 29.790 1.00 9.52 O -ATOM 265 CB GLU A 202 19.851 11.115 27.996 1.00 10.33 C -ATOM 266 CG GLU A 202 20.456 12.216 27.150 1.00 15.22 C -ATOM 267 CD GLU A 202 19.934 12.247 25.732 1.00 33.14 C -ATOM 268 OE1 GLU A 202 18.876 11.636 25.453 1.00 31.48 O -ATOM 269 OE2 GLU A 202 20.584 12.903 24.893 1.00 32.73 O -ATOM 270 N HIS A 203 19.292 12.833 30.689 1.00 7.27 N -ATOM 271 CA HIS A 203 19.122 14.162 31.255 1.00 8.16 C -ATOM 272 C HIS A 203 19.338 14.252 32.749 1.00 6.38 C -ATOM 273 O HIS A 203 18.951 15.245 33.372 1.00 9.47 O -ATOM 274 CB HIS A 203 17.759 14.696 30.817 1.00 8.73 C -ATOM 275 CG HIS A 203 17.713 14.942 29.344 1.00 9.72 C -ATOM 276 ND1 HIS A 203 16.830 14.317 28.492 1.00 9.67 N -ATOM 277 CD2 HIS A 203 18.555 15.650 28.557 1.00 11.61 C -ATOM 278 CE1 HIS A 203 17.135 14.617 27.243 1.00 11.04 C -ATOM 279 NE2 HIS A 203 18.179 15.424 27.253 1.00 12.67 N -ATOM 280 N SER A 204 19.963 13.230 33.321 1.00 6.12 N -ATOM 281 CA SER A 204 20.293 13.245 34.757 1.00 6.19 C -ATOM 282 C SER A 204 21.522 12.373 34.971 1.00 5.78 C -ATOM 283 O SER A 204 21.598 11.623 35.936 1.00 7.37 O -ATOM 284 CB SER A 204 19.103 12.762 35.607 1.00 7.84 C -ATOM 285 OG SER A 204 18.711 11.423 35.322 1.00 7.26 O -ATOM 286 N SER A 205 22.522 12.523 34.095 1.00 7.49 N -ATOM 287 CA SER A 205 23.716 11.677 34.166 1.00 7.15 C -ATOM 288 C SER A 205 24.779 12.097 35.162 1.00 7.74 C -ATOM 289 O SER A 205 25.709 11.333 35.427 1.00 8.58 O -ATOM 290 CB SER A 205 24.347 11.526 32.784 1.00 10.72 C -ATOM 291 OG SER A 205 24.971 12.726 32.397 1.00 11.89 O -ATOM 292 N ASN A 206 24.637 13.294 35.743 1.00 6.46 N -ATOM 293 CA ASN A 206 25.594 13.797 36.713 1.00 5.65 C -ATOM 294 C ASN A 206 25.043 13.648 38.132 1.00 6.69 C -ATOM 295 O ASN A 206 23.810 13.556 38.338 1.00 6.77 O -ATOM 296 CB ASN A 206 25.859 15.264 36.420 1.00 7.05 C -ATOM 297 CG ASN A 206 26.380 15.479 35.026 1.00 7.24 C -ATOM 298 OD1 ASN A 206 27.521 15.119 34.732 1.00 9.78 O -ATOM 299 ND2 ASN A 206 25.553 16.050 34.147 1.00 10.03 N -ATOM 300 N SER A 207 25.952 13.637 39.111 1.00 6.08 N -ATOM 301 CA SER A 207 25.583 13.544 40.516 1.00 4.83 C -ATOM 302 C SER A 207 26.427 14.511 41.300 1.00 5.78 C -ATOM 303 O SER A 207 27.626 14.673 41.006 1.00 7.25 O -ATOM 304 CB SER A 207 25.834 12.145 41.012 1.00 6.53 C -ATOM 305 OG SER A 207 25.074 11.210 40.255 1.00 8.56 O -ATOM 306 N ILE A 208 25.824 15.100 42.332 1.00 5.60 N -ATOM 307 CA ILE A 208 26.504 16.089 43.148 1.00 4.63 C -ATOM 308 C ILE A 208 26.089 15.936 44.583 1.00 5.01 C -ATOM 309 O ILE A 208 25.024 15.364 44.880 1.00 5.60 O -ATOM 310 CB ILE A 208 26.104 17.548 42.731 1.00 5.10 C -ATOM 311 CG1 ILE A 208 24.594 17.781 42.945 1.00 6.03 C -ATOM 312 CG2 ILE A 208 26.512 17.825 41.277 1.00 7.43 C -ATOM 313 CD1 ILE A 208 24.116 19.228 42.571 1.00 6.71 C -ATOM 314 N PRO A 209 26.916 16.401 45.520 1.00 5.64 N -ATOM 315 CA PRO A 209 26.506 16.325 46.932 1.00 5.65 C -ATOM 316 C PRO A 209 25.472 17.445 47.082 1.00 5.32 C -ATOM 317 O PRO A 209 25.426 18.382 46.273 1.00 5.95 O -ATOM 318 CB PRO A 209 27.790 16.654 47.692 1.00 6.79 C -ATOM 319 CG PRO A 209 28.525 17.578 46.750 1.00 8.95 C -ATOM 320 CD PRO A 209 28.257 16.999 45.369 1.00 5.75 C -ATOM 321 N LEU A 210 24.637 17.372 48.118 1.00 5.58 N -ATOM 322 CA LEU A 210 23.647 18.418 48.413 1.00 6.47 C -ATOM 323 C LEU A 210 23.807 18.731 49.910 1.00 7.39 C -ATOM 324 O LEU A 210 23.000 18.314 50.736 1.00 6.81 O -ATOM 325 CB LEU A 210 22.223 17.946 48.090 1.00 6.55 C -ATOM 326 CG LEU A 210 21.997 17.622 46.608 1.00 6.51 C -ATOM 327 CD1 LEU A 210 20.619 16.974 46.457 1.00 9.27 C -ATOM 328 CD2 LEU A 210 22.111 18.873 45.778 1.00 9.96 C -ATOM 329 N PRO A 211 24.864 19.483 50.246 1.00 8.28 N -ATOM 330 CA PRO A 211 25.109 19.826 51.653 1.00 10.26 C -ATOM 331 C PRO A 211 23.955 20.471 52.386 1.00 12.37 C -ATOM 332 O PRO A 211 23.808 20.263 53.606 1.00 13.53 O -ATOM 333 CB PRO A 211 26.337 20.732 51.588 1.00 13.15 C -ATOM 334 CG PRO A 211 27.064 20.210 50.373 1.00 12.85 C -ATOM 335 CD PRO A 211 25.952 19.971 49.384 1.00 8.74 C -ATOM 336 N ASP A 212 23.129 21.240 51.677 1.00 12.83 N -ATOM 337 CA ASP A 212 22.001 21.910 52.322 1.00 14.71 C -ATOM 338 C ASP A 212 20.941 20.929 52.770 1.00 17.08 C -ATOM 339 O ASP A 212 20.055 21.296 53.539 1.00 21.09 O -ATOM 340 CB ASP A 212 21.378 22.972 51.407 1.00 22.01 C -ATOM 341 CG ASP A 212 22.356 24.068 51.050 1.00 35.74 C -ATOM 342 OD1 ASP A 212 23.217 24.396 51.899 1.00 36.78 O -ATOM 343 OD2 ASP A 212 22.260 24.607 49.923 1.00 39.62 O -ATOM 344 N LEU A 213 21.027 19.699 52.285 1.00 13.40 N -ATOM 345 CA LEU A 213 20.117 18.637 52.682 1.00 12.92 C -ATOM 346 C LEU A 213 20.872 17.630 53.569 1.00 8.87 C -ATOM 347 O LEU A 213 20.347 16.562 53.899 1.00 15.13 O -ATOM 348 CB LEU A 213 19.574 17.897 51.453 1.00 15.56 C -ATOM 349 CG LEU A 213 18.662 18.649 50.477 1.00 20.43 C -ATOM 350 CD1 LEU A 213 18.244 17.720 49.331 1.00 18.11 C -ATOM 351 CD2 LEU A 213 17.427 19.135 51.223 1.00 21.32 C -ATOM 352 N GLY A 214 22.117 17.955 53.917 1.00 9.80 N -ATOM 353 CA GLY A 214 22.920 17.063 54.738 1.00 10.63 C -ATOM 354 C GLY A 214 23.437 15.860 53.961 1.00 9.82 C -ATOM 355 O GLY A 214 23.757 14.850 54.565 1.00 11.16 O -ATOM 356 N ILE A 215 23.545 15.980 52.626 1.00 7.74 N -ATOM 357 CA ILE A 215 23.990 14.880 51.760 1.00 8.48 C -ATOM 358 C ILE A 215 25.388 15.212 51.242 1.00 7.71 C -ATOM 359 O ILE A 215 25.579 16.192 50.502 1.00 8.49 O -ATOM 360 CB ILE A 215 23.005 14.692 50.570 1.00 9.04 C -ATOM 361 CG1 ILE A 215 21.643 14.219 51.107 1.00 11.28 C -ATOM 362 CG2 ILE A 215 23.586 13.694 49.573 1.00 10.94 C -ATOM 363 CD1 ILE A 215 20.528 14.198 50.052 1.00 13.32 C -ATOM 364 N TYR A 216 26.353 14.368 51.629 1.00 7.66 N -ATOM 365 CA TYR A 216 27.761 14.590 51.303 1.00 8.29 C -ATOM 366 C TYR A 216 28.419 13.552 50.400 1.00 11.13 C -ATOM 367 O TYR A 216 29.649 13.392 50.393 1.00 22.13 O -ATOM 368 CB TYR A 216 28.567 14.776 52.598 1.00 10.09 C -ATOM 369 CG TYR A 216 28.149 16.018 53.338 1.00 8.98 C -ATOM 370 CD1 TYR A 216 28.676 17.267 52.980 1.00 8.70 C -ATOM 371 CD2 TYR A 216 27.172 15.961 54.341 1.00 8.71 C -ATOM 372 CE1 TYR A 216 28.245 18.421 53.601 1.00 10.18 C -ATOM 373 CE2 TYR A 216 26.724 17.119 54.964 1.00 9.84 C -ATOM 374 CZ TYR A 216 27.270 18.339 54.592 1.00 9.08 C -ATOM 375 OH TYR A 216 26.923 19.516 55.219 1.00 10.69 O -ATOM 376 N GLU A 217 27.600 12.800 49.695 1.00 7.59 N -ATOM 377 CA GLU A 217 28.067 11.871 48.680 1.00 8.51 C -ATOM 378 C GLU A 217 27.295 12.326 47.431 1.00 8.64 C -ATOM 379 O GLU A 217 26.215 12.923 47.536 1.00 8.66 O -ATOM 380 CB GLU A 217 27.664 10.448 49.040 1.00 11.07 C -ATOM 381 CG GLU A 217 26.166 10.340 49.189 1.00 21.61 C -ATOM 382 CD GLU A 217 25.672 8.925 49.368 1.00 41.95 C -ATOM 383 OE1 GLU A 217 26.520 8.010 49.475 1.00 49.12 O -ATOM 384 OE2 GLU A 217 24.432 8.735 49.401 1.00 47.03 O -ATOM 385 N PRO A 218 27.811 12.025 46.244 1.00 7.31 N -ATOM 386 CA PRO A 218 27.096 12.454 45.036 1.00 7.64 C -ATOM 387 C PRO A 218 25.756 11.740 44.854 1.00 6.93 C -ATOM 388 O PRO A 218 25.680 10.506 44.963 1.00 9.23 O -ATOM 389 CB PRO A 218 28.065 12.102 43.890 1.00 8.76 C -ATOM 390 CG PRO A 218 29.415 12.001 44.588 1.00 10.57 C -ATOM 391 CD PRO A 218 29.062 11.343 45.901 1.00 8.48 C -ATOM 392 N VAL A 219 24.714 12.509 44.569 1.00 5.76 N -ATOM 393 CA VAL A 219 23.395 11.948 44.278 1.00 6.35 C -ATOM 394 C VAL A 219 22.926 12.560 42.952 1.00 5.08 C -ATOM 395 O VAL A 219 23.314 13.680 42.541 1.00 4.76 O -ATOM 396 CB VAL A 219 22.341 12.205 45.403 1.00 7.78 C -ATOM 397 CG1 VAL A 219 22.773 11.475 46.663 1.00 9.22 C -ATOM 398 CG2 VAL A 219 22.183 13.695 45.685 1.00 7.73 C -ATOM 399 N ARG A 220 22.087 11.810 42.258 1.00 5.66 N -ATOM 400 CA ARG A 220 21.637 12.196 40.950 1.00 5.89 C -ATOM 401 C ARG A 220 20.911 13.503 40.875 1.00 5.23 C -ATOM 402 O ARG A 220 20.022 13.760 41.672 1.00 5.90 O -ATOM 403 CB ARG A 220 20.740 11.096 40.413 1.00 6.40 C -ATOM 404 CG ARG A 220 20.124 11.402 39.063 1.00 7.27 C -ATOM 405 CD ARG A 220 19.169 10.308 38.630 1.00 9.10 C -ATOM 406 NE ARG A 220 19.762 8.975 38.599 1.00 9.44 N -ATOM 407 CZ ARG A 220 20.270 8.412 37.507 1.00 9.79 C -ATOM 408 NH1 ARG A 220 20.269 9.037 36.340 1.00 11.94 N -ATOM 409 NH2 ARG A 220 20.767 7.186 37.592 1.00 12.02 N -ATOM 410 N VAL A 221 21.279 14.314 39.886 1.00 4.83 N -ATOM 411 CA VAL A 221 20.583 15.563 39.609 1.00 6.67 C -ATOM 412 C VAL A 221 20.374 15.759 38.113 1.00 4.57 C -ATOM 413 O VAL A 221 21.095 15.182 37.281 1.00 6.33 O -ATOM 414 CB VAL A 221 21.333 16.815 40.185 1.00 3.98 C -ATOM 415 CG1 VAL A 221 21.364 16.717 41.712 1.00 5.47 C -ATOM 416 CG2 VAL A 221 22.713 16.946 39.607 1.00 6.44 C -ATOM 417 N CYS A 222 19.370 16.550 37.774 1.00 6.01 N -ATOM 418 CA CYS A 222 19.142 16.899 36.380 1.00 5.02 C -ATOM 419 C CYS A 222 20.209 17.899 35.909 1.00 6.50 C -ATOM 420 O CYS A 222 20.985 18.455 36.707 1.00 6.09 O -ATOM 421 CB CYS A 222 17.753 17.519 36.222 1.00 7.54 C -ATOM 422 SG CYS A 222 17.563 19.216 36.930 1.00 6.51 S -ATOM 423 N ASP A 223 20.270 18.091 34.593 1.00 6.81 N -ATOM 424 CA ASP A 223 21.264 18.982 34.021 1.00 7.76 C -ATOM 425 C ASP A 223 21.179 20.412 34.496 1.00 7.94 C -ATOM 426 O ASP A 223 22.198 21.088 34.650 1.00 8.74 O -ATOM 427 CB ASP A 223 21.220 18.952 32.501 1.00 9.40 C -ATOM 428 CG ASP A 223 21.560 17.587 31.942 1.00 10.75 C -ATOM 429 OD1 ASP A 223 22.285 16.842 32.638 1.00 10.82 O -ATOM 430 OD2 ASP A 223 21.128 17.263 30.793 1.00 14.30 O -ATOM 431 N SER A 224 19.964 20.904 34.718 1.00 8.22 N -ATOM 432 CA SER A 224 19.783 22.257 35.200 1.00 9.54 C -ATOM 433 C SER A 224 20.367 22.433 36.616 1.00 6.54 C -ATOM 434 O SER A 224 21.066 23.410 36.897 1.00 8.57 O -ATOM 435 CB SER A 224 18.299 22.618 35.204 1.00 10.39 C -ATOM 436 OG SER A 224 18.094 23.900 35.778 1.00 13.21 O -ATOM 437 N CYS A 225 20.048 21.498 37.517 1.00 6.61 N -ATOM 438 CA CYS A 225 20.552 21.566 38.878 1.00 4.38 C -ATOM 439 C CYS A 225 22.056 21.348 38.891 1.00 5.95 C -ATOM 440 O CYS A 225 22.753 21.950 39.695 1.00 5.93 O -ATOM 441 CB CYS A 225 19.841 20.541 39.772 1.00 5.09 C -ATOM 442 SG CYS A 225 18.088 21.009 40.057 1.00 6.45 S -ATOM 443 N PHE A 226 22.574 20.524 37.989 1.00 5.47 N -ATOM 444 CA PHE A 226 24.014 20.311 37.908 1.00 6.33 C -ATOM 445 C PHE A 226 24.709 21.620 37.507 1.00 6.50 C -ATOM 446 O PHE A 226 25.728 21.963 38.079 1.00 6.03 O -ATOM 447 CB PHE A 226 24.328 19.231 36.867 1.00 5.33 C -ATOM 448 CG PHE A 226 25.808 18.934 36.742 1.00 7.06 C -ATOM 449 CD1 PHE A 226 26.535 18.391 37.815 1.00 6.13 C -ATOM 450 CD2 PHE A 226 26.497 19.207 35.553 1.00 7.34 C -ATOM 451 CE1 PHE A 226 27.905 18.143 37.676 1.00 7.06 C -ATOM 452 CE2 PHE A 226 27.856 18.949 35.434 1.00 7.48 C -ATOM 453 CZ PHE A 226 28.551 18.429 36.480 1.00 7.07 C -ATOM 454 N GLU A 227 24.140 22.338 36.539 1.00 7.19 N -ATOM 455 CA GLU A 227 24.751 23.587 36.096 1.00 8.13 C -ATOM 456 C GLU A 227 24.752 24.582 37.238 1.00 7.53 C -ATOM 457 O GLU A 227 25.745 25.286 37.463 1.00 8.50 O -ATOM 458 CB GLU A 227 24.001 24.139 34.861 1.00 7.52 C -ATOM 459 CG GLU A 227 24.583 25.454 34.345 1.00 11.10 C -ATOM 460 CD GLU A 227 23.714 26.103 33.293 1.00 17.22 C -ATOM 461 OE1 GLU A 227 22.663 26.652 33.668 1.00 21.59 O -ATOM 462 OE2 GLU A 227 24.079 26.064 32.108 1.00 17.51 O -ATOM 463 N ASP A 228 23.651 24.654 37.976 1.00 7.62 N -ATOM 464 CA ASP A 228 23.554 25.588 39.097 1.00 8.33 C -ATOM 465 C ASP A 228 24.694 25.327 40.072 1.00 7.96 C -ATOM 466 O ASP A 228 25.333 26.256 40.571 1.00 8.98 O -ATOM 467 CB ASP A 228 22.245 25.394 39.887 1.00 10.56 C -ATOM 468 CG ASP A 228 21.010 25.835 39.134 1.00 13.53 C -ATOM 469 OD1 ASP A 228 21.128 26.548 38.131 1.00 14.50 O -ATOM 470 OD2 ASP A 228 19.897 25.462 39.581 1.00 16.52 O -ATOM 471 N TYR A 229 24.918 24.060 40.395 1.00 7.90 N -ATOM 472 CA TYR A 229 25.941 23.678 41.352 1.00 7.26 C -ATOM 473 C TYR A 229 27.324 23.975 40.820 1.00 7.34 C -ATOM 474 O TYR A 229 28.157 24.512 41.538 1.00 7.42 O -ATOM 475 CB TYR A 229 25.803 22.171 41.660 1.00 7.05 C -ATOM 476 CG TYR A 229 26.893 21.628 42.536 1.00 7.62 C -ATOM 477 CD1 TYR A 229 26.795 21.717 43.910 1.00 9.18 C -ATOM 478 CD2 TYR A 229 28.033 21.042 41.989 1.00 8.72 C -ATOM 479 CE1 TYR A 229 27.792 21.247 44.730 1.00 7.68 C -ATOM 480 CE2 TYR A 229 29.046 20.559 42.821 1.00 7.46 C -ATOM 481 CZ TYR A 229 28.916 20.666 44.179 1.00 7.01 C -ATOM 482 OH TYR A 229 29.905 20.137 44.994 1.00 9.73 O -ATOM 483 N GLU A 230 27.574 23.612 39.578 1.00 6.58 N -ATOM 484 CA GLU A 230 28.863 23.848 38.971 1.00 7.58 C -ATOM 485 C GLU A 230 29.173 25.334 38.932 1.00 6.58 C -ATOM 486 O GLU A 230 30.321 25.723 39.185 1.00 8.08 O -ATOM 487 CB GLU A 230 28.912 23.253 37.564 1.00 6.61 C -ATOM 488 CG GLU A 230 29.084 21.746 37.552 1.00 9.19 C -ATOM 489 CD GLU A 230 30.389 21.346 38.187 1.00 9.20 C -ATOM 490 OE1 GLU A 230 31.443 21.748 37.651 1.00 12.50 O -ATOM 491 OE2 GLU A 230 30.386 20.662 39.224 1.00 13.07 O -ATOM 492 N PHE A 231 28.182 26.165 38.626 1.00 6.84 N -ATOM 493 CA PHE A 231 28.439 27.605 38.616 1.00 6.60 C -ATOM 494 C PHE A 231 28.925 28.093 39.991 1.00 7.75 C -ATOM 495 O PHE A 231 29.840 28.942 40.082 1.00 8.63 O -ATOM 496 CB PHE A 231 27.181 28.378 38.237 1.00 8.00 C -ATOM 497 CG PHE A 231 26.907 28.424 36.754 1.00 7.20 C -ATOM 498 CD1 PHE A 231 27.790 27.933 35.824 1.00 8.70 C -ATOM 499 CD2 PHE A 231 25.725 28.973 36.311 1.00 8.56 C -ATOM 500 CE1 PHE A 231 27.477 27.992 34.441 1.00 10.47 C -ATOM 501 CE2 PHE A 231 25.424 29.029 34.956 1.00 11.13 C -ATOM 502 CZ PHE A 231 26.296 28.540 34.039 1.00 11.04 C -ATOM 503 N ILE A 232 28.319 27.594 41.069 1.00 7.13 N -ATOM 504 CA ILE A 232 28.712 27.998 42.413 1.00 8.33 C -ATOM 505 C ILE A 232 30.141 27.540 42.717 1.00 8.59 C -ATOM 506 O ILE A 232 30.953 28.313 43.262 1.00 11.63 O -ATOM 507 CB ILE A 232 27.716 27.430 43.459 1.00 11.09 C -ATOM 508 CG1 ILE A 232 26.385 28.178 43.333 1.00 12.16 C -ATOM 509 CG2 ILE A 232 28.309 27.516 44.871 1.00 14.04 C -ATOM 510 CD1 ILE A 232 25.284 27.654 44.185 1.00 19.24 C -ATOM 511 N VAL A 233 30.474 26.299 42.368 1.00 8.88 N -ATOM 512 CA VAL A 233 31.799 25.758 42.623 1.00 11.18 C -ATOM 513 C VAL A 233 32.931 26.537 41.970 1.00 11.13 C -ATOM 514 O VAL A 233 33.965 26.767 42.612 1.00 13.66 O -ATOM 515 CB VAL A 233 31.893 24.276 42.163 1.00 15.95 C -ATOM 516 CG1 VAL A 233 33.334 23.772 42.310 1.00 17.42 C -ATOM 517 CG2 VAL A 233 30.908 23.425 42.968 1.00 20.30 C -ATOM 518 N THR A 234 32.765 26.925 40.714 1.00 8.89 N -ATOM 519 CA THR A 234 33.832 27.624 40.023 1.00 9.51 C -ATOM 520 C THR A 234 33.685 29.135 39.961 1.00 9.47 C -ATOM 521 O THR A 234 34.460 29.814 39.271 1.00 10.05 O -ATOM 522 CB THR A 234 34.041 27.081 38.561 1.00 11.03 C -ATOM 523 OG1 THR A 234 32.800 27.064 37.832 1.00 9.76 O -ATOM 524 CG2 THR A 234 34.607 25.671 38.600 1.00 15.73 C -ATOM 525 N ASP A 235 32.715 29.677 40.681 1.00 7.29 N -ATOM 526 CA ASP A 235 32.525 31.116 40.631 1.00 8.56 C -ATOM 527 C ASP A 235 33.810 31.901 40.950 1.00 9.13 C -ATOM 528 O ASP A 235 34.333 31.696 42.046 1.00 11.00 O -ATOM 529 CB ASP A 235 31.428 31.509 41.606 1.00 9.56 C -ATOM 530 CG ASP A 235 31.027 32.944 41.405 1.00 10.41 C -ATOM 531 OD1 ASP A 235 31.922 33.815 41.296 1.00 10.71 O -ATOM 532 OD2 ASP A 235 29.841 33.224 41.259 1.00 12.52 O -TER 533 ASP A 235 -HETATM 534 ZN ZN A 300 16.916 19.183 39.167 1.00 5.81 ZN -HETATM 535 ZN ZN A 301 15.152 13.042 28.880 1.00 8.84 ZN -HETATM 536 O HOH A 1 11.899 19.763 37.981 1.00 21.60 O -HETATM 537 O HOH A 2 19.348 18.556 29.813 1.00 27.66 O -HETATM 538 O HOH A 3 5.931 5.876 34.633 1.00 25.69 O -HETATM 539 O HOH A 4 19.774 24.331 42.014 1.00 21.76 O -HETATM 540 O HOH A 5 26.272 15.632 31.331 1.00 26.51 O -HETATM 541 O HOH A 6 35.149 21.621 38.670 1.00 30.73 O -HETATM 542 O HOH A 7 22.298 29.064 42.643 1.00 26.72 O -HETATM 543 O HOH A 8 24.081 12.286 29.043 1.00 28.48 O -HETATM 544 O HOH A 9 11.802 14.592 49.668 1.00 28.54 O -HETATM 545 O HOH A 10 3.385 12.898 33.025 1.00 28.82 O -HETATM 546 O HOH A 11 4.770 13.825 31.068 1.00 28.91 O -HETATM 547 O HOH A 12 15.680 23.052 44.363 1.00 30.24 O -HETATM 548 O HOH A 13 30.511 29.949 45.416 1.00 31.53 O -HETATM 549 O HOH A 14 19.123 0.079 35.400 1.00 30.14 O -HETATM 550 O HOH A 15 16.975 5.812 24.617 1.00 29.13 O -HETATM 551 O HOH A 16 20.149 7.443 41.161 1.00 11.65 O -HETATM 552 O HOH A 17 22.886 15.344 35.262 1.00 12.14 O -HETATM 553 O HOH A 18 31.019 29.135 37.511 1.00 11.90 O -HETATM 554 O HOH A 19 5.983 5.893 31.219 1.00 26.60 O -HETATM 555 O HOH A 20 33.740 18.908 42.038 1.00 18.91 O -HETATM 556 O HOH A 21 26.707 10.348 38.097 1.00 16.63 O -HETATM 557 O HOH A 22 30.157 18.622 49.688 1.00 29.44 O -HETATM 558 O HOH A 23 15.040 7.642 22.575 1.00 19.19 O -HETATM 559 O HOH A 24 15.094 20.840 34.846 1.00 21.33 O -HETATM 560 O HOH A 25 24.527 20.821 33.059 1.00 18.51 O -HETATM 561 O HOH A 26 28.841 31.376 39.678 1.00 21.31 O -HETATM 562 O HOH A 27 25.198 8.435 34.854 1.00 25.25 O -HETATM 563 O HOH A 28 23.286 10.521 38.092 1.00 13.42 O -HETATM 564 O HOH A 29 6.381 2.321 29.587 1.00 28.47 O -HETATM 565 O HOH A 30 24.788 8.694 41.837 1.00 29.68 O -HETATM 566 O HOH A 31 22.792 14.928 31.820 1.00 16.03 O -HETATM 567 O HOH A 32 29.954 20.672 47.698 1.00 22.43 O -HETATM 568 O HOH A 33 10.621 -1.428 23.158 1.00 30.94 O -HETATM 569 O HOH A 34 30.815 18.904 33.146 1.00 22.22 O -HETATM 570 O HOH A 35 9.276 -1.533 28.905 1.00 29.51 O -HETATM 571 O HOH A 36 21.439 9.063 43.357 1.00 14.06 O -HETATM 572 O HOH A 37 30.302 16.490 33.795 1.00 21.52 O -HETATM 573 O HOH A 38 16.996 23.354 38.299 1.00 23.34 O -HETATM 574 O HOH A 39 28.652 23.042 48.080 1.00 24.43 O -HETATM 575 O HOH A 40 9.260 6.908 41.624 1.00 29.18 O -HETATM 576 O HOH A 41 16.578 11.983 24.938 1.00 22.99 O -HETATM 577 O HOH A 42 9.929 14.529 48.758 1.00 25.14 O -HETATM 578 O HOH A 43 15.622 15.141 47.327 1.00 19.64 O -HETATM 579 O HOH A 44 18.630 2.633 35.410 1.00 29.24 O -HETATM 580 O HOH A 45 10.305 -0.272 26.164 1.00 27.29 O -HETATM 581 O HOH A 46 16.694 14.574 23.381 1.00 29.19 O -HETATM 582 O HOH A 47 7.649 15.329 32.035 1.00 23.97 O -HETATM 583 O HOH A 48 14.609 19.832 51.784 1.00 28.56 O -HETATM 584 O HOH A 49 36.687 26.057 42.539 1.00 29.90 O -HETATM 585 O HOH A 50 23.657 22.254 48.834 1.00 23.46 O -HETATM 586 O HOH A 51 0.205 9.332 29.993 1.00 22.84 O -HETATM 587 O HOH A 52 6.945 15.954 29.716 1.00 24.51 O -HETATM 588 O HOH A 53 8.054 17.611 50.031 1.00 26.44 O -HETATM 589 O HOH A 54 16.416 8.776 27.095 1.00 26.83 O -HETATM 590 O HOH A 55 18.129 4.798 32.855 1.00 22.75 O -HETATM 591 O HOH A 56 37.314 23.672 41.298 1.00 26.82 O -HETATM 592 O HOH A 57 8.465 11.544 47.961 1.00 28.61 O -HETATM 593 O HOH A 58 18.463 17.575 32.813 1.00 19.88 O -HETATM 594 O HOH A 59 6.448 4.636 38.686 1.00 22.27 O -HETATM 595 O HOH A 60 24.147 29.347 40.366 1.00 27.72 O -HETATM 596 O HOH A 61 17.619 2.652 31.763 1.00 23.79 O -HETATM 597 O HOH A 62 19.549 22.101 45.247 1.00 29.75 O -HETATM 598 O HOH A 63 15.128 18.147 48.111 1.00 28.56 O -HETATM 599 O HOH A 64 17.842 7.861 28.702 1.00 14.01 O -HETATM 600 O HOH A 65 35.066 29.549 43.494 1.00 25.19 O -HETATM 601 O HOH A 66 22.197 13.014 56.800 1.00 28.80 O -HETATM 602 O HOH A 67 12.190 21.524 44.638 1.00 32.94 O -HETATM 603 O HOH A 68 6.738 13.600 47.248 1.00 20.57 O -HETATM 604 O HOH A 69 22.459 16.066 28.643 1.00 26.56 O -HETATM 605 O HOH A 70 24.719 21.390 46.489 1.00 11.46 O -HETATM 606 O HOH A 71 8.393 9.563 44.077 1.00 29.30 O -HETATM 607 O HOH A 72 17.084 12.680 49.038 1.00 29.51 O -HETATM 608 O HOH A 73 16.077 21.452 47.168 1.00 31.28 O -HETATM 609 O HOH A 74 20.501 15.992 25.832 1.00 32.99 O -HETATM 610 O HOH A 75 9.825 21.823 45.172 1.00 27.58 O -HETATM 611 O HOH A 76 32.167 13.224 52.477 1.00 27.31 O -HETATM 612 O HOH A 77 17.305 4.391 26.372 1.00 31.04 O -HETATM 613 O HOH A 78 8.492 20.052 44.443 1.00 20.94 O -HETATM 614 O HOH A 79 19.781 9.406 46.534 1.00 24.37 O -HETATM 615 O HOH A 80 29.124 7.435 47.465 1.00 31.18 O -HETATM 616 O HOH A 81 9.938 17.557 25.889 1.00 28.69 O -HETATM 617 O HOH A 82 33.010 20.011 39.767 1.00 21.08 O -HETATM 618 O HOH A 83 31.824 15.272 49.737 1.00 31.95 O -HETATM 619 O HOH A 84 21.896 21.899 42.528 1.00 19.07 O -HETATM 620 O HOH A 85 9.047 22.594 32.076 1.00 29.30 O -HETATM 621 O HOH A 86 28.235 31.995 42.972 1.00 28.33 O -HETATM 622 O HOH A 87 19.915 5.156 39.499 1.00 26.48 O -HETATM 623 O HOH A 88 27.747 7.842 41.700 1.00 29.87 O -HETATM 624 O HOH A 89 16.355 6.647 31.490 1.00 10.32 O -HETATM 625 O HOH A 90 17.507 -0.546 31.999 1.00 31.60 O -HETATM 626 O HOH A 91 23.026 22.402 44.778 1.00 18.18 O -HETATM 627 O HOH A 92 17.700 20.098 33.488 1.00 18.05 O -HETATM 628 O HOH A 94 21.244 8.162 45.727 1.00 25.90 O -HETATM 629 O HOH A 95 21.439 4.137 36.456 1.00 28.17 O -HETATM 630 O HOH A 96 18.446 4.892 29.550 1.00 26.81 O -HETATM 631 O HOH A 97 7.237 6.287 40.158 1.00 28.76 O -HETATM 632 O HOH A 99 12.359 20.092 34.968 1.00 27.84 O -HETATM 633 O HOH A 100 22.818 28.119 36.707 1.00 25.20 O -HETATM 634 O HOH A 101 27.726 8.403 45.107 1.00 29.61 O -HETATM 635 O HOH A 102 21.210 26.225 43.632 1.00 28.53 O -HETATM 636 O HOH A 103 14.624 21.221 53.143 1.00 29.14 O -HETATM 637 O HOH A 104 4.639 7.043 36.059 1.00 25.87 O -HETATM 638 O HOH A 105 18.253 14.537 53.565 1.00 29.76 O -HETATM 639 O HOH A 106 19.034 11.565 48.598 1.00 29.95 O -HETATM 640 O HOH A 107 17.013 23.394 53.956 1.00 31.67 O -HETATM 641 O HOH A 108 26.384 23.084 47.622 1.00 27.98 O -HETATM 642 O HOH A 109 8.361 19.373 31.600 1.00 28.40 O -HETATM 643 O HOH A 110 3.500 10.267 28.414 1.00 28.84 O -HETATM 644 O HOH A 111 11.093 21.358 41.673 1.00 27.54 O -CONECT 63 535 -CONECT 85 535 -CONECT 196 534 -CONECT 219 534 -CONECT 251 535 -CONECT 276 535 -CONECT 422 534 -CONECT 442 534 -CONECT 534 196 219 422 442 -CONECT 535 63 85 251 276 -MASTER 321 0 2 3 2 0 6 6 643 1 10 6 -END |