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|
HEADER DNA-BINDING PROTEIN 10-JAN-97 1RMD
TITLE RAG1 DIMERIZATION DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAG1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZINC-BINDING DIMERIZATION DOMAIN;
COMPND 5 SYNONYM: V(D)J RECOMBINATION ACTIVATING PROTEIN 1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: BL21
KEYWDS RAG1, V(D)J RECOMBINATION, ANTIBODY, MAD, RING FINGER, ZINC
KEYWDS 2 BINUCLEAR CLUSTER, ZINC FINGER, DNA-BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.F.BELLON,K.K.RODGERS,D.G.SCHATZ,J.E.COLEMAN,T.A.STEITZ
REVDAT 3 24-FEB-09 1RMD 1 VERSN
REVDAT 2 01-APR-03 1RMD 1 JRNL
REVDAT 1 23-JUL-97 1RMD 0
JRNL AUTH S.F.BELLON,K.K.RODGERS,D.G.SCHATZ,J.E.COLEMAN,
JRNL AUTH 2 T.A.STEITZ
JRNL TITL CRYSTAL STRUCTURE OF THE RAG1 DIMERIZATION DOMAIN
JRNL TITL 2 REVEALS MULTIPLE ZINC-BINDING MOTIFS INCLUDING A
JRNL TITL 3 NOVEL ZINC BINUCLEAR CLUSTER.
JRNL REF NAT.STRUCT.BIOL. V. 4 586 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9228952
JRNL DOI 10.1038/NSB0797-586
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 60.5
REMARK 3 NUMBER OF REFLECTIONS : 6970
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) : 0.209
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.600
REMARK 3 FREE R VALUE TEST SET COUNT : 668
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.20
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 29.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 372
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE : 0.2760
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 43
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.042
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 911
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 52
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.21
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.25
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 2.10
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.47
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PAR.WAT
REMARK 3 PARAMETER FILE 3 : PAR.ZN
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOP_116_117.ZN
REMARK 3 TOPOLOGY FILE 3 : TOP_118.ZN
REMARK 3 TOPOLOGY FILE 4 : TOP_119.ZN
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: LOCAL SCALING USING MAXSCALE WAS
REMARK 3 USED TO CORRECT THE HIGHLY ANISOTROPIC DATA. THE LOW OVERALL
REMARK 3 COMPLETION OF THE DATA REFLECT THIS ANISOTROPY.
REMARK 4
REMARK 4 1RMD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JUN-96
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.35
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE AREA DETECTOR
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 : 36957
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : 0.07200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.61000
REMARK 200 R SYM FOR SHELL (I) : 0.61000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: BAZFAZ
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5-10 % PEG 4K, 100MM HEPES, PH 7.5,
REMARK 280 10% ETHYLENE GLYCOL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.62000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 32.81000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 32.81000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 65.62000
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: DIMERIC
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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 65.62000
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 ILE A 28 -66.61 -101.88
REMARK 500 LYS A 55 -72.99 -78.45
REMARK 500 ASP A 95 -4.35 68.78
REMARK 500 ASN A 97 54.10 -119.95
REMARK 500 SER A 111 -9.28 -57.49
REMARK 500 SER A 115 -87.31 -68.59
REMARK 500
REMARK 500 REMARK: NULL
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 117 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 2 SG
REMARK 620 2 HIS A 6 ND1 114.1
REMARK 620 3 CYS A 29 SG 110.1 111.3
REMARK 620 4 HIS A 31 ND1 106.3 120.9 92.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 118 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 26 SG
REMARK 620 2 CYS A 29 SG 99.2
REMARK 620 3 CYS A 46 SG 106.2 106.3
REMARK 620 4 CYS A 49 SG 122.8 107.6 112.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 119 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 41 SG
REMARK 620 2 HIS A 43 ND1 99.6
REMARK 620 3 CYS A 61 SG 106.8 114.7
REMARK 620 4 CYS A 64 SG 101.0 113.5 118.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 120 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 91 SG
REMARK 620 2 CYS A 96 SG 114.3
REMARK 620 3 HIS A 108 NE2 99.3 111.3
REMARK 620 4 HIS A 112 NE2 105.0 119.8 104.8
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 117
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 118
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 119
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 120
DBREF 1RMD A 1 116 UNP P15919 RAG1_MOUSE 265 380
SEQRES 1 A 116 ASN CYS SER LYS ILE HIS LEU SER THR LYS LEU LEU ALA
SEQRES 2 A 116 VAL ASP PHE PRO ALA HIS PHE VAL LYS SER ILE SER CYS
SEQRES 3 A 116 GLN ILE CYS GLU HIS ILE LEU ALA ASP PRO VAL GLU THR
SEQRES 4 A 116 SER CYS LYS HIS LEU PHE CYS ARG ILE CYS ILE LEU ARG
SEQRES 5 A 116 CYS LEU LYS VAL MET GLY SER TYR CYS PRO SER CYS ARG
SEQRES 6 A 116 TYR PRO CYS PHE PRO THR ASP LEU GLU SER PRO VAL LYS
SEQRES 7 A 116 SER PHE LEU ASN ILE LEU ASN SER LEU MET VAL LYS CYS
SEQRES 8 A 116 PRO ALA GLN ASP CYS ASN GLU GLU VAL SER LEU GLU LYS
SEQRES 9 A 116 TYR ASN HIS HIS VAL SER SER HIS LYS GLU SER LYS
HET ZN A 117 1
HET ZN A 118 1
HET ZN A 119 1
HET ZN A 120 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 4(ZN 2+)
FORMUL 6 HOH *52(H2 O)
HELIX 1 1 CYS A 2 LYS A 4 5 3
HELIX 2 2 THR A 9 LEU A 11 5 3
HELIX 3 3 ALA A 18 SER A 23 1 6
HELIX 4 4 ARG A 47 VAL A 56 1 10
HELIX 5 5 PRO A 70 ASP A 72 5 3
HELIX 6 6 LYS A 78 SER A 86 1 9
HELIX 7 7 LEU A 102 SER A 110 1 9
SHEET 1 A 2 PRO A 36 GLU A 38 0
SHEET 2 A 2 LEU A 44 CYS A 46 -1 N PHE A 45 O VAL A 37
SHEET 1 B 2 MET A 88 LYS A 90 0
SHEET 2 B 2 GLU A 99 SER A 101 -1 N VAL A 100 O VAL A 89
LINK ZN ZN A 117 SG CYS A 2 1555 1555 2.31
LINK ZN ZN A 117 ND1 HIS A 6 1555 1555 1.87
LINK ZN ZN A 117 SG CYS A 29 1555 1555 2.35
LINK ZN ZN A 117 ND1 HIS A 31 1555 1555 2.08
LINK ZN ZN A 118 SG CYS A 26 1555 1555 2.33
LINK ZN ZN A 118 SG CYS A 29 1555 1555 2.32
LINK ZN ZN A 118 SG CYS A 46 1555 1555 2.24
LINK ZN ZN A 118 SG CYS A 49 1555 1555 2.26
LINK ZN ZN A 119 SG CYS A 41 1555 1555 2.37
LINK ZN ZN A 119 ND1 HIS A 43 1555 1555 2.07
LINK ZN ZN A 119 SG CYS A 61 1555 1555 2.28
LINK ZN ZN A 119 SG CYS A 64 1555 1555 2.25
LINK ZN ZN A 120 SG CYS A 91 1555 1555 2.31
LINK ZN ZN A 120 SG CYS A 96 1555 1555 2.39
LINK ZN ZN A 120 NE2 HIS A 108 1555 1555 1.99
LINK ZN ZN A 120 NE2 HIS A 112 1555 1555 1.96
SITE 1 AC1 4 CYS A 2 HIS A 6 CYS A 29 HIS A 31
SITE 1 AC2 4 CYS A 26 CYS A 29 CYS A 46 CYS A 49
SITE 1 AC3 4 CYS A 41 HIS A 43 CYS A 61 CYS A 64
SITE 1 AC4 4 CYS A 91 CYS A 96 HIS A 108 HIS A 112
CRYST1 57.580 57.580 98.430 90.00 90.00 120.00 P 32 2 1 6
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 0.017367 0.010027 0.000000 0.00000
SCALE2 0.000000 0.020054 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010160 0.00000
ATOM 1 N ASN A 1 0.736 27.946 53.948 1.00 37.25 N
ATOM 2 CA ASN A 1 0.517 27.822 52.473 1.00 36.11 C
ATOM 3 C ASN A 1 -0.262 28.992 51.864 1.00 33.55 C
ATOM 4 O ASN A 1 -0.528 29.997 52.539 1.00 33.59 O
ATOM 5 CB ASN A 1 -0.208 26.506 52.166 1.00 40.18 C
ATOM 6 CG ASN A 1 -1.431 26.291 53.037 1.00 42.71 C
ATOM 7 OD1 ASN A 1 -1.816 27.161 53.820 1.00 49.46 O
ATOM 8 ND2 ASN A 1 -2.048 25.118 52.909 1.00 45.85 N
ATOM 9 N CYS A 2 -0.610 28.869 50.581 1.00 28.40 N
ATOM 10 CA CYS A 2 -1.380 29.916 49.897 1.00 28.25 C
ATOM 11 C CYS A 2 -2.842 29.920 50.343 1.00 26.42 C
ATOM 12 O CYS A 2 -3.631 30.761 49.917 1.00 27.83 O
ATOM 13 CB CYS A 2 -1.295 29.758 48.373 1.00 26.23 C
ATOM 14 SG CYS A 2 -1.810 28.164 47.735 1.00 21.06 S
ATOM 15 N SER A 3 -3.192 28.949 51.180 1.00 25.33 N
ATOM 16 CA SER A 3 -4.537 28.800 51.725 1.00 25.26 C
ATOM 17 C SER A 3 -4.828 29.958 52.680 1.00 24.36 C
ATOM 18 O SER A 3 -5.990 30.273 52.955 1.00 24.59 O
ATOM 19 CB SER A 3 -4.645 27.456 52.463 1.00 26.33 C
ATOM 20 OG SER A 3 -5.976 26.966 52.533 1.00 32.06 O
ATOM 21 N LYS A 4 -3.765 30.578 53.186 1.00 24.65 N
ATOM 22 CA LYS A 4 -3.868 31.729 54.098 1.00 26.89 C
ATOM 23 C LYS A 4 -4.240 32.978 53.319 1.00 27.65 C
ATOM 24 O LYS A 4 -4.723 33.954 53.896 1.00 27.77 O
ATOM 25 CB LYS A 4 -2.520 32.021 54.772 1.00 23.67 C
ATOM 26 CG LYS A 4 -2.152 31.070 55.872 1.00 27.40 C
ATOM 27 CD LYS A 4 -0.895 31.523 56.584 1.00 22.76 C
ATOM 28 CE LYS A 4 -0.979 31.169 58.032 1.00 9.82 C
ATOM 29 NZ LYS A 4 0.281 31.498 58.675 1.00 24.93 N
ATOM 30 N ILE A 5 -3.965 32.943 52.016 1.00 26.14 N
ATOM 31 CA ILE A 5 -4.198 34.069 51.130 1.00 26.27 C
ATOM 32 C ILE A 5 -5.186 33.814 49.995 1.00 26.60 C
ATOM 33 O ILE A 5 -5.635 34.767 49.335 1.00 21.76 O
ATOM 34 CB ILE A 5 -2.856 34.564 50.508 1.00 28.67 C
ATOM 35 CG1 ILE A 5 -2.014 33.379 50.017 1.00 30.18 C
ATOM 36 CG2 ILE A 5 -2.080 35.394 51.518 1.00 32.08 C
ATOM 37 CD1 ILE A 5 -0.761 33.774 49.275 1.00 31.21 C
ATOM 38 N HIS A 6 -5.517 32.540 49.771 1.00 25.18 N
ATOM 39 CA HIS A 6 -6.431 32.157 48.697 1.00 22.43 C
ATOM 40 C HIS A 6 -7.803 31.677 49.167 1.00 20.05 C
ATOM 41 O HIS A 6 -7.946 31.192 50.281 1.00 14.95 O
ATOM 42 CB HIS A 6 -5.767 31.090 47.835 1.00 19.92 C
ATOM 43 CG HIS A 6 -4.604 31.595 47.045 1.00 20.06 C
ATOM 44 ND1 HIS A 6 -3.770 30.734 46.359 1.00 16.46 N
ATOM 45 CD2 HIS A 6 -4.162 32.867 46.886 1.00 20.79 C
ATOM 46 CE1 HIS A 6 -2.840 31.497 45.817 1.00 20.77 C
ATOM 47 NE2 HIS A 6 -3.032 32.800 46.107 1.00 21.53 N
ATOM 48 N LEU A 7 -8.815 31.839 48.318 1.00 15.72 N
ATOM 49 CA LEU A 7 -10.157 31.405 48.662 1.00 20.87 C
ATOM 50 C LEU A 7 -10.457 29.988 48.136 1.00 21.13 C
ATOM 51 O LEU A 7 -10.072 29.643 47.015 1.00 20.29 O
ATOM 52 CB LEU A 7 -11.184 32.403 48.120 1.00 21.07 C
ATOM 53 CG LEU A 7 -12.043 33.166 49.138 1.00 24.13 C
ATOM 54 CD1 LEU A 7 -11.212 33.711 50.331 1.00 16.06 C
ATOM 55 CD2 LEU A 7 -12.753 34.297 48.404 1.00 25.51 C
ATOM 56 N SER A 8 -11.105 29.168 48.966 1.00 16.69 N
ATOM 57 CA SER A 8 -11.479 27.798 48.601 1.00 14.82 C
ATOM 58 C SER A 8 -12.720 27.839 47.729 1.00 17.01 C
ATOM 59 O SER A 8 -13.635 28.642 47.978 1.00 18.20 O
ATOM 60 CB SER A 8 -11.803 26.970 49.852 1.00 16.93 C
ATOM 61 OG SER A 8 -12.551 25.810 49.505 1.00 15.42 O
ATOM 62 N THR A 9 -12.794 26.958 46.736 1.00 14.02 N
ATOM 63 CA THR A 9 -13.961 26.958 45.877 1.00 14.95 C
ATOM 64 C THR A 9 -15.260 26.583 46.626 1.00 17.29 C
ATOM 65 O THR A 9 -16.373 26.810 46.127 1.00 19.28 O
ATOM 66 CB THR A 9 -13.771 26.050 44.653 1.00 16.07 C
ATOM 67 OG1 THR A 9 -13.493 24.718 45.080 1.00 15.85 O
ATOM 68 CG2 THR A 9 -12.620 26.551 43.794 1.00 19.06 C
ATOM 69 N LYS A 10 -15.145 26.061 47.838 1.00 16.13 N
ATOM 70 CA LYS A 10 -16.353 25.698 48.550 1.00 21.31 C
ATOM 71 C LYS A 10 -17.042 26.947 49.091 1.00 19.86 C
ATOM 72 O LYS A 10 -18.159 26.860 49.595 1.00 21.29 O
ATOM 73 CB LYS A 10 -16.088 24.635 49.636 1.00 27.45 C
ATOM 74 CG LYS A 10 -15.299 25.115 50.841 1.00 42.69 C
ATOM 75 CD LYS A 10 -14.541 23.960 51.486 1.00 51.68 C
ATOM 76 CE LYS A 10 -13.586 24.459 52.574 1.00 55.89 C
ATOM 77 NZ LYS A 10 -12.623 23.389 53.000 1.00 56.88 N
ATOM 78 N LEU A 11 -16.404 28.113 48.943 1.00 17.01 N
ATOM 79 CA LEU A 11 -17.018 29.358 49.388 1.00 16.12 C
ATOM 80 C LEU A 11 -17.931 29.934 48.303 1.00 20.10 C
ATOM 81 O LEU A 11 -18.604 30.946 48.521 1.00 15.13 O
ATOM 82 CB LEU A 11 -15.972 30.393 49.805 1.00 15.55 C
ATOM 83 CG LEU A 11 -15.092 30.032 51.013 1.00 21.51 C
ATOM 84 CD1 LEU A 11 -14.175 31.206 51.395 1.00 18.27 C
ATOM 85 CD2 LEU A 11 -15.985 29.648 52.187 1.00 17.71 C
ATOM 86 N LEU A 12 -17.952 29.293 47.130 1.00 21.46 N
ATOM 87 CA LEU A 12 -18.799 29.750 46.024 1.00 19.76 C
ATOM 88 C LEU A 12 -20.258 29.611 46.414 1.00 22.19 C
ATOM 89 O LEU A 12 -20.693 28.546 46.865 1.00 18.17 O
ATOM 90 CB LEU A 12 -18.557 28.910 44.773 1.00 19.64 C
ATOM 91 CG LEU A 12 -17.283 29.202 43.975 1.00 25.00 C
ATOM 92 CD1 LEU A 12 -17.075 28.155 42.870 1.00 18.26 C
ATOM 93 CD2 LEU A 12 -17.348 30.630 43.422 1.00 18.28 C
ATOM 94 N ALA A 13 -21.016 30.681 46.210 1.00 21.09 N
ATOM 95 CA ALA A 13 -22.434 30.692 46.526 1.00 23.83 C
ATOM 96 C ALA A 13 -23.206 29.716 45.653 1.00 25.32 C
ATOM 97 O ALA A 13 -24.001 28.914 46.136 1.00 27.91 O
ATOM 98 CB ALA A 13 -22.992 32.093 46.339 1.00 22.64 C
ATOM 99 N VAL A 14 -22.959 29.789 44.358 1.00 24.82 N
ATOM 100 CA VAL A 14 -23.652 28.954 43.399 1.00 25.61 C
ATOM 101 C VAL A 14 -23.058 27.569 43.247 1.00 24.14 C
ATOM 102 O VAL A 14 -21.842 27.409 43.246 1.00 25.49 O
ATOM 103 CB VAL A 14 -23.646 29.630 42.033 1.00 25.53 C
ATOM 104 CG1 VAL A 14 -24.455 28.823 41.050 1.00 24.61 C
ATOM 105 CG2 VAL A 14 -24.195 31.039 42.163 1.00 24.64 C
ATOM 106 N ASP A 15 -23.925 26.580 43.060 1.00 22.37 N
ATOM 107 CA ASP A 15 -23.492 25.199 42.858 1.00 24.36 C
ATOM 108 C ASP A 15 -23.260 24.916 41.355 1.00 23.63 C
ATOM 109 O ASP A 15 -24.094 24.284 40.681 1.00 25.06 O
ATOM 110 CB ASP A 15 -24.547 24.246 43.430 1.00 30.13 C
ATOM 111 CG ASP A 15 -24.080 22.803 43.449 1.00 35.84 C
ATOM 112 OD1 ASP A 15 -22.853 22.573 43.373 1.00 37.65 O
ATOM 113 OD2 ASP A 15 -24.939 21.897 43.524 1.00 39.22 O
ATOM 114 N PHE A 16 -22.118 25.354 40.835 1.00 19.65 N
ATOM 115 CA PHE A 16 -21.792 25.184 39.412 1.00 18.42 C
ATOM 116 C PHE A 16 -21.395 23.749 39.012 1.00 17.84 C
ATOM 117 O PHE A 16 -21.055 22.930 39.880 1.00 16.49 O
ATOM 118 CB PHE A 16 -20.616 26.109 39.058 1.00 21.05 C
ATOM 119 CG PHE A 16 -20.948 27.584 39.046 1.00 15.67 C
ATOM 120 CD1 PHE A 16 -21.869 28.100 38.152 1.00 16.76 C
ATOM 121 CD2 PHE A 16 -20.293 28.457 39.908 1.00 16.73 C
ATOM 122 CE1 PHE A 16 -22.138 29.470 38.105 1.00 20.65 C
ATOM 123 CE2 PHE A 16 -20.550 29.827 39.875 1.00 21.29 C
ATOM 124 CZ PHE A 16 -21.477 30.339 38.970 1.00 17.79 C
ATOM 125 N PRO A 17 -21.451 23.414 37.691 1.00 15.95 N
ATOM 126 CA PRO A 17 -21.067 22.067 37.192 1.00 9.51 C
ATOM 127 C PRO A 17 -19.575 21.907 37.512 1.00 13.85 C
ATOM 128 O PRO A 17 -18.854 22.914 37.570 1.00 14.71 O
ATOM 129 CB PRO A 17 -21.296 22.183 35.695 1.00 11.22 C
ATOM 130 CG PRO A 17 -22.484 23.119 35.636 1.00 9.10 C
ATOM 131 CD PRO A 17 -22.116 24.201 36.633 1.00 6.31 C
ATOM 132 N ALA A 18 -19.106 20.677 37.727 1.00 11.55 N
ATOM 133 CA ALA A 18 -17.702 20.468 38.119 1.00 13.58 C
ATOM 134 C ALA A 18 -16.620 20.945 37.149 1.00 12.16 C
ATOM 135 O ALA A 18 -15.547 21.409 37.594 1.00 11.21 O
ATOM 136 CB ALA A 18 -17.442 19.021 38.486 1.00 12.60 C
ATOM 137 N HIS A 19 -16.872 20.833 35.846 1.00 4.09 N
ATOM 138 CA HIS A 19 -15.852 21.259 34.893 1.00 6.69 C
ATOM 139 C HIS A 19 -15.730 22.774 34.877 1.00 9.50 C
ATOM 140 O HIS A 19 -14.634 23.300 34.702 1.00 13.04 O
ATOM 141 CB HIS A 19 -16.082 20.661 33.519 1.00 4.91 C
ATOM 142 CG HIS A 19 -15.850 19.170 33.452 1.00 13.27 C
ATOM 143 ND1 HIS A 19 -14.915 18.519 34.232 1.00 18.73 N
ATOM 144 CD2 HIS A 19 -16.442 18.205 32.700 1.00 12.61 C
ATOM 145 CE1 HIS A 19 -14.941 17.220 33.970 1.00 14.24 C
ATOM 146 NE2 HIS A 19 -15.858 17.005 33.041 1.00 19.91 N
ATOM 147 N PHE A 20 -16.824 23.473 35.162 1.00 8.11 N
ATOM 148 CA PHE A 20 -16.767 24.922 35.196 1.00 13.45 C
ATOM 149 C PHE A 20 -15.997 25.352 36.453 1.00 14.14 C
ATOM 150 O PHE A 20 -15.194 26.282 36.402 1.00 13.12 O
ATOM 151 CB PHE A 20 -18.158 25.556 35.177 1.00 11.67 C
ATOM 152 CG PHE A 20 -18.139 27.052 35.366 1.00 15.45 C
ATOM 153 CD1 PHE A 20 -17.752 27.897 34.325 1.00 14.62 C
ATOM 154 CD2 PHE A 20 -18.456 27.611 36.591 1.00 9.48 C
ATOM 155 CE1 PHE A 20 -17.679 29.285 34.505 1.00 10.89 C
ATOM 156 CE2 PHE A 20 -18.386 29.000 36.780 1.00 15.46 C
ATOM 157 CZ PHE A 20 -17.995 29.835 35.732 1.00 5.13 C
ATOM 158 N VAL A 21 -16.253 24.682 37.573 1.00 12.16 N
ATOM 159 CA VAL A 21 -15.570 24.996 38.811 1.00 13.87 C
ATOM 160 C VAL A 21 -14.059 24.831 38.618 1.00 19.59 C
ATOM 161 O VAL A 21 -13.233 25.612 39.139 1.00 15.82 O
ATOM 162 CB VAL A 21 -15.994 24.058 39.934 1.00 9.26 C
ATOM 163 CG1 VAL A 21 -15.089 24.276 41.164 1.00 13.80 C
ATOM 164 CG2 VAL A 21 -17.429 24.327 40.316 1.00 13.03 C
ATOM 165 N LYS A 22 -13.713 23.783 37.880 1.00 18.69 N
ATOM 166 CA LYS A 22 -12.330 23.463 37.587 1.00 19.48 C
ATOM 167 C LYS A 22 -11.679 24.575 36.725 1.00 19.02 C
ATOM 168 O LYS A 22 -10.495 24.933 36.920 1.00 10.21 O
ATOM 169 CB LYS A 22 -12.308 22.122 36.862 1.00 26.95 C
ATOM 170 CG LYS A 22 -10.950 21.647 36.422 1.00 31.56 C
ATOM 171 CD LYS A 22 -10.842 21.625 34.913 1.00 36.46 C
ATOM 172 CE LYS A 22 -9.507 21.058 34.526 1.00 40.89 C
ATOM 173 NZ LYS A 22 -9.382 19.748 35.163 1.00 45.93 N
ATOM 174 N SER A 23 -12.484 25.141 35.815 1.00 14.81 N
ATOM 175 CA SER A 23 -12.033 26.192 34.902 1.00 15.27 C
ATOM 176 C SER A 23 -11.653 27.479 35.607 1.00 15.56 C
ATOM 177 O SER A 23 -10.838 28.218 35.098 1.00 9.87 O
ATOM 178 CB SER A 23 -13.083 26.502 33.835 1.00 15.11 C
ATOM 179 OG SER A 23 -14.182 27.243 34.349 1.00 20.08 O
ATOM 180 N ILE A 24 -12.270 27.772 36.750 1.00 14.87 N
ATOM 181 CA ILE A 24 -11.922 28.993 37.466 1.00 10.74 C
ATOM 182 C ILE A 24 -10.986 28.758 38.656 1.00 12.38 C
ATOM 183 O ILE A 24 -10.775 29.659 39.483 1.00 13.44 O
ATOM 184 CB ILE A 24 -13.191 29.813 37.840 1.00 13.14 C
ATOM 185 CG1 ILE A 24 -14.215 28.952 38.626 1.00 6.63 C
ATOM 186 CG2 ILE A 24 -13.841 30.307 36.542 1.00 12.80 C
ATOM 187 CD1 ILE A 24 -13.811 28.604 40.086 1.00 2.81 C
ATOM 188 N SER A 25 -10.427 27.546 38.727 1.00 11.49 N
ATOM 189 CA SER A 25 -9.492 27.156 39.790 1.00 15.12 C
ATOM 190 C SER A 25 -8.010 27.110 39.327 1.00 14.28 C
ATOM 191 O SER A 25 -7.709 26.885 38.159 1.00 13.70 O
ATOM 192 CB SER A 25 -9.875 25.781 40.360 1.00 12.25 C
ATOM 193 OG SER A 25 -11.225 25.743 40.795 1.00 18.74 O
ATOM 194 N CYS A 26 -7.093 27.347 40.253 1.00 15.10 N
ATOM 195 CA CYS A 26 -5.668 27.287 39.953 1.00 17.94 C
ATOM 196 C CYS A 26 -5.309 25.814 39.806 1.00 18.73 C
ATOM 197 O CYS A 26 -5.532 25.030 40.716 1.00 18.49 O
ATOM 198 CB CYS A 26 -4.859 27.914 41.096 1.00 16.32 C
ATOM 199 SG CYS A 26 -3.126 27.486 41.043 1.00 17.54 S
ATOM 200 N GLN A 27 -4.737 25.436 38.667 1.00 26.19 N
ATOM 201 CA GLN A 27 -4.403 24.027 38.423 1.00 26.18 C
ATOM 202 C GLN A 27 -3.303 23.405 39.287 1.00 25.49 C
ATOM 203 O GLN A 27 -3.081 22.195 39.229 1.00 26.55 O
ATOM 204 CB GLN A 27 -4.185 23.765 36.933 1.00 26.70 C
ATOM 205 CG GLN A 27 -5.431 24.019 36.077 1.00 29.57 C
ATOM 206 CD GLN A 27 -6.675 23.351 36.634 1.00 29.07 C
ATOM 207 OE1 GLN A 27 -6.839 22.140 36.542 1.00 35.32 O
ATOM 208 NE2 GLN A 27 -7.567 24.144 37.198 1.00 30.79 N
ATOM 209 N ILE A 28 -2.654 24.237 40.103 1.00 23.88 N
ATOM 210 CA ILE A 28 -1.632 23.791 41.058 1.00 19.87 C
ATOM 211 C ILE A 28 -2.243 23.732 42.472 1.00 16.76 C
ATOM 212 O ILE A 28 -2.452 22.670 43.009 1.00 16.39 O
ATOM 213 CB ILE A 28 -0.415 24.741 41.079 1.00 18.25 C
ATOM 214 CG1 ILE A 28 0.430 24.512 39.825 1.00 18.88 C
ATOM 215 CG2 ILE A 28 0.442 24.510 42.329 1.00 20.96 C
ATOM 216 CD1 ILE A 28 1.497 25.571 39.599 1.00 20.30 C
ATOM 217 N CYS A 29 -2.602 24.882 43.023 1.00 19.20 N
ATOM 218 CA CYS A 29 -3.154 24.959 44.361 1.00 19.74 C
ATOM 219 C CYS A 29 -4.640 24.635 44.509 1.00 22.70 C
ATOM 220 O CYS A 29 -5.101 24.404 45.626 1.00 28.44 O
ATOM 221 CB CYS A 29 -2.827 26.328 44.994 1.00 20.14 C
ATOM 222 SG CYS A 29 -3.813 27.775 44.505 1.00 19.27 S
ATOM 223 N GLU A 30 -5.389 24.619 43.407 1.00 22.26 N
ATOM 224 CA GLU A 30 -6.834 24.320 43.438 1.00 21.68 C
ATOM 225 C GLU A 30 -7.766 25.358 44.070 1.00 20.23 C
ATOM 226 O GLU A 30 -8.969 25.140 44.201 1.00 19.73 O
ATOM 227 CB GLU A 30 -7.091 22.952 44.058 1.00 21.41 C
ATOM 228 CG GLU A 30 -6.682 21.837 43.134 1.00 29.58 C
ATOM 229 CD GLU A 30 -6.939 20.474 43.707 1.00 34.94 C
ATOM 230 OE1 GLU A 30 -7.954 20.283 44.412 1.00 45.72 O
ATOM 231 OE2 GLU A 30 -6.125 19.581 43.439 1.00 37.75 O
ATOM 232 N HIS A 31 -7.225 26.494 44.470 1.00 18.27 N
ATOM 233 CA HIS A 31 -8.075 27.527 45.049 1.00 20.61 C
ATOM 234 C HIS A 31 -8.700 28.317 43.897 1.00 19.02 C
ATOM 235 O HIS A 31 -8.405 28.037 42.722 1.00 20.78 O
ATOM 236 CB HIS A 31 -7.222 28.460 45.911 1.00 17.40 C
ATOM 237 CG HIS A 31 -6.631 27.791 47.107 1.00 17.29 C
ATOM 238 ND1 HIS A 31 -5.281 27.815 47.337 1.00 21.35 N
ATOM 239 CD2 HIS A 31 -7.263 27.225 48.160 1.00 16.10 C
ATOM 240 CE1 HIS A 31 -5.124 27.271 48.530 1.00 20.56 C
ATOM 241 NE2 HIS A 31 -6.298 26.900 49.064 1.00 15.53 N
ATOM 242 N ILE A 32 -9.596 29.254 44.214 1.00 13.80 N
ATOM 243 CA ILE A 32 -10.150 30.108 43.160 1.00 16.38 C
ATOM 244 C ILE A 32 -8.932 30.925 42.662 1.00 19.63 C
ATOM 245 O ILE A 32 -8.165 31.474 43.477 1.00 16.35 O
ATOM 246 CB ILE A 32 -11.200 31.096 43.696 1.00 11.44 C
ATOM 247 CG1 ILE A 32 -12.365 30.336 44.321 1.00 16.73 C
ATOM 248 CG2 ILE A 32 -11.706 31.976 42.567 1.00 5.14 C
ATOM 249 CD1 ILE A 32 -13.426 31.240 44.939 1.00 17.57 C
ATOM 250 N LEU A 33 -8.707 30.958 41.352 1.00 18.06 N
ATOM 251 CA LEU A 33 -7.554 31.704 40.813 1.00 19.44 C
ATOM 252 C LEU A 33 -7.363 33.088 41.448 1.00 17.05 C
ATOM 253 O LEU A 33 -8.299 33.892 41.526 1.00 15.30 O
ATOM 254 CB LEU A 33 -7.692 31.895 39.293 1.00 22.36 C
ATOM 255 CG LEU A 33 -7.565 30.666 38.401 1.00 22.49 C
ATOM 256 CD1 LEU A 33 -8.308 30.888 37.094 1.00 21.72 C
ATOM 257 CD2 LEU A 33 -6.111 30.370 38.166 1.00 19.58 C
ATOM 258 N ALA A 34 -6.150 33.366 41.898 1.00 13.30 N
ATOM 259 CA ALA A 34 -5.869 34.673 42.479 1.00 18.80 C
ATOM 260 C ALA A 34 -4.801 35.234 41.573 1.00 15.86 C
ATOM 261 O ALA A 34 -3.718 34.671 41.507 1.00 24.18 O
ATOM 262 CB ALA A 34 -5.345 34.525 43.918 1.00 16.71 C
ATOM 263 N ASP A 35 -5.107 36.315 40.858 1.00 20.29 N
ATOM 264 CA ASP A 35 -4.176 36.951 39.896 1.00 20.17 C
ATOM 265 C ASP A 35 -3.783 35.914 38.870 1.00 20.39 C
ATOM 266 O ASP A 35 -2.612 35.524 38.779 1.00 22.70 O
ATOM 267 CB ASP A 35 -2.920 37.459 40.612 1.00 24.63 C
ATOM 268 CG ASP A 35 -2.094 38.407 39.756 1.00 27.49 C
ATOM 269 OD1 ASP A 35 -2.608 38.892 38.727 1.00 24.45 O
ATOM 270 OD2 ASP A 35 -0.929 38.673 40.125 1.00 31.17 O
ATOM 271 N PRO A 36 -4.756 35.443 38.066 1.00 21.38 N
ATOM 272 CA PRO A 36 -4.501 34.417 37.041 1.00 18.55 C
ATOM 273 C PRO A 36 -3.610 34.824 35.890 1.00 18.95 C
ATOM 274 O PRO A 36 -3.603 35.973 35.480 1.00 21.40 O
ATOM 275 CB PRO A 36 -5.909 34.104 36.537 1.00 17.66 C
ATOM 276 CG PRO A 36 -6.590 35.445 36.623 1.00 16.88 C
ATOM 277 CD PRO A 36 -6.151 35.919 37.993 1.00 15.70 C
ATOM 278 N VAL A 37 -2.799 33.882 35.428 1.00 20.68 N
ATOM 279 CA VAL A 37 -1.947 34.084 34.255 1.00 21.35 C
ATOM 280 C VAL A 37 -2.174 32.846 33.423 1.00 21.04 C
ATOM 281 O VAL A 37 -2.422 31.749 33.959 1.00 23.19 O
ATOM 282 CB VAL A 37 -0.429 34.214 34.557 1.00 19.61 C
ATOM 283 CG1 VAL A 37 -0.154 35.531 35.219 1.00 23.56 C
ATOM 284 CG2 VAL A 37 0.072 33.067 35.412 1.00 22.77 C
ATOM 285 N GLU A 38 -2.061 33.012 32.116 1.00 17.58 N
ATOM 286 CA GLU A 38 -2.278 31.936 31.175 1.00 19.30 C
ATOM 287 C GLU A 38 -0.993 31.538 30.455 1.00 21.62 C
ATOM 288 O GLU A 38 -0.243 32.397 29.950 1.00 21.10 O
ATOM 289 CB GLU A 38 -3.348 32.367 30.162 1.00 15.37 C
ATOM 290 CG GLU A 38 -3.742 31.313 29.158 1.00 18.15 C
ATOM 291 CD GLU A 38 -4.949 31.719 28.321 1.00 15.85 C
ATOM 292 OE1 GLU A 38 -5.532 32.772 28.570 1.00 18.33 O
ATOM 293 OE2 GLU A 38 -5.338 30.956 27.417 1.00 23.02 O
ATOM 294 N THR A 39 -0.738 30.232 30.447 1.00 21.55 N
ATOM 295 CA THR A 39 0.425 29.668 29.779 1.00 19.90 C
ATOM 296 C THR A 39 0.146 29.637 28.284 1.00 21.50 C
ATOM 297 O THR A 39 -1.011 29.753 27.864 1.00 22.45 O
ATOM 298 CB THR A 39 0.712 28.219 30.245 1.00 21.90 C
ATOM 299 OG1 THR A 39 -0.383 27.362 29.873 1.00 18.93 O
ATOM 300 CG2 THR A 39 0.930 28.171 31.739 1.00 15.63 C
ATOM 301 N SER A 40 1.197 29.461 27.483 1.00 22.60 N
ATOM 302 CA SER A 40 1.056 29.395 26.025 1.00 23.23 C
ATOM 303 C SER A 40 0.045 28.297 25.658 1.00 23.52 C
ATOM 304 O SER A 40 -0.776 28.461 24.735 1.00 22.19 O
ATOM 305 CB SER A 40 2.429 29.134 25.381 1.00 24.28 C
ATOM 306 OG SER A 40 3.332 30.202 25.673 1.00 24.23 O
ATOM 307 N CYS A 41 0.026 27.246 26.478 1.00 19.73 N
ATOM 308 CA CYS A 41 -0.877 26.124 26.283 1.00 19.74 C
ATOM 309 C CYS A 41 -2.305 26.333 26.836 1.00 19.27 C
ATOM 310 O CYS A 41 -3.059 25.371 26.992 1.00 20.45 O
ATOM 311 CB CYS A 41 -0.236 24.840 26.832 1.00 17.91 C
ATOM 312 SG CYS A 41 0.489 25.010 28.485 1.00 15.41 S
ATOM 313 N LYS A 42 -2.668 27.583 27.129 1.00 18.23 N
ATOM 314 CA LYS A 42 -4.013 27.943 27.604 1.00 17.75 C
ATOM 315 C LYS A 42 -4.465 27.380 28.951 1.00 19.11 C
ATOM 316 O LYS A 42 -5.652 27.147 29.174 1.00 19.36 O
ATOM 317 CB LYS A 42 -5.066 27.582 26.550 1.00 22.39 C
ATOM 318 CG LYS A 42 -4.740 28.021 25.128 1.00 22.74 C
ATOM 319 CD LYS A 42 -5.240 29.398 24.822 1.00 27.52 C
ATOM 320 CE LYS A 42 -5.046 29.691 23.354 1.00 37.80 C
ATOM 321 NZ LYS A 42 -5.657 28.613 22.476 1.00 42.21 N
ATOM 322 N HIS A 43 -3.526 27.142 29.845 1.00 18.89 N
ATOM 323 CA HIS A 43 -3.867 26.644 31.152 1.00 13.21 C
ATOM 324 C HIS A 43 -3.701 27.762 32.182 1.00 17.36 C
ATOM 325 O HIS A 43 -2.844 28.627 32.026 1.00 14.21 O
ATOM 326 CB HIS A 43 -2.986 25.448 31.452 1.00 16.40 C
ATOM 327 CG HIS A 43 -3.300 24.276 30.588 1.00 18.66 C
ATOM 328 ND1 HIS A 43 -2.338 23.677 29.815 1.00 24.24 N
ATOM 329 CD2 HIS A 43 -4.473 23.647 30.399 1.00 19.72 C
ATOM 330 CE1 HIS A 43 -2.954 22.695 29.192 1.00 24.75 C
ATOM 331 NE2 HIS A 43 -4.248 22.639 29.516 1.00 14.35 N
ATOM 332 N LEU A 44 -4.509 27.730 33.244 1.00 16.82 N
ATOM 333 CA LEU A 44 -4.480 28.773 34.273 1.00 18.28 C
ATOM 334 C LEU A 44 -3.873 28.426 35.644 1.00 16.73 C
ATOM 335 O LEU A 44 -4.034 27.313 36.138 1.00 19.42 O
ATOM 336 CB LEU A 44 -5.899 29.315 34.464 1.00 17.12 C
ATOM 337 CG LEU A 44 -6.576 29.847 33.192 1.00 18.55 C
ATOM 338 CD1 LEU A 44 -7.922 30.397 33.512 1.00 9.50 C
ATOM 339 CD2 LEU A 44 -5.723 30.922 32.535 1.00 13.63 C
ATOM 340 N PHE A 45 -3.162 29.387 36.234 1.00 15.07 N
ATOM 341 CA PHE A 45 -2.525 29.248 37.562 1.00 17.27 C
ATOM 342 C PHE A 45 -2.378 30.640 38.184 1.00 18.21 C
ATOM 343 O PHE A 45 -2.218 31.630 37.460 1.00 19.09 O
ATOM 344 CB PHE A 45 -1.101 28.671 37.473 1.00 16.69 C
ATOM 345 CG PHE A 45 -0.987 27.466 36.619 1.00 19.25 C
ATOM 346 CD1 PHE A 45 -0.770 27.593 35.253 1.00 18.52 C
ATOM 347 CD2 PHE A 45 -1.159 26.197 37.158 1.00 20.45 C
ATOM 348 CE1 PHE A 45 -0.727 26.472 34.419 1.00 16.38 C
ATOM 349 CE2 PHE A 45 -1.117 25.062 36.340 1.00 22.69 C
ATOM 350 CZ PHE A 45 -0.903 25.206 34.952 1.00 21.31 C
ATOM 351 N CYS A 46 -2.420 30.719 39.519 1.00 20.99 N
ATOM 352 CA CYS A 46 -2.234 32.000 40.216 1.00 20.09 C
ATOM 353 C CYS A 46 -0.801 32.391 39.860 1.00 20.75 C
ATOM 354 O CYS A 46 0.074 31.523 39.862 1.00 20.57 O
ATOM 355 CB CYS A 46 -2.278 31.828 41.747 1.00 19.21 C
ATOM 356 SG CYS A 46 -3.595 30.806 42.489 1.00 20.10 S
ATOM 357 N ARG A 47 -0.551 33.668 39.561 1.00 25.00 N
ATOM 358 CA ARG A 47 0.812 34.143 39.234 1.00 26.48 C
ATOM 359 C ARG A 47 1.910 33.579 40.156 1.00 24.57 C
ATOM 360 O ARG A 47 2.965 33.198 39.675 1.00 26.66 O
ATOM 361 CB ARG A 47 0.871 35.681 39.268 1.00 32.22 C
ATOM 362 CG ARG A 47 2.275 36.312 39.243 1.00 31.34 C
ATOM 363 CD ARG A 47 2.805 36.600 37.833 1.00 36.45 C
ATOM 364 NE ARG A 47 1.882 37.366 36.992 1.00 31.64 N
ATOM 365 CZ ARG A 47 1.200 38.432 37.393 1.00 34.62 C
ATOM 366 NH1 ARG A 47 1.337 38.882 38.631 1.00 36.38 N
ATOM 367 NH2 ARG A 47 0.317 39.011 36.581 1.00 33.76 N
ATOM 368 N ILE A 48 1.672 33.497 41.465 1.00 23.36 N
ATOM 369 CA ILE A 48 2.707 32.978 42.343 1.00 27.21 C
ATOM 370 C ILE A 48 2.853 31.474 42.300 1.00 28.50 C
ATOM 371 O ILE A 48 3.955 30.951 42.464 1.00 34.52 O
ATOM 372 CB ILE A 48 2.545 33.394 43.843 1.00 25.77 C
ATOM 373 CG1 ILE A 48 1.299 32.745 44.452 1.00 31.60 C
ATOM 374 CG2 ILE A 48 2.516 34.911 43.976 1.00 24.35 C
ATOM 375 CD1 ILE A 48 1.133 32.982 45.962 1.00 33.13 C
ATOM 376 N CYS A 49 1.760 30.761 42.077 1.00 26.91 N
ATOM 377 CA CYS A 49 1.864 29.304 42.086 1.00 25.29 C
ATOM 378 C CYS A 49 2.685 28.775 40.920 1.00 26.44 C
ATOM 379 O CYS A 49 3.556 27.914 41.101 1.00 25.67 O
ATOM 380 CB CYS A 49 0.481 28.658 42.119 1.00 21.26 C
ATOM 381 SG CYS A 49 -0.464 29.078 43.620 1.00 18.47 S
ATOM 382 N ILE A 50 2.449 29.347 39.745 1.00 24.93 N
ATOM 383 CA ILE A 50 3.146 28.909 38.546 1.00 27.53 C
ATOM 384 C ILE A 50 4.648 29.267 38.550 1.00 28.72 C
ATOM 385 O ILE A 50 5.490 28.405 38.303 1.00 26.01 O
ATOM 386 CB ILE A 50 2.414 29.388 37.263 1.00 18.69 C
ATOM 387 CG1 ILE A 50 3.073 28.773 36.027 1.00 20.46 C
ATOM 388 CG2 ILE A 50 2.332 30.908 37.214 1.00 13.36 C
ATOM 389 CD1 ILE A 50 3.114 27.249 36.053 1.00 18.09 C
ATOM 390 N LEU A 51 4.982 30.494 38.935 1.00 29.33 N
ATOM 391 CA LEU A 51 6.378 30.902 38.963 1.00 31.12 C
ATOM 392 C LEU A 51 7.209 30.029 39.902 1.00 35.28 C
ATOM 393 O LEU A 51 8.375 29.755 39.628 1.00 34.50 O
ATOM 394 CB LEU A 51 6.490 32.370 39.365 1.00 29.03 C
ATOM 395 CG LEU A 51 6.063 33.352 38.274 1.00 27.75 C
ATOM 396 CD1 LEU A 51 6.077 34.806 38.759 1.00 24.00 C
ATOM 397 CD2 LEU A 51 6.997 33.169 37.103 1.00 25.41 C
ATOM 398 N ARG A 52 6.620 29.575 41.001 1.00 35.46 N
ATOM 399 CA ARG A 52 7.388 28.749 41.910 1.00 38.24 C
ATOM 400 C ARG A 52 7.621 27.378 41.295 1.00 40.47 C
ATOM 401 O ARG A 52 8.706 26.821 41.419 1.00 42.43 O
ATOM 402 CB ARG A 52 6.704 28.649 43.278 1.00 40.03 C
ATOM 403 CG ARG A 52 7.410 27.747 44.310 1.00 46.22 C
ATOM 404 CD ARG A 52 6.950 26.280 44.246 1.00 52.98 C
ATOM 405 NE ARG A 52 5.490 26.185 44.132 1.00 62.84 N
ATOM 406 CZ ARG A 52 4.802 25.057 43.927 1.00 65.56 C
ATOM 407 NH1 ARG A 52 5.422 23.885 43.825 1.00 67.12 N
ATOM 408 NH2 ARG A 52 3.487 25.113 43.742 1.00 67.46 N
ATOM 409 N CYS A 53 6.612 26.845 40.612 1.00 42.51 N
ATOM 410 CA CYS A 53 6.720 25.521 39.990 1.00 43.46 C
ATOM 411 C CYS A 53 7.727 25.509 38.865 1.00 41.90 C
ATOM 412 O CYS A 53 8.365 24.492 38.611 1.00 40.70 O
ATOM 413 CB CYS A 53 5.369 25.049 39.447 1.00 45.61 C
ATOM 414 SG CYS A 53 4.390 24.099 40.606 1.00 51.97 S
ATOM 415 N LEU A 54 7.834 26.637 38.171 1.00 42.28 N
ATOM 416 CA LEU A 54 8.768 26.768 37.063 1.00 44.14 C
ATOM 417 C LEU A 54 10.180 26.792 37.616 1.00 45.97 C
ATOM 418 O LEU A 54 11.114 26.286 36.988 1.00 48.06 O
ATOM 419 CB LEU A 54 8.481 28.037 36.271 1.00 41.72 C
ATOM 420 CG LEU A 54 7.132 28.019 35.550 1.00 40.32 C
ATOM 421 CD1 LEU A 54 6.949 29.337 34.831 1.00 42.40 C
ATOM 422 CD2 LEU A 54 7.045 26.838 34.571 1.00 37.85 C
ATOM 423 N LYS A 55 10.319 27.340 38.818 1.00 45.56 N
ATOM 424 CA LYS A 55 11.620 27.400 39.451 1.00 46.97 C
ATOM 425 C LYS A 55 11.981 26.033 40.055 1.00 45.18 C
ATOM 426 O LYS A 55 12.724 25.260 39.464 1.00 45.07 O
ATOM 427 CB LYS A 55 11.661 28.514 40.503 1.00 47.69 C
ATOM 428 CG LYS A 55 13.052 29.102 40.704 1.00 54.48 C
ATOM 429 CD LYS A 55 13.088 30.253 41.729 1.00 61.19 C
ATOM 430 CE LYS A 55 12.716 29.778 43.134 1.00 63.86 C
ATOM 431 NZ LYS A 55 13.556 28.629 43.610 1.00 64.75 N
ATOM 432 N VAL A 56 11.334 25.674 41.151 1.00 43.22 N
ATOM 433 CA VAL A 56 11.646 24.424 41.825 1.00 42.41 C
ATOM 434 C VAL A 56 11.429 23.117 41.080 1.00 41.23 C
ATOM 435 O VAL A 56 12.112 22.142 41.367 1.00 42.68 O
ATOM 436 CB VAL A 56 10.935 24.340 43.187 1.00 42.40 C
ATOM 437 CG1 VAL A 56 11.198 25.617 43.988 1.00 40.43 C
ATOM 438 CG2 VAL A 56 9.438 24.120 42.993 1.00 45.35 C
ATOM 439 N MET A 57 10.520 23.091 40.111 1.00 42.94 N
ATOM 440 CA MET A 57 10.228 21.849 39.384 1.00 45.44 C
ATOM 441 C MET A 57 10.748 21.717 37.956 1.00 44.98 C
ATOM 442 O MET A 57 11.046 20.610 37.500 1.00 46.05 O
ATOM 443 CB MET A 57 8.722 21.574 39.384 1.00 49.11 C
ATOM 444 CG MET A 57 8.174 21.034 40.693 1.00 53.61 C
ATOM 445 SD MET A 57 8.768 19.363 41.034 1.00 56.35 S
ATOM 446 CE MET A 57 7.861 18.391 39.774 1.00 56.87 C
ATOM 447 N GLY A 58 10.829 22.827 37.236 1.00 41.32 N
ATOM 448 CA GLY A 58 11.302 22.749 35.873 1.00 37.27 C
ATOM 449 C GLY A 58 10.476 23.635 34.975 1.00 36.38 C
ATOM 450 O GLY A 58 9.436 24.162 35.383 1.00 36.50 O
ATOM 451 N SER A 59 10.941 23.798 33.744 1.00 33.03 N
ATOM 452 CA SER A 59 10.250 24.636 32.792 1.00 32.83 C
ATOM 453 C SER A 59 9.283 23.853 31.914 1.00 32.98 C
ATOM 454 O SER A 59 9.468 23.725 30.698 1.00 31.09 O
ATOM 455 CB SER A 59 11.253 25.462 31.994 1.00 30.71 C
ATOM 456 OG SER A 59 11.904 26.364 32.879 1.00 28.18 O
ATOM 457 N TYR A 60 8.248 23.336 32.578 1.00 31.06 N
ATOM 458 CA TYR A 60 7.176 22.566 31.961 1.00 29.69 C
ATOM 459 C TYR A 60 5.845 22.846 32.658 1.00 26.56 C
ATOM 460 O TYR A 60 5.809 23.033 33.879 1.00 20.68 O
ATOM 461 CB TYR A 60 7.493 21.090 32.062 1.00 32.15 C
ATOM 462 CG TYR A 60 8.667 20.698 31.232 1.00 33.88 C
ATOM 463 CD1 TYR A 60 8.619 20.778 29.838 1.00 34.07 C
ATOM 464 CD2 TYR A 60 9.831 20.252 31.834 1.00 38.07 C
ATOM 465 CE1 TYR A 60 9.714 20.423 29.065 1.00 37.45 C
ATOM 466 CE2 TYR A 60 10.939 19.890 31.072 1.00 40.57 C
ATOM 467 CZ TYR A 60 10.870 19.975 29.698 1.00 39.48 C
ATOM 468 OH TYR A 60 11.974 19.622 28.974 1.00 42.02 O
ATOM 469 N CYS A 61 4.757 22.863 31.888 1.00 24.79 N
ATOM 470 CA CYS A 61 3.415 23.127 32.424 1.00 19.81 C
ATOM 471 C CYS A 61 2.954 22.023 33.345 1.00 18.29 C
ATOM 472 O CYS A 61 2.933 20.854 32.963 1.00 16.57 O
ATOM 473 CB CYS A 61 2.391 23.257 31.294 1.00 22.52 C
ATOM 474 SG CYS A 61 0.687 23.464 31.869 1.00 23.48 S
ATOM 475 N PRO A 62 2.527 22.378 34.567 1.00 19.09 N
ATOM 476 CA PRO A 62 2.062 21.358 35.516 1.00 20.38 C
ATOM 477 C PRO A 62 0.873 20.540 34.967 1.00 21.58 C
ATOM 478 O PRO A 62 0.738 19.355 35.275 1.00 20.98 O
ATOM 479 CB PRO A 62 1.656 22.193 36.731 1.00 21.11 C
ATOM 480 CG PRO A 62 2.514 23.418 36.621 1.00 17.99 C
ATOM 481 CD PRO A 62 2.436 23.721 35.157 1.00 17.96 C
ATOM 482 N SER A 63 0.027 21.175 34.152 1.00 22.27 N
ATOM 483 CA SER A 63 -1.141 20.516 33.572 1.00 21.56 C
ATOM 484 C SER A 63 -0.806 19.559 32.443 1.00 25.34 C
ATOM 485 O SER A 63 -1.155 18.374 32.508 1.00 26.08 O
ATOM 486 CB SER A 63 -2.127 21.545 33.023 1.00 23.28 C
ATOM 487 OG SER A 63 -2.728 22.312 34.050 1.00 32.17 O
ATOM 488 N CYS A 64 -0.119 20.067 31.417 1.00 23.17 N
ATOM 489 CA CYS A 64 0.198 19.247 30.253 1.00 21.55 C
ATOM 490 C CYS A 64 1.647 18.865 29.990 1.00 23.11 C
ATOM 491 O CYS A 64 1.922 18.054 29.100 1.00 23.72 O
ATOM 492 CB CYS A 64 -0.413 19.873 29.002 1.00 18.17 C
ATOM 493 SG CYS A 64 0.238 21.456 28.576 1.00 18.62 S
ATOM 494 N ARG A 65 2.573 19.461 30.739 1.00 30.01 N
ATOM 495 CA ARG A 65 4.011 19.156 30.629 1.00 30.85 C
ATOM 496 C ARG A 65 4.692 19.692 29.386 1.00 30.50 C
ATOM 497 O ARG A 65 5.755 19.207 28.994 1.00 31.90 O
ATOM 498 CB ARG A 65 4.258 17.642 30.719 1.00 36.38 C
ATOM 499 CG ARG A 65 3.897 16.982 32.063 1.00 47.96 C
ATOM 500 CD ARG A 65 3.757 15.461 31.907 1.00 51.59 C
ATOM 501 NE ARG A 65 2.562 15.120 31.127 1.00 59.29 N
ATOM 502 CZ ARG A 65 2.557 14.467 29.955 1.00 63.49 C
ATOM 503 NH1 ARG A 65 3.694 14.053 29.384 1.00 64.67 N
ATOM 504 NH2 ARG A 65 1.402 14.250 29.333 1.00 61.69 N
ATOM 505 N TYR A 66 4.074 20.678 28.753 1.00 31.64 N
ATOM 506 CA TYR A 66 4.632 21.292 27.540 1.00 33.68 C
ATOM 507 C TYR A 66 5.565 22.408 28.043 1.00 29.63 C
ATOM 508 O TYR A 66 5.255 23.074 29.033 1.00 26.36 O
ATOM 509 CB TYR A 66 3.476 21.856 26.692 1.00 39.50 C
ATOM 510 CG TYR A 66 3.750 22.073 25.217 1.00 47.68 C
ATOM 511 CD1 TYR A 66 4.034 20.999 24.375 1.00 51.09 C
ATOM 512 CD2 TYR A 66 3.678 23.360 24.654 1.00 51.26 C
ATOM 513 CE1 TYR A 66 4.248 21.193 23.005 1.00 57.55 C
ATOM 514 CE2 TYR A 66 3.890 23.573 23.291 1.00 54.50 C
ATOM 515 CZ TYR A 66 4.174 22.483 22.462 1.00 58.41 C
ATOM 516 OH TYR A 66 4.402 22.674 21.104 1.00 55.67 O
ATOM 517 N PRO A 67 6.738 22.590 27.402 1.00 29.14 N
ATOM 518 CA PRO A 67 7.694 23.631 27.818 1.00 27.79 C
ATOM 519 C PRO A 67 6.998 24.942 28.202 1.00 26.09 C
ATOM 520 O PRO A 67 6.162 25.442 27.459 1.00 26.65 O
ATOM 521 CB PRO A 67 8.585 23.773 26.595 1.00 24.48 C
ATOM 522 CG PRO A 67 8.628 22.357 26.083 1.00 25.99 C
ATOM 523 CD PRO A 67 7.196 21.919 26.169 1.00 27.18 C
ATOM 524 N CYS A 68 7.342 25.469 29.376 1.00 26.58 N
ATOM 525 CA CYS A 68 6.721 26.673 29.903 1.00 27.32 C
ATOM 526 C CYS A 68 7.699 27.637 30.580 1.00 26.69 C
ATOM 527 O CYS A 68 8.406 27.266 31.507 1.00 27.41 O
ATOM 528 CB CYS A 68 5.629 26.252 30.898 1.00 27.44 C
ATOM 529 SG CYS A 68 4.600 27.590 31.523 1.00 30.87 S
ATOM 530 N PHE A 69 7.683 28.899 30.161 1.00 28.36 N
ATOM 531 CA PHE A 69 8.584 29.892 30.728 1.00 30.91 C
ATOM 532 C PHE A 69 7.874 31.103 31.300 1.00 31.05 C
ATOM 533 O PHE A 69 6.831 31.508 30.788 1.00 35.31 O
ATOM 534 CB PHE A 69 9.583 30.351 29.655 1.00 33.04 C
ATOM 535 CG PHE A 69 10.480 29.247 29.176 1.00 32.64 C
ATOM 536 CD1 PHE A 69 10.061 28.389 28.172 1.00 30.17 C
ATOM 537 CD2 PHE A 69 11.703 29.014 29.795 1.00 29.83 C
ATOM 538 CE1 PHE A 69 10.831 27.283 27.805 1.00 34.59 C
ATOM 539 CE2 PHE A 69 12.472 27.925 29.441 1.00 36.06 C
ATOM 540 CZ PHE A 69 12.036 27.054 28.434 1.00 36.15 C
ATOM 541 N PRO A 70 8.429 31.702 32.371 1.00 28.82 N
ATOM 542 CA PRO A 70 7.874 32.887 33.040 1.00 30.13 C
ATOM 543 C PRO A 70 7.525 33.986 32.061 1.00 31.50 C
ATOM 544 O PRO A 70 6.501 34.659 32.193 1.00 32.13 O
ATOM 545 CB PRO A 70 9.007 33.312 33.954 1.00 28.28 C
ATOM 546 CG PRO A 70 9.490 31.975 34.446 1.00 29.68 C
ATOM 547 CD PRO A 70 9.545 31.146 33.158 1.00 27.98 C
ATOM 548 N THR A 71 8.351 34.092 31.031 1.00 31.78 N
ATOM 549 CA THR A 71 8.182 35.082 29.990 1.00 29.38 C
ATOM 550 C THR A 71 6.962 34.818 29.084 1.00 29.03 C
ATOM 551 O THR A 71 6.535 35.689 28.329 1.00 24.30 O
ATOM 552 CB THR A 71 9.488 35.185 29.176 1.00 32.95 C
ATOM 553 OG1 THR A 71 9.343 36.178 28.161 1.00 35.00 O
ATOM 554 CG2 THR A 71 9.880 33.825 28.570 1.00 32.44 C
ATOM 555 N ASP A 72 6.377 33.633 29.194 1.00 27.13 N
ATOM 556 CA ASP A 72 5.204 33.272 28.397 1.00 29.51 C
ATOM 557 C ASP A 72 3.895 33.623 29.116 1.00 30.93 C
ATOM 558 O ASP A 72 2.799 33.605 28.510 1.00 27.24 O
ATOM 559 CB ASP A 72 5.181 31.761 28.170 1.00 30.27 C
ATOM 560 CG ASP A 72 6.048 31.324 27.035 1.00 31.16 C
ATOM 561 OD1 ASP A 72 5.968 31.966 25.961 1.00 30.94 O
ATOM 562 OD2 ASP A 72 6.763 30.308 27.217 1.00 33.99 O
ATOM 563 N LEU A 73 4.013 33.924 30.410 1.00 28.23 N
ATOM 564 CA LEU A 73 2.840 34.183 31.238 1.00 28.33 C
ATOM 565 C LEU A 73 2.066 35.456 30.984 1.00 26.64 C
ATOM 566 O LEU A 73 2.527 36.544 31.310 1.00 26.81 O
ATOM 567 CB LEU A 73 3.199 34.026 32.718 1.00 28.42 C
ATOM 568 CG LEU A 73 3.190 32.590 33.287 1.00 30.31 C
ATOM 569 CD1 LEU A 73 2.988 31.528 32.231 1.00 27.78 C
ATOM 570 CD2 LEU A 73 4.463 32.319 34.059 1.00 26.76 C
ATOM 571 N GLU A 74 0.894 35.309 30.379 1.00 21.92 N
ATOM 572 CA GLU A 74 0.051 36.448 30.083 1.00 22.24 C
ATOM 573 C GLU A 74 -1.174 36.486 30.958 1.00 22.35 C
ATOM 574 O GLU A 74 -1.367 35.635 31.819 1.00 24.58 O
ATOM 575 CB GLU A 74 -0.396 36.406 28.628 1.00 25.65 C
ATOM 576 CG GLU A 74 0.666 36.860 27.607 1.00 37.15 C
ATOM 577 CD GLU A 74 1.175 38.281 27.847 1.00 39.70 C
ATOM 578 OE1 GLU A 74 0.350 39.240 27.863 1.00 46.86 O
ATOM 579 OE2 GLU A 74 2.405 38.431 28.029 1.00 35.23 O
ATOM 580 N SER A 75 -2.002 37.495 30.745 1.00 22.82 N
ATOM 581 CA SER A 75 -3.233 37.615 31.496 1.00 22.14 C
ATOM 582 C SER A 75 -4.354 36.958 30.684 1.00 22.64 C
ATOM 583 O SER A 75 -4.324 36.979 29.457 1.00 18.26 O
ATOM 584 CB SER A 75 -3.552 39.086 31.711 1.00 25.12 C
ATOM 585 OG SER A 75 -4.810 39.222 32.332 1.00 28.16 O
ATOM 586 N PRO A 76 -5.310 36.289 31.352 1.00 20.62 N
ATOM 587 CA PRO A 76 -6.406 35.658 30.608 1.00 17.77 C
ATOM 588 C PRO A 76 -7.182 36.754 29.867 1.00 16.67 C
ATOM 589 O PRO A 76 -7.212 37.919 30.302 1.00 13.29 O
ATOM 590 CB PRO A 76 -7.286 35.076 31.723 1.00 12.83 C
ATOM 591 CG PRO A 76 -6.326 34.787 32.796 1.00 14.49 C
ATOM 592 CD PRO A 76 -5.413 35.977 32.790 1.00 19.31 C
ATOM 593 N VAL A 77 -7.845 36.360 28.788 1.00 11.34 N
ATOM 594 CA VAL A 77 -8.646 37.263 27.983 1.00 14.67 C
ATOM 595 C VAL A 77 -9.620 38.019 28.914 1.00 18.65 C
ATOM 596 O VAL A 77 -9.973 37.527 29.983 1.00 20.56 O
ATOM 597 CB VAL A 77 -9.365 36.434 26.903 1.00 14.65 C
ATOM 598 CG1 VAL A 77 -10.682 35.903 27.415 1.00 14.96 C
ATOM 599 CG2 VAL A 77 -9.489 37.195 25.607 1.00 21.32 C
ATOM 600 N LYS A 78 -10.077 39.193 28.496 1.00 24.24 N
ATOM 601 CA LYS A 78 -10.962 40.016 29.327 1.00 23.92 C
ATOM 602 C LYS A 78 -12.268 39.351 29.750 1.00 24.57 C
ATOM 603 O LYS A 78 -12.639 39.402 30.930 1.00 24.17 O
ATOM 604 CB LYS A 78 -11.285 41.337 28.632 1.00 24.64 C
ATOM 605 CG LYS A 78 -12.169 42.242 29.483 1.00 30.36 C
ATOM 606 CD LYS A 78 -11.412 42.702 30.735 1.00 37.89 C
ATOM 607 CE LYS A 78 -12.271 43.555 31.677 1.00 41.89 C
ATOM 608 NZ LYS A 78 -13.073 44.626 30.986 1.00 47.12 N
ATOM 609 N SER A 79 -12.975 38.770 28.774 1.00 23.81 N
ATOM 610 CA SER A 79 -14.257 38.091 29.019 1.00 23.41 C
ATOM 611 C SER A 79 -14.163 36.994 30.051 1.00 22.05 C
ATOM 612 O SER A 79 -15.150 36.707 30.721 1.00 24.71 O
ATOM 613 CB SER A 79 -14.843 37.515 27.730 1.00 20.80 C
ATOM 614 OG SER A 79 -14.837 38.508 26.722 1.00 26.79 O
ATOM 615 N PHE A 80 -13.005 36.343 30.143 1.00 19.55 N
ATOM 616 CA PHE A 80 -12.838 35.299 31.150 1.00 19.16 C
ATOM 617 C PHE A 80 -12.671 35.984 32.486 1.00 19.28 C
ATOM 618 O PHE A 80 -13.284 35.595 33.476 1.00 21.01 O
ATOM 619 CB PHE A 80 -11.623 34.416 30.898 1.00 16.88 C
ATOM 620 CG PHE A 80 -11.433 33.383 31.961 1.00 16.44 C
ATOM 621 CD1 PHE A 80 -12.289 32.286 32.038 1.00 16.88 C
ATOM 622 CD2 PHE A 80 -10.486 33.556 32.956 1.00 12.56 C
ATOM 623 CE1 PHE A 80 -12.197 31.381 33.107 1.00 14.74 C
ATOM 624 CE2 PHE A 80 -10.389 32.660 34.027 1.00 13.31 C
ATOM 625 CZ PHE A 80 -11.242 31.579 34.102 1.00 9.67 C
ATOM 626 N LEU A 81 -11.831 37.012 32.516 1.00 21.19 N
ATOM 627 CA LEU A 81 -11.635 37.761 33.751 1.00 19.00 C
ATOM 628 C LEU A 81 -12.958 38.285 34.296 1.00 21.01 C
ATOM 629 O LEU A 81 -13.148 38.335 35.509 1.00 18.13 O
ATOM 630 CB LEU A 81 -10.693 38.939 33.544 1.00 16.56 C
ATOM 631 CG LEU A 81 -9.248 38.578 33.258 1.00 17.38 C
ATOM 632 CD1 LEU A 81 -8.472 39.866 33.284 1.00 18.20 C
ATOM 633 CD2 LEU A 81 -8.699 37.572 34.302 1.00 17.60 C
ATOM 634 N ASN A 82 -13.865 38.679 33.403 1.00 19.94 N
ATOM 635 CA ASN A 82 -15.165 39.195 33.829 1.00 23.79 C
ATOM 636 C ASN A 82 -16.023 38.153 34.538 1.00 24.83 C
ATOM 637 O ASN A 82 -16.707 38.468 35.517 1.00 23.24 O
ATOM 638 CB ASN A 82 -15.940 39.745 32.638 1.00 27.35 C
ATOM 639 CG ASN A 82 -15.372 41.048 32.110 1.00 25.55 C
ATOM 640 OD1 ASN A 82 -15.799 41.531 31.062 1.00 26.78 O
ATOM 641 ND2 ASN A 82 -14.423 41.630 32.830 1.00 23.60 N
ATOM 642 N ILE A 83 -15.995 36.919 34.029 1.00 21.10 N
ATOM 643 CA ILE A 83 -16.761 35.813 34.604 1.00 17.83 C
ATOM 644 C ILE A 83 -16.198 35.447 35.995 1.00 19.80 C
ATOM 645 O ILE A 83 -16.929 35.305 36.991 1.00 18.49 O
ATOM 646 CB ILE A 83 -16.729 34.608 33.644 1.00 15.62 C
ATOM 647 CG1 ILE A 83 -17.561 34.937 32.385 1.00 15.00 C
ATOM 648 CG2 ILE A 83 -17.229 33.383 34.346 1.00 13.59 C
ATOM 649 CD1 ILE A 83 -17.307 34.050 31.151 1.00 5.23 C
ATOM 650 N LEU A 84 -14.877 35.380 36.060 1.00 21.12 N
ATOM 651 CA LEU A 84 -14.164 35.077 37.286 1.00 21.52 C
ATOM 652 C LEU A 84 -14.381 36.164 38.337 1.00 21.27 C
ATOM 653 O LEU A 84 -14.793 35.870 39.447 1.00 25.42 O
ATOM 654 CB LEU A 84 -12.672 34.964 36.984 1.00 18.68 C
ATOM 655 CG LEU A 84 -11.728 34.926 38.181 1.00 22.94 C
ATOM 656 CD1 LEU A 84 -11.756 33.524 38.812 1.00 16.13 C
ATOM 657 CD2 LEU A 84 -10.303 35.318 37.723 1.00 15.93 C
ATOM 658 N ASN A 85 -14.108 37.416 37.982 1.00 23.83 N
ATOM 659 CA ASN A 85 -14.250 38.539 38.921 1.00 25.37 C
ATOM 660 C ASN A 85 -15.672 38.786 39.443 1.00 26.61 C
ATOM 661 O ASN A 85 -15.857 39.519 40.429 1.00 25.78 O
ATOM 662 CB ASN A 85 -13.667 39.836 38.328 1.00 21.72 C
ATOM 663 CG ASN A 85 -12.143 39.869 38.367 1.00 17.00 C
ATOM 664 OD1 ASN A 85 -11.532 39.582 39.402 1.00 19.52 O
ATOM 665 ND2 ASN A 85 -11.520 40.230 37.241 1.00 18.15 N
ATOM 666 N SER A 86 -16.656 38.148 38.800 1.00 25.88 N
ATOM 667 CA SER A 86 -18.064 38.276 39.190 1.00 26.01 C
ATOM 668 C SER A 86 -18.624 37.152 40.054 1.00 24.39 C
ATOM 669 O SER A 86 -19.730 37.286 40.598 1.00 22.44 O
ATOM 670 CB SER A 86 -18.916 38.391 37.954 1.00 25.42 C
ATOM 671 OG SER A 86 -18.444 39.466 37.180 1.00 36.49 O
ATOM 672 N LEU A 87 -17.883 36.049 40.170 1.00 21.89 N
ATOM 673 CA LEU A 87 -18.350 34.901 40.965 1.00 25.13 C
ATOM 674 C LEU A 87 -18.838 35.333 42.363 1.00 25.74 C
ATOM 675 O LEU A 87 -18.181 36.122 43.048 1.00 29.50 O
ATOM 676 CB LEU A 87 -17.242 33.832 41.131 1.00 19.45 C
ATOM 677 CG LEU A 87 -16.568 33.150 39.944 1.00 20.31 C
ATOM 678 CD1 LEU A 87 -15.600 32.069 40.458 1.00 15.57 C
ATOM 679 CD2 LEU A 87 -17.610 32.532 39.021 1.00 22.11 C
ATOM 680 N MET A 88 -19.993 34.834 42.783 1.00 22.15 N
ATOM 681 CA MET A 88 -20.480 35.204 44.098 1.00 21.50 C
ATOM 682 C MET A 88 -19.891 34.249 45.158 1.00 23.27 C
ATOM 683 O MET A 88 -19.851 33.024 44.978 1.00 18.18 O
ATOM 684 CB MET A 88 -22.005 35.191 44.107 1.00 23.56 C
ATOM 685 CG MET A 88 -22.636 36.242 43.198 1.00 24.27 C
ATOM 686 SD MET A 88 -22.080 37.918 43.629 1.00 33.14 S
ATOM 687 CE MET A 88 -22.740 38.074 45.303 1.00 24.99 C
ATOM 688 N VAL A 89 -19.396 34.809 46.252 1.00 21.49 N
ATOM 689 CA VAL A 89 -18.819 33.983 47.296 1.00 24.33 C
ATOM 690 C VAL A 89 -19.399 34.279 48.686 1.00 23.95 C
ATOM 691 O VAL A 89 -19.720 35.425 49.007 1.00 22.93 O
ATOM 692 CB VAL A 89 -17.273 34.075 47.259 1.00 24.73 C
ATOM 693 CG1 VAL A 89 -16.849 35.422 46.670 1.00 29.09 C
ATOM 694 CG2 VAL A 89 -16.670 33.862 48.649 1.00 23.27 C
ATOM 695 N LYS A 90 -19.638 33.214 49.449 1.00 23.80 N
ATOM 696 CA LYS A 90 -20.172 33.309 50.794 1.00 22.73 C
ATOM 697 C LYS A 90 -19.071 33.594 51.806 1.00 23.20 C
ATOM 698 O LYS A 90 -18.237 32.727 52.113 1.00 23.38 O
ATOM 699 CB LYS A 90 -20.900 32.010 51.190 1.00 21.99 C
ATOM 700 CG LYS A 90 -22.244 31.784 50.482 1.00 29.52 C
ATOM 701 CD LYS A 90 -22.770 30.364 50.713 1.00 33.17 C
ATOM 702 CE LYS A 90 -21.729 29.329 50.271 1.00 33.76 C
ATOM 703 NZ LYS A 90 -22.174 27.932 50.458 1.00 32.52 N
ATOM 704 N CYS A 91 -19.100 34.802 52.359 1.00 23.19 N
ATOM 705 CA CYS A 91 -18.131 35.221 53.377 1.00 22.75 C
ATOM 706 C CYS A 91 -18.319 34.296 54.585 1.00 17.45 C
ATOM 707 O CYS A 91 -19.432 34.075 55.027 1.00 17.88 O
ATOM 708 CB CYS A 91 -18.382 36.683 53.761 1.00 21.78 C
ATOM 709 SG CYS A 91 -17.492 37.214 55.219 1.00 29.76 S
ATOM 710 N PRO A 92 -17.229 33.682 55.074 1.00 18.69 N
ATOM 711 CA PRO A 92 -17.215 32.753 56.213 1.00 17.31 C
ATOM 712 C PRO A 92 -17.010 33.400 57.599 1.00 18.54 C
ATOM 713 O PRO A 92 -16.866 32.720 58.621 1.00 16.19 O
ATOM 714 CB PRO A 92 -16.075 31.795 55.846 1.00 13.85 C
ATOM 715 CG PRO A 92 -15.060 32.742 55.241 1.00 13.62 C
ATOM 716 CD PRO A 92 -15.904 33.747 54.419 1.00 12.09 C
ATOM 717 N ALA A 93 -16.968 34.719 57.630 1.00 20.05 N
ATOM 718 CA ALA A 93 -16.811 35.404 58.904 1.00 26.05 C
ATOM 719 C ALA A 93 -18.029 35.046 59.767 1.00 28.10 C
ATOM 720 O ALA A 93 -19.160 35.103 59.289 1.00 25.99 O
ATOM 721 CB ALA A 93 -16.741 36.909 58.682 1.00 23.33 C
ATOM 722 N GLN A 94 -17.784 34.690 61.029 1.00 31.29 N
ATOM 723 CA GLN A 94 -18.825 34.306 61.991 1.00 34.99 C
ATOM 724 C GLN A 94 -20.075 35.194 61.999 1.00 35.18 C
ATOM 725 O GLN A 94 -19.973 36.407 62.148 1.00 36.82 O
ATOM 726 CB GLN A 94 -18.196 34.284 63.381 1.00 40.92 C
ATOM 727 CG GLN A 94 -19.080 33.814 64.514 1.00 48.43 C
ATOM 728 CD GLN A 94 -18.293 33.655 65.812 1.00 51.14 C
ATOM 729 OE1 GLN A 94 -17.446 34.494 66.151 1.00 52.09 O
ATOM 730 NE2 GLN A 94 -18.554 32.567 66.530 1.00 46.26 N
ATOM 731 N ASP A 95 -21.246 34.579 61.822 1.00 38.41 N
ATOM 732 CA ASP A 95 -22.538 35.281 61.807 1.00 41.86 C
ATOM 733 C ASP A 95 -22.837 36.207 60.637 1.00 43.09 C
ATOM 734 O ASP A 95 -23.920 36.801 60.560 1.00 43.18 O
ATOM 735 CB ASP A 95 -22.777 36.030 63.114 1.00 49.33 C
ATOM 736 CG ASP A 95 -23.367 35.140 64.180 1.00 55.18 C
ATOM 737 OD1 ASP A 95 -24.607 34.946 64.168 1.00 59.22 O
ATOM 738 OD2 ASP A 95 -22.594 34.617 65.013 1.00 59.45 O
ATOM 739 N CYS A 96 -21.861 36.380 59.754 1.00 43.30 N
ATOM 740 CA CYS A 96 -22.058 37.201 58.570 1.00 39.18 C
ATOM 741 C CYS A 96 -22.700 36.284 57.535 1.00 38.15 C
ATOM 742 O CYS A 96 -22.202 35.184 57.250 1.00 36.88 O
ATOM 743 CB CYS A 96 -20.729 37.728 58.041 1.00 37.17 C
ATOM 744 SG CYS A 96 -20.944 38.636 56.525 1.00 29.25 S
ATOM 745 N ASN A 97 -23.837 36.701 57.012 1.00 36.69 N
ATOM 746 CA ASN A 97 -24.509 35.871 56.028 1.00 41.55 C
ATOM 747 C ASN A 97 -24.614 36.670 54.755 1.00 39.87 C
ATOM 748 O ASN A 97 -25.688 36.842 54.161 1.00 39.81 O
ATOM 749 CB ASN A 97 -25.876 35.418 56.551 1.00 45.46 C
ATOM 750 CG ASN A 97 -25.758 34.518 57.784 1.00 50.18 C
ATOM 751 OD1 ASN A 97 -25.540 33.310 57.670 1.00 49.29 O
ATOM 752 ND2 ASN A 97 -25.873 35.118 58.971 1.00 56.91 N
ATOM 753 N GLU A 98 -23.454 37.139 54.334 1.00 37.52 N
ATOM 754 CA GLU A 98 -23.354 37.965 53.157 1.00 36.78 C
ATOM 755 C GLU A 98 -22.602 37.276 52.040 1.00 31.54 C
ATOM 756 O GLU A 98 -21.647 36.531 52.263 1.00 30.48 O
ATOM 757 CB GLU A 98 -22.680 39.290 53.527 1.00 41.62 C
ATOM 758 CG GLU A 98 -23.611 40.484 53.610 1.00 44.57 C
ATOM 759 CD GLU A 98 -23.351 41.455 52.475 1.00 51.60 C
ATOM 760 OE1 GLU A 98 -23.742 41.151 51.326 1.00 55.54 O
ATOM 761 OE2 GLU A 98 -22.722 42.507 52.717 1.00 54.82 O
ATOM 762 N GLU A 99 -23.078 37.516 50.833 1.00 27.11 N
ATOM 763 CA GLU A 99 -22.485 36.970 49.639 1.00 24.01 C
ATOM 764 C GLU A 99 -22.030 38.172 48.813 1.00 24.61 C
ATOM 765 O GLU A 99 -22.768 39.137 48.680 1.00 26.26 O
ATOM 766 CB GLU A 99 -23.533 36.132 48.890 1.00 17.37 C
ATOM 767 CG GLU A 99 -24.190 35.077 49.793 1.00 21.60 C
ATOM 768 CD GLU A 99 -24.978 33.992 49.044 1.00 26.22 C
ATOM 769 OE1 GLU A 99 -25.274 34.161 47.837 1.00 32.80 O
ATOM 770 OE2 GLU A 99 -25.310 32.957 49.669 1.00 25.37 O
ATOM 771 N VAL A 100 -20.800 38.142 48.306 1.00 23.33 N
ATOM 772 CA VAL A 100 -20.281 39.242 47.494 1.00 22.73 C
ATOM 773 C VAL A 100 -19.445 38.706 46.317 1.00 23.67 C
ATOM 774 O VAL A 100 -18.942 37.574 46.357 1.00 23.12 O
ATOM 775 CB VAL A 100 -19.374 40.194 48.322 1.00 24.46 C
ATOM 776 CG1 VAL A 100 -20.163 40.899 49.401 1.00 23.70 C
ATOM 777 CG2 VAL A 100 -18.219 39.415 48.935 1.00 26.22 C
ATOM 778 N SER A 101 -19.259 39.546 45.300 1.00 23.21 N
ATOM 779 CA SER A 101 -18.489 39.179 44.121 1.00 22.66 C
ATOM 780 C SER A 101 -17.016 39.086 44.484 1.00 24.59 C
ATOM 781 O SER A 101 -16.565 39.724 45.435 1.00 25.14 O
ATOM 782 CB SER A 101 -18.669 40.207 43.020 1.00 22.12 C
ATOM 783 OG SER A 101 -17.914 41.355 43.305 1.00 22.63 O
ATOM 784 N LEU A 102 -16.275 38.312 43.700 1.00 23.34 N
ATOM 785 CA LEU A 102 -14.858 38.096 43.922 1.00 21.08 C
ATOM 786 C LEU A 102 -14.069 39.393 43.949 1.00 24.68 C
ATOM 787 O LEU A 102 -13.154 39.543 44.759 1.00 28.23 O
ATOM 788 CB LEU A 102 -14.289 37.194 42.836 1.00 16.36 C
ATOM 789 CG LEU A 102 -12.902 36.672 43.200 1.00 18.20 C
ATOM 790 CD1 LEU A 102 -13.047 35.750 44.410 1.00 15.32 C
ATOM 791 CD2 LEU A 102 -12.268 35.936 42.020 1.00 15.92 C
ATOM 792 N GLU A 103 -14.419 40.338 43.081 1.00 25.44 N
ATOM 793 CA GLU A 103 -13.703 41.614 43.038 1.00 28.39 C
ATOM 794 C GLU A 103 -14.046 42.516 44.218 1.00 28.88 C
ATOM 795 O GLU A 103 -13.235 43.334 44.634 1.00 30.22 O
ATOM 796 CB GLU A 103 -13.958 42.333 41.719 1.00 31.94 C
ATOM 797 CG GLU A 103 -15.415 42.633 41.448 1.00 35.60 C
ATOM 798 CD GLU A 103 -15.699 43.075 40.011 1.00 37.94 C
ATOM 799 OE1 GLU A 103 -14.758 43.181 39.172 1.00 34.14 O
ATOM 800 OE2 GLU A 103 -16.895 43.308 39.722 1.00 41.34 O
ATOM 801 N LYS A 104 -15.233 42.338 44.791 1.00 27.92 N
ATOM 802 CA LYS A 104 -15.624 43.142 45.943 1.00 28.65 C
ATOM 803 C LYS A 104 -15.330 42.450 47.276 1.00 26.34 C
ATOM 804 O LYS A 104 -15.541 43.025 48.338 1.00 25.96 O
ATOM 805 CB LYS A 104 -17.105 43.527 45.861 1.00 31.82 C
ATOM 806 CG LYS A 104 -17.384 44.676 44.881 1.00 42.42 C
ATOM 807 CD LYS A 104 -18.830 45.218 44.956 1.00 48.19 C
ATOM 808 CE LYS A 104 -19.234 45.698 46.381 1.00 55.05 C
ATOM 809 NZ LYS A 104 -18.388 46.794 46.985 1.00 51.48 N
ATOM 810 N TYR A 105 -14.758 41.255 47.219 1.00 22.52 N
ATOM 811 CA TYR A 105 -14.477 40.512 48.425 1.00 24.17 C
ATOM 812 C TYR A 105 -13.489 41.144 49.389 1.00 26.48 C
ATOM 813 O TYR A 105 -13.821 41.340 50.545 1.00 28.78 O
ATOM 814 CB TYR A 105 -14.056 39.101 48.086 1.00 22.59 C
ATOM 815 CG TYR A 105 -13.988 38.200 49.287 1.00 21.82 C
ATOM 816 CD1 TYR A 105 -15.138 37.621 49.819 1.00 20.81 C
ATOM 817 CD2 TYR A 105 -12.764 37.877 49.856 1.00 19.26 C
ATOM 818 CE1 TYR A 105 -15.060 36.737 50.890 1.00 22.58 C
ATOM 819 CE2 TYR A 105 -12.675 37.000 50.916 1.00 18.53 C
ATOM 820 CZ TYR A 105 -13.814 36.429 51.431 1.00 21.12 C
ATOM 821 OH TYR A 105 -13.682 35.548 52.489 1.00 21.01 O
ATOM 822 N ASN A 106 -12.277 41.449 48.946 1.00 29.75 N
ATOM 823 CA ASN A 106 -11.302 42.070 49.844 1.00 34.70 C
ATOM 824 C ASN A 106 -11.812 43.329 50.530 1.00 37.34 C
ATOM 825 O ASN A 106 -11.424 43.633 51.654 1.00 38.52 O
ATOM 826 CB ASN A 106 -10.027 42.392 49.097 1.00 35.62 C
ATOM 827 CG ASN A 106 -9.322 41.156 48.637 1.00 39.60 C
ATOM 828 OD1 ASN A 106 -9.894 40.065 48.650 1.00 40.86 O
ATOM 829 ND2 ASN A 106 -8.063 41.302 48.250 1.00 42.02 N
ATOM 830 N HIS A 107 -12.666 44.074 49.844 1.00 38.96 N
ATOM 831 CA HIS A 107 -13.219 45.280 50.416 1.00 36.98 C
ATOM 832 C HIS A 107 -14.216 44.923 51.498 1.00 35.40 C
ATOM 833 O HIS A 107 -14.320 45.628 52.508 1.00 33.78 O
ATOM 834 CB HIS A 107 -13.907 46.130 49.352 1.00 41.59 C
ATOM 835 CG HIS A 107 -14.588 47.335 49.916 1.00 45.33 C
ATOM 836 ND1 HIS A 107 -13.890 48.384 50.490 1.00 45.00 N
ATOM 837 CD2 HIS A 107 -15.899 47.637 50.069 1.00 45.18 C
ATOM 838 CE1 HIS A 107 -14.740 49.267 50.967 1.00 46.58 C
ATOM 839 NE2 HIS A 107 -15.971 48.837 50.726 1.00 47.09 N
ATOM 840 N HIS A 108 -14.978 43.852 51.263 1.00 34.78 N
ATOM 841 CA HIS A 108 -15.969 43.388 52.230 1.00 32.97 C
ATOM 842 C HIS A 108 -15.273 42.867 53.461 1.00 35.13 C
ATOM 843 O HIS A 108 -15.733 43.126 54.577 1.00 40.68 O
ATOM 844 CB HIS A 108 -16.865 42.274 51.670 1.00 30.56 C
ATOM 845 CG HIS A 108 -17.694 41.582 52.722 1.00 31.68 C
ATOM 846 ND1 HIS A 108 -18.828 42.116 53.279 1.00 30.07 N
ATOM 847 CD2 HIS A 108 -17.518 40.387 53.341 1.00 31.24 C
ATOM 848 CE1 HIS A 108 -19.301 41.257 54.203 1.00 28.52 C
ATOM 849 NE2 HIS A 108 -18.545 40.184 54.287 1.00 27.49 N
ATOM 850 N VAL A 109 -14.197 42.104 53.276 1.00 31.57 N
ATOM 851 CA VAL A 109 -13.504 41.572 54.427 1.00 33.74 C
ATOM 852 C VAL A 109 -13.002 42.698 55.308 1.00 36.30 C
ATOM 853 O VAL A 109 -13.346 42.741 56.493 1.00 35.92 O
ATOM 854 CB VAL A 109 -12.360 40.571 54.068 1.00 33.17 C
ATOM 855 CG1 VAL A 109 -12.946 39.350 53.393 1.00 33.15 C
ATOM 856 CG2 VAL A 109 -11.322 41.203 53.173 1.00 35.09 C
ATOM 857 N SER A 110 -12.314 43.668 54.699 1.00 37.79 N
ATOM 858 CA SER A 110 -11.737 44.803 55.421 1.00 41.68 C
ATOM 859 C SER A 110 -12.809 45.609 56.127 1.00 44.42 C
ATOM 860 O SER A 110 -12.737 45.852 57.338 1.00 47.40 O
ATOM 861 CB SER A 110 -10.982 45.722 54.468 1.00 42.78 C
ATOM 862 OG SER A 110 -11.885 46.557 53.762 1.00 50.84 O
ATOM 863 N SER A 111 -13.834 45.982 55.374 1.00 44.02 N
ATOM 864 CA SER A 111 -14.927 46.757 55.926 1.00 45.10 C
ATOM 865 C SER A 111 -15.621 46.077 57.116 1.00 43.59 C
ATOM 866 O SER A 111 -16.446 46.694 57.779 1.00 46.57 O
ATOM 867 CB SER A 111 -15.932 47.076 54.823 1.00 45.68 C
ATOM 868 OG SER A 111 -16.439 45.886 54.239 1.00 51.83 O
ATOM 869 N HIS A 112 -15.292 44.816 57.383 1.00 43.66 N
ATOM 870 CA HIS A 112 -15.889 44.085 58.504 1.00 46.06 C
ATOM 871 C HIS A 112 -15.562 44.847 59.780 1.00 48.01 C
ATOM 872 O HIS A 112 -14.414 45.246 59.980 1.00 51.76 O
ATOM 873 CB HIS A 112 -15.311 42.661 58.599 1.00 44.84 C
ATOM 874 CG HIS A 112 -16.281 41.579 58.233 1.00 45.59 C
ATOM 875 ND1 HIS A 112 -17.227 41.064 59.100 1.00 48.58 N
ATOM 876 CD2 HIS A 112 -16.445 40.890 57.072 1.00 40.51 C
ATOM 877 CE1 HIS A 112 -17.915 40.104 58.458 1.00 43.64 C
ATOM 878 NE2 HIS A 112 -17.480 39.956 57.219 1.00 37.06 N
ATOM 879 N LYS A 113 -16.566 45.067 60.627 1.00 49.06 N
ATOM 880 CA LYS A 113 -16.373 45.796 61.887 1.00 49.63 C
ATOM 881 C LYS A 113 -15.670 44.911 62.930 1.00 48.39 C
ATOM 882 O LYS A 113 -16.108 43.796 63.201 1.00 46.16 O
ATOM 883 CB LYS A 113 -17.730 46.291 62.409 1.00 53.52 C
ATOM 884 CG LYS A 113 -17.688 47.365 63.497 1.00 58.56 C
ATOM 885 CD LYS A 113 -17.234 48.718 62.943 1.00 64.88 C
ATOM 886 CE LYS A 113 -17.370 49.835 63.998 1.00 67.80 C
ATOM 887 NZ LYS A 113 -16.774 51.160 63.600 1.00 64.07 N
ATOM 888 N GLU A 114 -14.564 45.402 63.487 1.00 50.24 N
ATOM 889 CA GLU A 114 -13.804 44.643 64.487 1.00 54.08 C
ATOM 890 C GLU A 114 -14.432 44.733 65.890 1.00 55.75 C
ATOM 891 O GLU A 114 -15.382 45.496 66.091 1.00 55.61 O
ATOM 892 CB GLU A 114 -12.349 45.136 64.539 1.00 56.18 C
ATOM 893 CG GLU A 114 -11.539 45.041 63.231 1.00 58.02 C
ATOM 894 CD GLU A 114 -10.016 45.190 63.453 1.00 61.52 C
ATOM 895 OE1 GLU A 114 -9.579 45.289 64.617 1.00 63.05 O
ATOM 896 OE2 GLU A 114 -9.240 45.179 62.475 1.00 60.48 O
ATOM 897 N SER A 115 -13.909 43.958 66.848 1.00 57.04 N
ATOM 898 CA SER A 115 -14.410 43.967 68.233 1.00 60.26 C
ATOM 899 C SER A 115 -14.097 45.294 68.957 1.00 64.33 C
ATOM 900 O SER A 115 -14.948 46.189 68.995 1.00 66.97 O
ATOM 901 CB SER A 115 -13.855 42.773 69.025 1.00 56.54 C
ATOM 902 OG SER A 115 -14.325 41.546 68.497 1.00 49.56 O
ATOM 903 N LYS A 116 -12.917 45.391 69.574 1.00 67.23 N
ATOM 904 CA LYS A 116 -12.447 46.605 70.266 1.00 70.68 C
ATOM 905 C LYS A 116 -13.443 47.331 71.180 1.00 72.84 C
ATOM 906 O LYS A 116 -12.991 48.296 71.847 1.00 73.36 O
ATOM 907 CB LYS A 116 -11.890 47.605 69.257 1.00 71.75 C
ATOM 908 CG LYS A 116 -10.857 47.017 68.362 1.00 73.74 C
ATOM 909 CD LYS A 116 -10.280 48.046 67.430 1.00 76.40 C
ATOM 910 CE LYS A 116 -9.353 47.345 66.476 1.00 77.72 C
ATOM 911 NZ LYS A 116 -8.413 48.212 65.726 1.00 78.48 N
TER 912 LYS A 116
HETATM 913 ZN ZN A 117 -3.674 28.883 46.574 1.00 23.28 ZN
HETATM 914 ZN ZN A 118 -2.582 28.847 42.854 1.00 24.14 ZN
HETATM 915 ZN ZN A 119 -0.311 23.240 29.837 1.00 23.33 ZN
HETATM 916 ZN ZN A 120 -18.665 39.074 55.936 1.00 34.77 ZN
HETATM 917 O HOH A 200 -8.645 41.408 37.078 1.00 32.34 O
HETATM 918 O HOH A 201 -22.203 34.367 53.789 1.00 28.66 O
HETATM 919 O HOH A 202 -21.025 31.496 42.941 1.00 11.52 O
HETATM 920 O HOH A 203 -10.979 23.198 42.905 1.00 35.10 O
HETATM 921 O HOH A 204 -6.441 21.665 28.398 1.00 22.93 O
HETATM 922 O HOH A 205 -7.924 33.755 27.548 1.00 17.21 O
HETATM 923 O HOH A 206 -12.362 39.225 25.736 1.00 29.10 O
HETATM 924 O HOH A 207 -16.604 39.368 68.155 1.00 48.60 O
HETATM 925 O HOH A 209 11.391 19.770 25.435 1.00 47.61 O
HETATM 926 O HOH A 210 -19.558 35.415 37.136 1.00 20.76 O
HETATM 927 O HOH A 211 -8.997 17.752 42.543 1.00 70.66 O
HETATM 928 O HOH A 212 -17.848 39.815 29.218 1.00 29.73 O
HETATM 929 O HOH A 213 0.354 24.858 23.327 1.00 39.34 O
HETATM 930 O HOH A 214 -20.053 22.709 42.510 1.00 41.65 O
HETATM 931 O HOH A 215 -0.550 35.214 42.541 1.00 28.15 O
HETATM 932 O HOH A 216 3.721 36.113 26.945 1.00 31.95 O
HETATM 933 O HOH A 217 -11.370 41.278 46.235 1.00 22.29 O
HETATM 934 O HOH A 218 -14.710 20.438 40.295 1.00 60.70 O
HETATM 935 O HOH A 219 -3.867 24.186 24.685 1.00 60.10 O
HETATM 936 O HOH A 220 -18.806 22.753 33.446 1.00 24.72 O
HETATM 937 O HOH A 221 -4.291 38.215 36.626 1.00 30.88 O
HETATM 938 O HOH A 222 -21.802 33.392 41.115 1.00 21.95 O
HETATM 939 O HOH A 223 -10.464 25.082 46.772 1.00 23.85 O
HETATM 940 O HOH A 224 -6.687 25.926 33.517 1.00 9.06 O
HETATM 941 O HOH A 226 -20.008 25.768 42.540 1.00 42.46 O
HETATM 942 O HOH A 227 -4.817 20.813 35.171 1.00 31.38 O
HETATM 943 O HOH A 228 -4.569 18.419 45.166 1.00 52.23 O
HETATM 944 O HOH A 229 -19.287 19.876 34.487 1.00 17.13 O
HETATM 945 O HOH A 230 -9.508 22.465 39.519 1.00 45.01 O
HETATM 946 O HOH A 231 0.065 35.419 58.587 1.00 41.28 O
HETATM 947 O HOH A 232 -8.045 28.603 55.402 1.00 72.69 O
HETATM 948 O HOH A 233 1.922 19.146 25.593 1.00 45.51 O
HETATM 949 O HOH A 234 -17.250 38.173 24.387 1.00 24.65 O
HETATM 950 O HOH A 235 -9.201 38.043 42.880 1.00 38.20 O
HETATM 951 O HOH A 236 -9.213 38.592 45.787 1.00 36.97 O
HETATM 952 O HOH A 237 -13.075 41.878 35.324 1.00 30.43 O
HETATM 953 O HOH A 238 -7.860 36.674 40.891 1.00 16.17 O
HETATM 954 O HOH A 239 -8.953 34.635 43.869 1.00 43.17 O
HETATM 955 O HOH A 240 -7.558 32.525 52.921 1.00 40.08 O
HETATM 956 O HOH A 241 -11.496 29.499 51.681 1.00 25.31 O
HETATM 957 O HOH A 242 5.209 22.297 41.811 1.00 19.13 O
HETATM 958 O HOH A 244 -8.278 27.167 35.413 1.00 12.83 O
HETATM 959 O HOH A 245 -8.077 32.807 45.674 1.00 34.04 O
HETATM 960 O HOH A 246 2.083 30.866 50.448 1.00 60.62 O
HETATM 961 O HOH A 247 -17.855 25.003 45.039 1.00 26.08 O
HETATM 962 O HOH A 248 -0.982 20.533 42.199 1.00 50.98 O
HETATM 963 O HOH A 249 -26.860 27.221 43.025 1.00 29.09 O
HETATM 964 O HOH A 250 -11.290 24.583 55.905 1.00 67.16 O
HETATM 965 O HOH A 251 10.262 34.797 25.020 1.00 57.85 O
HETATM 966 O HOH A 252 1.812 38.800 33.347 1.00 35.48 O
HETATM 967 O HOH A 253 -8.741 40.145 26.520 1.00 48.18 O
HETATM 968 O HOH A 254 -5.258 35.143 26.702 1.00 76.99 O
CONECT 14 913
CONECT 44 913
CONECT 199 914
CONECT 222 913 914
CONECT 238 913
CONECT 312 915
CONECT 328 915
CONECT 356 914
CONECT 381 914
CONECT 474 915
CONECT 493 915
CONECT 709 916
CONECT 744 916
CONECT 849 916
CONECT 878 916
CONECT 913 14 44 222 238
CONECT 914 199 222 356 381
CONECT 915 312 328 474 493
CONECT 916 709 744 849 878
MASTER 297 0 4 7 4 0 4 6 967 1 19 9
END
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