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3LCK_al.pdb
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HEADER TYROSINE-PROTEIN KINASE 08-APR-97 3LCK
TITLE THE KINASE DOMAIN OF HUMAN LYMPHOCYTE KINASE (LCK),
TITLE 2 ACTIVATED FORM (AUTO-PHOSPHORYLATED ON TYR394)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PROTEIN TYROSINE KINASE DOMAIN;
COMPND 5 SYNONYM: LCK;
COMPND 6 EC: 2.7.1.112;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: PHOSPHORYLATION ON TYR 394
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: SF9;
SOURCE 6 GENE: LCK;
SOURCE 7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 8 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 10 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 11 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PFASTBAC-1-BMON14272;
SOURCE 14 EXPRESSION_SYSTEM_GENE: POLYHEDRIN
KEYWDS TYROSINE-PROTEIN KINASE, ATP-BINDING, PHOSPHORYLATION,
KEYWDS 2 SIGNAL TRANSDUCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR H.YAMAGUCHI,W.A.HENDRICKSON
REVDAT 2 24-FEB-09 3LCK 1 VERSN
REVDAT 1 2 03-DEC-97 3LCK 0
JRNL AUTH H.YAMAGUCHI,W.A.HENDRICKSON
JRNL TITL STRUCTURAL BASIS FOR ACTIVATION OF HUMAN
JRNL TITL 2 LYMPHOCYTE KINASE LCK UPON TYROSINE
JRNL TITL 3 PHOSPHORYLATION.
JRNL REF NATURE V. 384 484 1996
JRNL REFN ISSN 0028-0836
JRNL PMID 8945479
JRNL DOI 10.1038/384484A0
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.1000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 31241
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : R FREE THROUGHOUT EXCEPT
REMARK 3 FOR THE LAST ROUND
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.78
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3876
REMARK 3 BIN R VALUE (WORKING SET) : 0.2090
REMARK 3 BIN FREE R VALUE : 0.2260
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 2347
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 340
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.37
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.90
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.86
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.45
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) : 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 : PARAM19X.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19.SOL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPH19X.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3LCK 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 : 21-JUL-96
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97950
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : SAGITTAL FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : FUJI
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31599
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 8.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.02800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 37.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.04700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 21.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR, MOLECULAR
REMARK 200 REPLACEMENT, MAD
REMARK 200 SOFTWARE USED: MADSYS
REMARK 200 STARTING MODEL: PDB ENTRY 1IRK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED IN HANGING
REMARK 280 DROPS WITH 1.6 M AMMONIUM SULFATE AND 0.1 M BISTRIS-HCL (PH
REMARK 280 6.5 @ RT) AS A WELL SOLUTION., VAPOR DIFFUSION - HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 21.02000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.58500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.81000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.58500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.02000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.81000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: 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 O HOH A 1070 O HOH A 1081 1.25
REMARK 500 O HOH A 1146 O HOH A 1163 1.47
REMARK 500 O HOH A 1150 O HOH A 1272 1.65
REMARK 500 O HOH A 1061 O HOH A 1081 1.66
REMARK 500 O HOH A 1223 O HOH A 1224 1.69
REMARK 500 NZ LYS A 405 O HOH A 1207 1.72
REMARK 500 O HOH A 1157 O HOH A 1259 1.86
REMARK 500 O HOH A 1061 O HOH A 1070 1.90
REMARK 500 O HOH A 1270 O HOH A 1278 1.94
REMARK 500 O HOH A 1095 O HOH A 1336 1.95
REMARK 500 O HOH A 1182 O HOH A 1239 2.01
REMARK 500 O HOH A 1240 O HOH A 1305 2.01
REMARK 500 O HOH A 1260 O HOH A 1301 2.02
REMARK 500 O HOH A 1145 O HOH A 1202 2.03
REMARK 500 CG2 ILE A 389 O ASP A 391 2.06
REMARK 500 O HOH A 1170 O HOH A 1239 2.08
REMARK 500 O HOH A 1117 O HOH A 1250 2.09
REMARK 500 NE2 GLN A 277 OE1 GLU A 310 2.14
REMARK 500 OE1 GLU A 454 O HOH A 1284 2.17
REMARK 500 O HOH A 1107 O HOH A 1178 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 267 NE2 HIS A 267 CD2 -0.068
REMARK 500 HIS A 267 NE2 HIS A 267 CD2 -0.067
REMARK 500 HIS A 362 NE2 HIS A 362 CD2 -0.066
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TRP A 233 CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 TRP A 233 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES
REMARK 500 TRP A 234 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TRP A 234 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES
REMARK 500 TRP A 238 CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 TRP A 238 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 TRP A 260 CD1 - CG - CD2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 TRP A 260 CG - CD1 - NE1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 TRP A 260 CE2 - CD2 - CG ANGL. DEV. = -7.2 DEGREES
REMARK 500 TRP A 406 CD1 - CG - CD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 TRP A 406 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 TRP A 424 CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 TRP A 424 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES
REMARK 500 TRP A 477 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP A 477 CE2 - CD2 - CG ANGL. DEV. = -5.2 DEGREES
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 ARG A 363 -2.05 71.69
REMARK 500 ASP A 382 81.26 54.21
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 A1300 DISTANCE = 5.35 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 901
DBREF 3LCK A 231 501 UNP P06239 LCK_HUMAN 230 500
SEQADV 3LCK PTR A 394 UNP P06239 TYR 393 CONFLICT
SEQRES 1 A 271 LYS PRO TRP TRP GLU ASP GLU TRP GLU VAL PRO ARG GLU
SEQRES 2 A 271 THR LEU LYS LEU VAL GLU ARG LEU GLY ALA GLY GLN PHE
SEQRES 3 A 271 GLY GLU VAL TRP MET GLY TYR TYR ASN GLY HIS THR LYS
SEQRES 4 A 271 VAL ALA VAL LYS SER LEU LYS GLN GLY SER MET SER PRO
SEQRES 5 A 271 ASP ALA PHE LEU ALA GLU ALA ASN LEU MET LYS GLN LEU
SEQRES 6 A 271 GLN HIS GLN ARG LEU VAL ARG LEU TYR ALA VAL VAL THR
SEQRES 7 A 271 GLN GLU PRO ILE TYR ILE ILE THR GLU TYR MET GLU ASN
SEQRES 8 A 271 GLY SER LEU VAL ASP PHE LEU LYS THR PRO SER GLY ILE
SEQRES 9 A 271 LYS LEU THR ILE ASN LYS LEU LEU ASP MET ALA ALA GLN
SEQRES 10 A 271 ILE ALA GLU GLY MET ALA PHE ILE GLU GLU ARG ASN TYR
SEQRES 11 A 271 ILE HIS ARG ASP LEU ARG ALA ALA ASN ILE LEU VAL SER
SEQRES 12 A 271 ASP THR LEU SER CYS LYS ILE ALA ASP PHE GLY LEU ALA
SEQRES 13 A 271 ARG LEU ILE GLU ASP ASN GLU PTR THR ALA ARG GLU GLY
SEQRES 14 A 271 ALA LYS PHE PRO ILE LYS TRP THR ALA PRO GLU ALA ILE
SEQRES 15 A 271 ASN TYR GLY THR PHE THR ILE LYS SER ASP VAL TRP SER
SEQRES 16 A 271 PHE GLY ILE LEU LEU THR GLU ILE VAL THR HIS GLY ARG
SEQRES 17 A 271 ILE PRO TYR PRO GLY MET THR ASN PRO GLU VAL ILE GLN
SEQRES 18 A 271 ASN LEU GLU ARG GLY TYR ARG MET VAL ARG PRO ASP ASN
SEQRES 19 A 271 CYS PRO GLU GLU LEU TYR GLN LEU MET ARG LEU CYS TRP
SEQRES 20 A 271 LYS GLU ARG PRO GLU ASP ARG PRO THR PHE ASP TYR LEU
SEQRES 21 A 271 ARG SER VAL LEU GLU ASP PHE PHE THR ALA THR
MODRES 3LCK PTR A 394 TYR O-PHOSPHOTYROSINE
HET PTR A 394 16
HET SO4 A 901 5
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM SO4 SULFATE ION
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 PTR C9 H12 N O6 P
FORMUL 2 SO4 O4 S 2-
FORMUL 3 HOH *340(H2 O)
LINK N PTR A 394 C GLU A 393 1555 1555
LINK C PTR A 394 N THR A 395 1555 1555
CISPEP 1 GLU A 310 PRO A 311 0 -1.26
SITE 1 AC1 9 GLN A 298 ARG A 299 SER A 377 LYS A 379
SITE 2 AC1 9 TYR A 457 ARG A 458 ARG A 474 HOH A1027
SITE 3 AC1 9 HOH A1248
CRYST1 42.040 73.620 91.170 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.023787 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013583 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010969 0.00000
ATOM 1 N LYS A 231 1.209 17.165 -20.081 1.00 16.21 N
ATOM 2 CA LYS A 231 0.441 18.397 -20.174 1.00 15.80 C
ATOM 3 C LYS A 231 1.176 19.552 -19.515 1.00 14.99 C
ATOM 4 O LYS A 231 1.931 19.350 -18.563 1.00 13.61 O
ATOM 5 CB LYS A 231 -0.907 18.222 -19.494 1.00 17.05 C
ATOM 6 CG LYS A 231 -1.755 17.145 -20.147 1.00 20.27 C
ATOM 7 CD LYS A 231 -3.069 17.006 -19.396 1.00 22.15 C
ATOM 8 CE LYS A 231 -3.975 16.019 -20.118 1.00 25.00 C
ATOM 9 NZ LYS A 231 -5.267 15.947 -19.460 1.00 28.64 N
ATOM 10 N PRO A 232 0.983 20.789 -19.982 1.00 14.02 N
ATOM 11 CA PRO A 232 1.495 21.981 -19.324 1.00 12.59 C
ATOM 12 C PRO A 232 0.922 22.043 -17.917 1.00 11.18 C
ATOM 13 O PRO A 232 -0.156 21.505 -17.655 1.00 9.36 O
ATOM 14 CB PRO A 232 1.052 23.112 -20.227 1.00 13.41 C
ATOM 15 CG PRO A 232 -0.221 22.576 -20.842 1.00 14.82 C
ATOM 16 CD PRO A 232 0.156 21.125 -21.135 1.00 15.15 C
ATOM 17 N TRP A 233 1.608 22.691 -16.978 1.00 10.27 N
ATOM 18 CA TRP A 233 1.097 22.710 -15.622 1.00 10.13 C
ATOM 19 C TRP A 233 -0.305 23.299 -15.523 1.00 10.13 C
ATOM 20 O TRP A 233 -1.076 22.898 -14.652 1.00 8.94 O
ATOM 21 CB TRP A 233 2.047 23.499 -14.716 1.00 9.37 C
ATOM 22 CG TRP A 233 2.130 24.999 -14.986 1.00 8.49 C
ATOM 23 CD1 TRP A 233 3.168 25.538 -15.697 1.00 8.75 C
ATOM 24 CD2 TRP A 233 1.240 25.947 -14.547 1.00 7.59 C
ATOM 25 NE1 TRP A 233 2.933 26.828 -15.705 1.00 9.14 N
ATOM 26 CE2 TRP A 233 1.802 27.113 -15.037 1.00 8.55 C
ATOM 27 CE3 TRP A 233 0.068 25.980 -13.823 1.00 8.53 C
ATOM 28 CZ2 TRP A 233 1.201 28.336 -14.810 1.00 8.04 C
ATOM 29 CZ3 TRP A 233 -0.535 27.202 -13.593 1.00 7.58 C
ATOM 30 CH2 TRP A 233 0.026 28.368 -14.083 1.00 8.25 C
ATOM 31 N TRP A 234 -0.694 24.235 -16.398 1.00 9.14 N
ATOM 32 CA TRP A 234 -2.030 24.804 -16.307 1.00 9.12 C
ATOM 33 C TRP A 234 -3.123 23.860 -16.781 1.00 8.48 C
ATOM 34 O TRP A 234 -4.314 24.140 -16.650 1.00 9.20 O
ATOM 35 CB TRP A 234 -2.105 26.115 -17.110 1.00 8.11 C
ATOM 36 CG TRP A 234 -1.650 26.033 -18.561 1.00 6.96 C
ATOM 37 CD1 TRP A 234 -2.517 25.691 -19.567 1.00 7.96 C
ATOM 38 CD2 TRP A 234 -0.387 26.301 -19.022 1.00 8.14 C
ATOM 39 NE1 TRP A 234 -1.800 25.745 -20.663 1.00 6.87 N
ATOM 40 CE2 TRP A 234 -0.535 26.101 -20.382 1.00 8.14 C
ATOM 41 CE3 TRP A 234 0.834 26.673 -18.492 1.00 11.26 C
ATOM 42 CZ2 TRP A 234 0.533 26.272 -21.240 1.00 10.32 C
ATOM 43 CZ3 TRP A 234 1.906 26.842 -19.348 1.00 11.97 C
ATOM 44 CH2 TRP A 234 1.756 26.643 -20.709 1.00 11.98 C
ATOM 45 N GLU A 235 -2.749 22.714 -17.344 1.00 8.90 N
ATOM 46 CA GLU A 235 -3.741 21.728 -17.729 1.00 10.36 C
ATOM 47 C GLU A 235 -3.525 20.443 -16.942 1.00 11.19 C
ATOM 48 O GLU A 235 -4.390 19.572 -16.867 1.00 12.29 O
ATOM 49 CB GLU A 235 -3.642 21.408 -19.217 1.00 10.89 C
ATOM 50 CG GLU A 235 -3.978 22.577 -20.125 1.00 13.76 C
ATOM 51 CD GLU A 235 -4.135 22.144 -21.570 1.00 17.14 C
ATOM 52 OE1 GLU A 235 -3.991 20.954 -21.840 1.00 19.20 O
ATOM 53 OE2 GLU A 235 -4.410 22.992 -22.419 1.00 20.17 O
ATOM 54 N ASP A 236 -2.348 20.304 -16.336 1.00 11.83 N
ATOM 55 CA ASP A 236 -2.036 19.094 -15.598 1.00 13.01 C
ATOM 56 C ASP A 236 -2.965 18.875 -14.409 1.00 12.38 C
ATOM 57 O ASP A 236 -3.117 19.732 -13.541 1.00 11.11 O
ATOM 58 CB ASP A 236 -0.598 19.173 -15.121 1.00 15.07 C
ATOM 59 CG ASP A 236 -0.141 17.846 -14.557 1.00 19.28 C
ATOM 60 OD1 ASP A 236 0.178 16.956 -15.346 1.00 22.90 O
ATOM 61 OD2 ASP A 236 -0.111 17.703 -13.337 1.00 21.07 O
ATOM 62 N GLU A 237 -3.596 17.705 -14.333 1.00 12.39 N
ATOM 63 CA GLU A 237 -4.530 17.432 -13.252 1.00 13.88 C
ATOM 64 C GLU A 237 -3.920 17.334 -11.857 1.00 11.64 C
ATOM 65 O GLU A 237 -4.624 17.397 -10.849 1.00 11.36 O
ATOM 66 CB GLU A 237 -5.284 16.141 -13.573 1.00 16.80 C
ATOM 67 CG GLU A 237 -4.430 15.098 -14.290 1.00 24.81 C
ATOM 68 CD GLU A 237 -4.048 15.501 -15.713 1.00 27.82 C
ATOM 69 OE1 GLU A 237 -4.921 15.970 -16.447 1.00 31.56 O
ATOM 70 OE2 GLU A 237 -2.884 15.344 -16.090 1.00 30.94 O
ATOM 71 N TRP A 238 -2.602 17.182 -11.761 1.00 9.32 N
ATOM 72 CA TRP A 238 -1.959 17.090 -10.463 1.00 7.72 C
ATOM 73 C TRP A 238 -1.470 18.420 -9.913 1.00 6.01 C
ATOM 74 O TRP A 238 -1.181 18.552 -8.725 1.00 5.41 O
ATOM 75 CB TRP A 238 -0.781 16.126 -10.547 1.00 7.58 C
ATOM 76 CG TRP A 238 -1.219 14.672 -10.536 1.00 9.64 C
ATOM 77 CD1 TRP A 238 -1.340 13.985 -9.358 1.00 10.99 C
ATOM 78 CD2 TRP A 238 -1.531 13.907 -11.627 1.00 11.61 C
ATOM 79 NE1 TRP A 238 -1.728 12.781 -9.700 1.00 12.60 N
ATOM 80 CE2 TRP A 238 -1.851 12.695 -11.036 1.00 12.94 C
ATOM 81 CE3 TRP A 238 -1.585 14.064 -12.996 1.00 11.57 C
ATOM 82 CZ2 TRP A 238 -2.236 11.616 -11.800 1.00 13.56 C
ATOM 83 CZ3 TRP A 238 -1.970 12.985 -13.762 1.00 13.41 C
ATOM 84 CH2 TRP A 238 -2.288 11.774 -13.172 1.00 15.45 C
ATOM 85 N GLU A 239 -1.365 19.447 -10.751 1.00 6.13 N
ATOM 86 CA GLU A 239 -0.861 20.728 -10.288 1.00 5.11 C
ATOM 87 C GLU A 239 -1.809 21.418 -9.313 1.00 5.61 C
ATOM 88 O GLU A 239 -3.015 21.483 -9.553 1.00 5.36 O
ATOM 89 CB GLU A 239 -0.633 21.650 -11.482 1.00 6.11 C
ATOM 90 CG GLU A 239 0.068 22.953 -11.124 1.00 6.30 C
ATOM 91 CD GLU A 239 1.573 22.811 -10.934 1.00 8.35 C
ATOM 92 OE1 GLU A 239 2.146 21.869 -11.484 1.00 7.02 O
ATOM 93 OE2 GLU A 239 2.170 23.644 -10.252 1.00 6.74 O
ATOM 94 N VAL A 240 -1.307 21.934 -8.189 1.00 4.42 N
ATOM 95 CA VAL A 240 -2.160 22.679 -7.276 1.00 4.15 C
ATOM 96 C VAL A 240 -1.451 23.959 -6.844 1.00 5.01 C
ATOM 97 O VAL A 240 -0.222 24.021 -6.793 1.00 5.22 O
ATOM 98 CB VAL A 240 -2.499 21.864 -6.002 1.00 2.27 C
ATOM 99 CG1 VAL A 240 -3.227 20.586 -6.386 1.00 2.47 C
ATOM 100 CG2 VAL A 240 -1.223 21.561 -5.232 1.00 3.50 C
ATOM 101 N PRO A 241 -2.198 25.021 -6.535 1.00 4.42 N
ATOM 102 CA PRO A 241 -1.678 26.258 -5.975 1.00 5.20 C
ATOM 103 C PRO A 241 -0.922 25.955 -4.697 1.00 5.24 C
ATOM 104 O PRO A 241 -1.378 25.151 -3.887 1.00 6.17 O
ATOM 105 CB PRO A 241 -2.904 27.111 -5.744 1.00 4.43 C
ATOM 106 CG PRO A 241 -3.880 26.592 -6.766 1.00 5.23 C
ATOM 107 CD PRO A 241 -3.641 25.084 -6.713 1.00 5.26 C
ATOM 108 N ARG A 242 0.225 26.577 -4.456 1.00 5.40 N
ATOM 109 CA ARG A 242 0.959 26.255 -3.252 1.00 6.14 C
ATOM 110 C ARG A 242 0.148 26.661 -2.024 1.00 7.69 C
ATOM 111 O ARG A 242 0.336 26.118 -0.937 1.00 7.20 O
ATOM 112 CB ARG A 242 2.296 26.982 -3.250 1.00 8.09 C
ATOM 113 CG ARG A 242 3.282 26.367 -2.266 1.00 8.76 C
ATOM 114 CD ARG A 242 4.514 27.248 -2.085 1.00 11.88 C
ATOM 115 NE ARG A 242 5.131 27.609 -3.351 1.00 10.97 N
ATOM 116 CZ ARG A 242 6.014 26.809 -3.944 1.00 11.07 C
ATOM 117 NH1 ARG A 242 6.361 25.650 -3.390 1.00 10.59 N
ATOM 118 NH2 ARG A 242 6.548 27.181 -5.102 1.00 11.63 N
ATOM 119 N GLU A 243 -0.793 27.599 -2.172 1.00 7.06 N
ATOM 120 CA GLU A 243 -1.599 28.040 -1.042 1.00 7.61 C
ATOM 121 C GLU A 243 -2.530 26.968 -0.496 1.00 7.60 C
ATOM 122 O GLU A 243 -3.093 27.110 0.591 1.00 6.77 O
ATOM 123 CB GLU A 243 -2.470 29.235 -1.418 1.00 10.91 C
ATOM 124 CG GLU A 243 -1.717 30.497 -1.809 1.00 17.01 C
ATOM 125 CD GLU A 243 -1.029 30.423 -3.165 1.00 20.07 C
ATOM 126 OE1 GLU A 243 -1.381 29.556 -3.965 1.00 19.16 O
ATOM 127 OE2 GLU A 243 -0.147 31.243 -3.421 1.00 23.90 O
ATOM 128 N THR A 244 -2.746 25.890 -1.249 1.00 7.10 N
ATOM 129 CA THR A 244 -3.627 24.835 -0.787 1.00 6.30 C
ATOM 130 C THR A 244 -2.910 23.952 0.224 1.00 6.43 C
ATOM 131 O THR A 244 -3.498 23.060 0.834 1.00 6.07 O
ATOM 132 CB THR A 244 -4.086 23.980 -1.976 1.00 6.42 C
ATOM 133 OG1 THR A 244 -2.935 23.287 -2.444 1.00 5.48 O
ATOM 134 CG2 THR A 244 -4.715 24.812 -3.090 1.00 6.38 C
ATOM 135 N LEU A 245 -1.618 24.204 0.441 1.00 6.01 N
ATOM 136 CA LEU A 245 -0.842 23.353 1.330 1.00 7.09 C
ATOM 137 C LEU A 245 -0.318 24.040 2.578 1.00 8.00 C
ATOM 138 O LEU A 245 0.094 25.202 2.575 1.00 8.21 O
ATOM 139 CB LEU A 245 0.350 22.772 0.575 1.00 6.80 C
ATOM 140 CG LEU A 245 0.078 21.869 -0.629 1.00 7.25 C
ATOM 141 CD1 LEU A 245 1.352 21.741 -1.450 1.00 6.70 C
ATOM 142 CD2 LEU A 245 -0.431 20.512 -0.159 1.00 5.68 C
ATOM 143 N LYS A 246 -0.335 23.294 3.677 1.00 7.73 N
ATOM 144 CA LYS A 246 0.232 23.795 4.906 1.00 9.33 C
ATOM 145 C LYS A 246 1.198 22.732 5.396 1.00 8.87 C
ATOM 146 O LYS A 246 0.804 21.607 5.705 1.00 7.97 O
ATOM 147 CB LYS A 246 -0.836 24.010 5.964 1.00 10.98 C
ATOM 148 CG LYS A 246 -0.230 24.636 7.209 1.00 17.01 C
ATOM 149 CD LYS A 246 -1.194 24.514 8.380 1.00 23.00 C
ATOM 150 CE LYS A 246 -0.563 25.092 9.638 1.00 26.38 C
ATOM 151 NZ LYS A 246 -1.313 24.684 10.814 1.00 30.26 N
ATOM 152 N ALEU A 247 2.494 23.031 5.443 0.60 8.61 N
ATOM 153 N BLEU A 247 2.485 23.063 5.462 0.40 8.36 N
ATOM 154 CA ALEU A 247 3.437 22.051 5.950 0.60 9.06 C
ATOM 155 CA BLEU A 247 3.463 22.109 5.949 0.40 8.57 C
ATOM 156 C ALEU A 247 3.484 22.164 7.463 0.60 9.54 C
ATOM 157 C BLEU A 247 3.471 22.173 7.469 0.40 9.11 C
ATOM 158 O ALEU A 247 3.766 23.222 8.022 0.60 10.40 O
ATOM 159 O BLEU A 247 3.719 23.227 8.054 0.40 9.66 O
ATOM 160 CB ALEU A 247 4.820 22.306 5.354 0.60 8.98 C
ATOM 161 CB BLEU A 247 4.839 22.465 5.397 0.40 7.78 C
ATOM 162 CG ALEU A 247 4.989 21.924 3.887 0.60 8.52 C
ATOM 163 CG BLEU A 247 4.943 22.579 3.882 0.40 7.25 C
ATOM 164 CD1ALEU A 247 3.922 22.614 3.053 0.60 9.47 C
ATOM 165 CD1BLEU A 247 6.374 22.889 3.484 0.40 7.59 C
ATOM 166 CD2ALEU A 247 6.378 22.310 3.418 0.60 8.63 C
ATOM 167 CD2BLEU A 247 4.494 21.275 3.245 0.40 5.77 C
ATOM 168 N VAL A 248 3.200 21.070 8.160 1.00 9.40 N
ATOM 169 CA VAL A 248 3.134 21.131 9.609 1.00 9.96 C
ATOM 170 C VAL A 248 4.289 20.525 10.393 1.00 10.94 C
ATOM 171 O VAL A 248 4.750 21.094 11.384 1.00 10.90 O
ATOM 172 CB VAL A 248 1.809 20.480 10.030 1.00 8.71 C
ATOM 173 CG1 VAL A 248 1.708 20.431 11.544 1.00 12.57 C
ATOM 174 CG2 VAL A 248 0.658 21.281 9.449 1.00 9.66 C
ATOM 175 N GLU A 249 4.791 19.362 9.985 1.00 10.86 N
ATOM 176 CA GLU A 249 5.861 18.733 10.734 1.00 11.12 C
ATOM 177 C GLU A 249 6.935 18.234 9.781 1.00 11.70 C
ATOM 178 O GLU A 249 6.662 17.462 8.862 1.00 10.08 O
ATOM 179 CB GLU A 249 5.311 17.560 11.537 1.00 11.69 C
ATOM 180 CG GLU A 249 6.400 16.828 12.312 1.00 17.48 C
ATOM 181 CD GLU A 249 5.931 15.565 13.023 1.00 19.99 C
ATOM 182 OE1 GLU A 249 4.730 15.409 13.235 1.00 23.92 O
ATOM 183 OE2 GLU A 249 6.770 14.732 13.365 1.00 22.26 O
ATOM 184 N ARG A 250 8.183 18.662 9.942 1.00 11.05 N
ATOM 185 CA ARG A 250 9.187 18.148 9.036 1.00 12.21 C
ATOM 186 C ARG A 250 9.588 16.754 9.492 1.00 12.32 C
ATOM 187 O ARG A 250 9.943 16.522 10.647 1.00 13.24 O
ATOM 188 CB ARG A 250 10.406 19.053 9.024 1.00 12.24 C
ATOM 189 CG ARG A 250 11.367 18.599 7.941 1.00 16.30 C
ATOM 190 CD ARG A 250 12.552 19.536 7.887 1.00 20.13 C
ATOM 191 NE ARG A 250 13.136 19.656 9.206 1.00 24.09 N
ATOM 192 CZ ARG A 250 13.528 20.851 9.637 1.00 27.53 C
ATOM 193 NH1 ARG A 250 13.386 21.918 8.852 1.00 28.47 N
ATOM 194 NH2 ARG A 250 14.036 20.986 10.862 1.00 29.34 N
ATOM 195 N LEU A 251 9.513 15.786 8.585 1.00 11.14 N
ATOM 196 CA LEU A 251 9.840 14.419 8.932 1.00 10.02 C
ATOM 197 C LEU A 251 11.281 14.099 8.606 1.00 11.33 C
ATOM 198 O LEU A 251 11.887 13.182 9.160 1.00 11.59 O
ATOM 199 CB LEU A 251 8.943 13.470 8.170 1.00 9.46 C
ATOM 200 CG LEU A 251 7.454 13.660 8.384 1.00 9.82 C
ATOM 201 CD1 LEU A 251 6.681 12.699 7.497 1.00 9.96 C
ATOM 202 CD2 LEU A 251 7.126 13.429 9.850 1.00 9.85 C
ATOM 203 N GLY A 252 11.847 14.857 7.676 1.00 11.35 N
ATOM 204 CA GLY A 252 13.212 14.587 7.289 1.00 12.59 C
ATOM 205 C GLY A 252 13.800 15.714 6.468 1.00 12.50 C
ATOM 206 O GLY A 252 13.114 16.534 5.860 1.00 11.55 O
ATOM 207 N ALA A 253 15.125 15.738 6.469 1.00 12.90 N
ATOM 208 CA ALA A 253 15.837 16.746 5.722 1.00 13.42 C
ATOM 209 C ALA A 253 17.123 16.120 5.216 1.00 14.94 C
ATOM 210 O ALA A 253 17.786 15.358 5.918 1.00 15.53 O
ATOM 211 CB ALA A 253 16.188 17.926 6.609 1.00 13.57 C
ATOM 212 N GLY A 254 17.474 16.425 3.972 1.00 13.58 N
ATOM 213 CA GLY A 254 18.672 15.860 3.399 1.00 12.15 C
ATOM 214 C GLY A 254 19.290 16.789 2.373 1.00 11.12 C
ATOM 215 O GLY A 254 18.915 17.945 2.189 1.00 10.73 O
ATOM 216 N GLN A 255 20.273 16.229 1.690 1.00 11.79 N
ATOM 217 CA GLN A 255 21.012 16.968 0.696 1.00 12.84 C
ATOM 218 C GLN A 255 20.151 17.557 -0.415 1.00 12.24 C
ATOM 219 O GLN A 255 20.457 18.613 -0.964 1.00 10.94 O
ATOM 220 CB GLN A 255 22.060 16.015 0.127 1.00 14.08 C
ATOM 221 CG GLN A 255 23.064 16.666 -0.801 1.00 15.81 C
ATOM 222 CD GLN A 255 24.067 15.666 -1.350 1.00 16.07 C
ATOM 223 OE1 GLN A 255 24.205 14.547 -0.854 1.00 17.33 O
ATOM 224 NE2 GLN A 255 24.782 16.041 -2.404 1.00 16.83 N
ATOM 225 N PHE A 256 19.039 16.906 -0.760 1.00 12.39 N
ATOM 226 CA PHE A 256 18.243 17.360 -1.889 1.00 12.80 C
ATOM 227 C PHE A 256 16.910 17.991 -1.519 1.00 12.58 C
ATOM 228 O PHE A 256 16.072 18.255 -2.384 1.00 11.81 O
ATOM 229 CB PHE A 256 17.994 16.182 -2.811 1.00 13.74 C
ATOM 230 CG PHE A 256 19.280 15.477 -3.193 1.00 16.19 C
ATOM 231 CD1 PHE A 256 20.245 16.148 -3.917 1.00 15.99 C
ATOM 232 CD2 PHE A 256 19.475 14.165 -2.809 1.00 17.29 C
ATOM 233 CE1 PHE A 256 21.417 15.495 -4.255 1.00 17.47 C
ATOM 234 CE2 PHE A 256 20.648 13.523 -3.152 1.00 17.64 C
ATOM 235 CZ PHE A 256 21.621 14.184 -3.873 1.00 17.43 C
ATOM 236 N GLY A 257 16.671 18.237 -0.234 1.00 11.64 N
ATOM 237 CA GLY A 257 15.414 18.834 0.173 1.00 11.22 C
ATOM 238 C GLY A 257 14.903 18.241 1.479 1.00 10.42 C
ATOM 239 O GLY A 257 15.626 17.620 2.258 1.00 11.37 O
ATOM 240 N GLU A 258 13.604 18.406 1.709 1.00 9.18 N
ATOM 241 CA GLU A 258 12.977 17.937 2.928 1.00 8.91 C
ATOM 242 C GLU A 258 11.658 17.223 2.648 1.00 7.68 C
ATOM 243 O GLU A 258 11.043 17.325 1.594 1.00 6.79 O
ATOM 244 CB GLU A 258 12.692 19.117 3.868 1.00 13.23 C
ATOM 245 CG GLU A 258 13.865 20.063 4.065 1.00 16.26 C
ATOM 246 CD GLU A 258 13.548 21.235 4.995 1.00 21.28 C
ATOM 247 OE1 GLU A 258 12.425 21.751 4.939 1.00 22.29 O
ATOM 248 OE2 GLU A 258 14.432 21.630 5.763 1.00 23.58 O
ATOM 249 N AVAL A 259 11.230 16.466 3.651 0.77 6.68 N
ATOM 250 N BVAL A 259 11.225 16.477 3.663 0.23 7.22 N
ATOM 251 CA AVAL A 259 9.962 15.764 3.621 0.77 6.42 C
ATOM 252 CA BVAL A 259 9.969 15.753 3.629 0.23 6.94 C
ATOM 253 C AVAL A 259 9.154 16.199 4.834 0.77 6.61 C
ATOM 254 C BVAL A 259 9.155 16.189 4.839 0.23 6.69 C
ATOM 255 O AVAL A 259 9.610 16.170 5.977 0.77 6.17 O
ATOM 256 O BVAL A 259 9.593 16.150 5.987 0.23 6.58 O
ATOM 257 CB AVAL A 259 10.184 14.255 3.669 0.77 6.71 C
ATOM 258 CB BVAL A 259 10.225 14.240 3.678 0.23 7.11 C
ATOM 259 CG1AVAL A 259 8.845 13.532 3.767 0.77 7.34 C
ATOM 260 CG1BVAL A 259 10.983 13.894 4.945 0.23 7.22 C
ATOM 261 CG2AVAL A 259 10.893 13.808 2.399 0.77 5.86 C
ATOM 262 CG2BVAL A 259 8.900 13.498 3.643 0.23 7.25 C
ATOM 263 N TRP A 260 7.928 16.637 4.571 1.00 5.96 N
ATOM 264 CA TRP A 260 7.063 17.137 5.624 1.00 5.35 C
ATOM 265 C TRP A 260 5.703 16.437 5.647 1.00 6.63 C
ATOM 266 O TRP A 260 5.204 15.869 4.669 1.00 5.10 O
ATOM 267 CB TRP A 260 6.786 18.635 5.430 1.00 7.78 C
ATOM 268 CG TRP A 260 7.924 19.603 5.638 1.00 8.83 C
ATOM 269 CD1 TRP A 260 9.009 19.634 4.818 1.00 9.20 C
ATOM 270 CD2 TRP A 260 7.933 20.534 6.636 1.00 9.40 C
ATOM 271 NE1 TRP A 260 9.723 20.610 5.306 1.00 9.64 N
ATOM 272 CE2 TRP A 260 9.128 21.163 6.370 1.00 10.16 C
ATOM 273 CE3 TRP A 260 7.119 20.914 7.684 1.00 8.95 C
ATOM 274 CZ2 TRP A 260 9.544 22.201 7.164 1.00 10.51 C
ATOM 275 CZ3 TRP A 260 7.540 21.962 8.483 1.00 11.87 C
ATOM 276 CH2 TRP A 260 8.742 22.587 8.210 1.00 9.80 C
ATOM 277 N MET A 261 5.096 16.471 6.830 1.00 5.74 N
ATOM 278 CA MET A 261 3.719 16.045 6.985 1.00 5.59 C
ATOM 279 C MET A 261 2.936 17.347 6.927 1.00 5.90 C
ATOM 280 O MET A 261 3.245 18.318 7.622 1.00 7.08 O
ATOM 281 CB MET A 261 3.501 15.363 8.328 1.00 7.03 C
ATOM 282 CG MET A 261 2.062 14.966 8.669 1.00 7.80 C
ATOM 283 SD MET A 261 0.929 16.312 9.111 1.00 10.08 S
ATOM 284 CE MET A 261 1.373 16.498 10.813 1.00 11.00 C
ATOM 285 N GLY A 262 1.935 17.401 6.061 1.00 4.92 N
ATOM 286 CA GLY A 262 1.153 18.610 5.941 1.00 4.08 C
ATOM 287 C GLY A 262 -0.299 18.309 5.632 1.00 2.27 C
ATOM 288 O GLY A 262 -0.761 17.169 5.644 1.00 2.00 O
ATOM 289 N TYR A 263 -1.031 19.379 5.346 1.00 3.18 N
ATOM 290 CA TYR A 263 -2.442 19.265 5.037 1.00 3.58 C
ATOM 291 C TYR A 263 -2.780 20.011 3.758 1.00 2.77 C
ATOM 292 O TYR A 263 -2.306 21.114 3.492 1.00 4.04 O
ATOM 293 CB TYR A 263 -3.301 19.839 6.165 1.00 4.41 C
ATOM 294 CG TYR A 263 -3.237 19.006 7.429 1.00 6.28 C
ATOM 295 CD1 TYR A 263 -4.070 17.913 7.551 1.00 8.24 C
ATOM 296 CD2 TYR A 263 -2.341 19.321 8.429 1.00 10.19 C
ATOM 297 CE1 TYR A 263 -4.010 17.121 8.674 1.00 10.25 C
ATOM 298 CE2 TYR A 263 -2.278 18.530 9.555 1.00 10.81 C
ATOM 299 CZ TYR A 263 -3.111 17.438 9.666 1.00 12.04 C
ATOM 300 OH TYR A 263 -3.032 16.627 10.780 1.00 16.24 O
ATOM 301 N TYR A 264 -3.594 19.367 2.935 1.00 3.84 N
ATOM 302 CA TYR A 264 -4.090 19.970 1.710 1.00 4.44 C
ATOM 303 C TYR A 264 -5.503 20.456 1.990 1.00 3.16 C
ATOM 304 O TYR A 264 -6.359 19.701 2.451 1.00 4.15 O
ATOM 305 CB TYR A 264 -4.112 18.944 0.575 1.00 4.60 C
ATOM 306 CG TYR A 264 -4.831 19.460 -0.658 1.00 5.66 C
ATOM 307 CD1 TYR A 264 -4.146 20.211 -1.596 1.00 3.98 C
ATOM 308 CD2 TYR A 264 -6.178 19.179 -0.820 1.00 6.06 C
ATOM 309 CE1 TYR A 264 -4.816 20.688 -2.703 1.00 5.22 C
ATOM 310 CE2 TYR A 264 -6.849 19.656 -1.928 1.00 7.30 C
ATOM 311 CZ TYR A 264 -6.159 20.408 -2.857 1.00 6.64 C
ATOM 312 OH TYR A 264 -6.835 20.898 -3.954 1.00 8.03 O
ATOM 313 N ASN A 265 -5.742 21.732 1.695 1.00 4.96 N
ATOM 314 CA ASN A 265 -7.021 22.368 1.956 1.00 4.78 C
ATOM 315 C ASN A 265 -7.555 22.091 3.355 1.00 4.48 C
ATOM 316 O ASN A 265 -8.718 21.754 3.589 1.00 5.58 O
ATOM 317 CB ASN A 265 -8.044 21.925 0.898 1.00 6.42 C
ATOM 318 CG ASN A 265 -7.907 22.709 -0.406 1.00 7.68 C
ATOM 319 OD1 ASN A 265 -8.778 22.652 -1.276 1.00 9.95 O
ATOM 320 ND2 ASN A 265 -6.834 23.474 -0.592 1.00 5.04 N
ATOM 321 N GLY A 266 -6.621 22.258 4.290 1.00 4.49 N
ATOM 322 CA GLY A 266 -6.891 22.157 5.712 1.00 5.33 C
ATOM 323 C GLY A 266 -7.212 20.786 6.287 1.00 4.71 C
ATOM 324 O GLY A 266 -6.796 20.484 7.405 1.00 5.89 O
ATOM 325 N AHIS A 267 -7.913 19.907 5.573 0.49 4.35 N
ATOM 326 N BHIS A 267 -7.902 19.911 5.561 0.51 4.57 N
ATOM 327 CA AHIS A 267 -8.325 18.647 6.168 0.49 4.57 C
ATOM 328 CA BHIS A 267 -8.327 18.653 6.149 0.51 4.85 C
ATOM 329 C AHIS A 267 -7.632 17.372 5.716 0.49 4.38 C
ATOM 330 C BHIS A 267 -7.652 17.367 5.702 0.51 4.47 C
ATOM 331 O AHIS A 267 -7.683 16.362 6.419 0.49 4.76 O
ATOM 332 O BHIS A 267 -7.735 16.352 6.396 0.51 4.49 O
ATOM 333 CB AHIS A 267 -9.812 18.439 5.948 0.49 4.23 C
ATOM 334 CB BHIS A 267 -9.818 18.493 5.927 0.51 4.76 C
ATOM 335 CG AHIS A 267 -10.680 19.517 6.571 0.49 4.08 C
ATOM 336 CG BHIS A 267 -10.616 19.573 6.630 0.51 4.48 C
ATOM 337 ND1AHIS A 267 -11.476 20.371 5.941 0.49 5.39 N
ATOM 338 ND1BHIS A 267 -10.677 19.794 7.936 0.51 4.23 N
ATOM 339 CD2AHIS A 267 -10.791 19.749 7.921 0.49 4.14 C
ATOM 340 CD2BHIS A 267 -11.417 20.496 6.003 0.51 5.80 C
ATOM 341 CE1AHIS A 267 -12.066 21.109 6.849 0.49 5.06 C
ATOM 342 CE1BHIS A 267 -11.483 20.806 8.130 0.51 6.51 C
ATOM 343 NE2AHIS A 267 -11.648 20.727 8.033 0.49 6.43 N
ATOM 344 NE2BHIS A 267 -11.921 21.223 6.963 0.51 5.58 N
ATOM 345 N THR A 268 -6.993 17.343 4.550 1.00 3.83 N
ATOM 346 CA THR A 268 -6.410 16.092 4.092 1.00 2.87 C
ATOM 347 C THR A 268 -4.924 15.978 4.370 1.00 2.05 C
ATOM 348 O THR A 268 -4.117 16.748 3.854 1.00 4.25 O
ATOM 349 CB THR A 268 -6.678 15.945 2.582 1.00 2.23 C
ATOM 350 OG1 THR A 268 -8.086 16.086 2.409 1.00 3.36 O
ATOM 351 CG2 THR A 268 -6.197 14.607 2.024 1.00 2.00 C
ATOM 352 N LYS A 269 -4.545 14.998 5.187 1.00 2.08 N
ATOM 353 CA LYS A 269 -3.147 14.813 5.537 1.00 2.00 C
ATOM 354 C LYS A 269 -2.384 14.244 4.354 1.00 2.56 C
ATOM 355 O LYS A 269 -2.820 13.290 3.710 1.00 2.51 O
ATOM 356 CB LYS A 269 -3.045 13.861 6.709 1.00 3.83 C
ATOM 357 CG LYS A 269 -1.731 13.966 7.452 1.00 7.50 C
ATOM 358 CD LYS A 269 -1.883 13.085 8.677 1.00 12.53 C
ATOM 359 CE LYS A 269 -1.056 13.616 9.831 1.00 16.88 C
ATOM 360 NZ LYS A 269 -1.306 12.828 11.026 1.00 20.23 N
ATOM 361 N VAL A 270 -1.228 14.845 4.073 1.00 3.00 N
ATOM 362 CA VAL A 270 -0.407 14.433 2.950 1.00 3.30 C
ATOM 363 C VAL A 270 1.071 14.548 3.297 1.00 3.25 C
ATOM 364 O VAL A 270 1.460 15.211 4.262 1.00 3.06 O
ATOM 365 CB VAL A 270 -0.681 15.317 1.709 1.00 2.69 C
ATOM 366 CG1 VAL A 270 -2.118 15.135 1.243 1.00 3.85 C
ATOM 367 CG2 VAL A 270 -0.404 16.781 2.060 1.00 3.46 C
ATOM 368 N ALA A 271 1.912 13.870 2.516 1.00 3.09 N
ATOM 369 CA ALA A 271 3.350 14.020 2.666 1.00 2.00 C
ATOM 370 C ALA A 271 3.826 15.008 1.608 1.00 2.43 C
ATOM 371 O ALA A 271 3.379 14.962 0.461 1.00 2.85 O
ATOM 372 CB ALA A 271 4.067 12.704 2.428 1.00 2.94 C
ATOM 373 N VAL A 272 4.716 15.934 1.950 1.00 2.87 N
ATOM 374 CA VAL A 272 5.208 16.888 0.968 1.00 3.03 C
ATOM 375 C VAL A 272 6.720 16.792 0.849 1.00 4.24 C
ATOM 376 O VAL A 272 7.436 16.984 1.830 1.00 6.69 O
ATOM 377 CB VAL A 272 4.828 18.325 1.375 1.00 2.00 C
ATOM 378 CG1 VAL A 272 5.382 19.324 0.363 1.00 2.85 C
ATOM 379 CG2 VAL A 272 3.314 18.436 1.457 1.00 3.94 C
ATOM 380 N LYS A 273 7.243 16.464 -0.331 1.00 5.31 N
ATOM 381 CA LYS A 273 8.684 16.437 -0.503 1.00 5.86 C
ATOM 382 C LYS A 273 9.088 17.689 -1.264 1.00 6.31 C
ATOM 383 O LYS A 273 8.569 17.983 -2.340 1.00 5.50 O
ATOM 384 CB LYS A 273 9.115 15.189 -1.286 1.00 7.60 C
ATOM 385 CG LYS A 273 10.627 15.168 -1.467 1.00 8.60 C
ATOM 386 CD LYS A 273 11.152 13.805 -1.903 1.00 12.93 C
ATOM 387 CE LYS A 273 10.638 13.380 -3.272 1.00 14.96 C
ATOM 388 NZ LYS A 273 11.286 12.145 -3.690 1.00 16.62 N
ATOM 389 N ASER A 274 10.017 18.465 -0.714 0.65 6.04 N
ATOM 390 N BSER A 274 10.013 18.470 -0.714 0.35 6.57 N
ATOM 391 CA ASER A 274 10.427 19.691 -1.370 0.65 6.89 C
ATOM 392 CA BSER A 274 10.416 19.696 -1.376 0.35 7.51 C
ATOM 393 C ASER A 274 11.835 19.589 -1.925 0.65 8.38 C
ATOM 394 C BSER A 274 11.835 19.612 -1.913 0.35 8.41 C
ATOM 395 O ASER A 274 12.719 18.975 -1.332 0.65 9.88 O
ATOM 396 O BSER A 274 12.727 19.029 -1.298 0.35 9.18 O
ATOM 397 CB ASER A 274 10.377 20.849 -0.389 0.65 7.66 C
ATOM 398 CB BSER A 274 10.311 20.855 -0.396 0.35 8.18 C
ATOM 399 OG ASER A 274 11.302 20.628 0.667 0.65 7.49 O
ATOM 400 OG BSER A 274 10.666 22.089 -1.004 0.35 8.80 O
ATOM 401 N LEU A 275 12.064 20.197 -3.084 1.00 9.21 N
ATOM 402 CA LEU A 275 13.389 20.171 -3.674 1.00 8.78 C
ATOM 403 C LEU A 275 14.233 21.344 -3.213 1.00 9.69 C
ATOM 404 O LEU A 275 13.839 22.509 -3.307 1.00 9.96 O
ATOM 405 CB LEU A 275 13.289 20.209 -5.192 1.00 8.45 C
ATOM 406 CG LEU A 275 14.575 20.453 -5.984 1.00 8.36 C
ATOM 407 CD1 LEU A 275 15.591 19.358 -5.706 1.00 6.66 C
ATOM 408 CD2 LEU A 275 14.242 20.488 -7.467 1.00 8.64 C
ATOM 409 N LYS A 276 15.414 21.040 -2.687 1.00 9.79 N
ATOM 410 CA LYS A 276 16.328 22.095 -2.302 1.00 12.83 C
ATOM 411 C LYS A 276 16.888 22.719 -3.576 1.00 13.85 C
ATOM 412 O LYS A 276 17.617 22.069 -4.325 1.00 12.82 O
ATOM 413 CB LYS A 276 17.435 21.488 -1.453 1.00 13.89 C
ATOM 414 CG LYS A 276 18.471 22.511 -1.035 1.00 16.60 C
ATOM 415 CD LYS A 276 19.440 21.878 -0.058 1.00 18.42 C
ATOM 416 CE LYS A 276 20.500 22.909 0.298 1.00 23.13 C
ATOM 417 NZ LYS A 276 21.386 22.403 1.329 1.00 24.89 N
ATOM 418 N AGLN A 277 16.560 23.981 -3.867 0.64 14.48 N
ATOM 419 N BGLN A 277 16.570 23.984 -3.854 0.36 14.50 N
ATOM 420 CA AGLN A 277 17.048 24.576 -5.100 0.64 16.20 C
ATOM 421 CA BGLN A 277 17.055 24.625 -5.067 0.36 16.00 C
ATOM 422 C AGLN A 277 18.552 24.459 -5.261 0.64 15.73 C
ATOM 423 C BGLN A 277 18.556 24.454 -5.258 0.36 15.68 C
ATOM 424 O AGLN A 277 19.326 24.758 -4.352 0.64 16.49 O
ATOM 425 O BGLN A 277 19.348 24.713 -4.352 0.36 15.98 O
ATOM 426 CB AGLN A 277 16.698 26.057 -5.193 0.64 16.38 C
ATOM 427 CB BGLN A 277 16.738 26.113 -5.025 0.36 16.70 C
ATOM 428 CG AGLN A 277 15.213 26.340 -5.372 0.64 17.91 C
ATOM 429 CG BGLN A 277 17.184 26.898 -6.251 0.36 18.31 C
ATOM 430 CD AGLN A 277 14.466 26.659 -4.081 0.64 19.24 C
ATOM 431 CD BGLN A 277 16.182 26.894 -7.394 0.36 20.04 C
ATOM 432 OE1AGLN A 277 14.604 25.955 -3.069 0.64 20.13 O
ATOM 433 OE1BGLN A 277 16.492 27.316 -8.507 0.36 21.52 O
ATOM 434 NE2AGLN A 277 13.672 27.724 -4.083 0.64 17.90 N
ATOM 435 NE2BGLN A 277 14.951 26.447 -7.161 0.36 20.81 N
ATOM 436 N GLY A 278 18.985 24.018 -6.441 1.00 15.58 N
ATOM 437 CA GLY A 278 20.407 23.876 -6.707 1.00 14.69 C
ATOM 438 C GLY A 278 21.009 22.539 -6.298 1.00 14.49 C
ATOM 439 O GLY A 278 22.112 22.206 -6.731 1.00 15.24 O
ATOM 440 N SER A 279 20.341 21.719 -5.486 1.00 12.97 N
ATOM 441 CA SER A 279 20.941 20.465 -5.061 1.00 12.68 C
ATOM 442 C SER A 279 20.917 19.395 -6.136 1.00 12.50 C
ATOM 443 O SER A 279 21.704 18.451 -6.123 1.00 14.17 O
ATOM 444 CB SER A 279 20.218 19.925 -3.834 1.00 13.71 C
ATOM 445 OG SER A 279 18.879 19.570 -4.150 1.00 13.61 O
ATOM 446 N MET A 280 19.985 19.514 -7.076 1.00 11.08 N
ATOM 447 CA MET A 280 19.886 18.552 -8.151 1.00 9.58 C
ATOM 448 C MET A 280 18.962 19.120 -9.215 1.00 9.47 C
ATOM 449 O MET A 280 18.274 20.117 -9.001 1.00 8.53 O
ATOM 450 CB MET A 280 19.318 17.236 -7.645 1.00 9.80 C
ATOM 451 CG MET A 280 17.891 17.369 -7.137 1.00 9.72 C
ATOM 452 SD MET A 280 17.186 15.781 -6.629 1.00 12.16 S
ATOM 453 CE MET A 280 16.672 15.156 -8.203 1.00 10.82 C
ATOM 454 N SER A 281 18.930 18.511 -10.394 1.00 8.61 N
ATOM 455 CA SER A 281 18.070 19.019 -11.444 1.00 7.74 C
ATOM 456 C SER A 281 16.592 18.991 -11.101 1.00 7.40 C
ATOM 457 O SER A 281 16.060 17.974 -10.658 1.00 7.33 O
ATOM 458 CB SER A 281 18.272 18.215 -12.712 1.00 8.61 C
ATOM 459 OG SER A 281 17.273 18.559 -13.656 1.00 7.95 O
ATOM 460 N APRO A 282 15.882 20.095 -11.306 0.51 7.01 N
ATOM 461 N BPRO A 282 15.884 20.099 -11.304 0.49 7.60 N
ATOM 462 CA APRO A 282 14.439 20.152 -11.158 0.51 6.47 C
ATOM 463 CA BPRO A 282 14.438 20.165 -11.179 0.49 7.14 C
ATOM 464 C APRO A 282 13.760 19.188 -12.124 0.51 5.97 C
ATOM 465 C BPRO A 282 13.769 19.172 -12.117 0.49 6.42 C
ATOM 466 O APRO A 282 12.694 18.643 -11.839 0.51 4.49 O
ATOM 467 O BPRO A 282 12.727 18.595 -11.809 0.49 5.00 O
ATOM 468 CB APRO A 282 14.127 21.612 -11.397 0.51 6.83 C
ATOM 469 CB BPRO A 282 14.119 21.610 -11.492 0.49 7.73 C
ATOM 470 CG APRO A 282 15.210 22.032 -12.364 0.51 5.48 C
ATOM 471 CG BPRO A 282 15.379 22.331 -11.078 0.49 7.85 C
ATOM 472 CD APRO A 282 16.437 21.356 -11.771 0.51 6.85 C
ATOM 473 CD BPRO A 282 16.456 21.398 -11.615 0.49 8.05 C
ATOM 474 N ASP A 283 14.365 18.952 -13.290 1.00 6.18 N
ATOM 475 CA ASP A 283 13.804 17.999 -14.232 1.00 6.15 C
ATOM 476 C ASP A 283 13.933 16.595 -13.658 1.00 5.75 C
ATOM 477 O ASP A 283 13.022 15.769 -13.724 1.00 5.35 O
ATOM 478 CB ASP A 283 14.549 18.068 -15.562 1.00 8.36 C
ATOM 479 CG ASP A 283 13.973 17.116 -16.597 1.00 9.33 C
ATOM 480 OD1 ASP A 283 12.804 17.272 -16.946 1.00 14.99 O
ATOM 481 OD2 ASP A 283 14.685 16.221 -17.051 1.00 8.45 O
ATOM 482 N ALA A 284 15.090 16.296 -13.079 1.00 6.42 N
ATOM 483 CA ALA A 284 15.292 14.992 -12.476 1.00 7.51 C
ATOM 484 C ALA A 284 14.341 14.769 -11.304 1.00 7.89 C
ATOM 485 O ALA A 284 13.788 13.688 -11.092 1.00 8.38 O
ATOM 486 CB ALA A 284 16.720 14.878 -11.971 1.00 9.31 C
ATOM 487 N PHE A 285 14.148 15.819 -10.510 1.00 7.54 N
ATOM 488 CA PHE A 285 13.244 15.734 -9.377 1.00 7.78 C
ATOM 489 C PHE A 285 11.822 15.437 -9.846 1.00 7.53 C
ATOM 490 O PHE A 285 11.170 14.507 -9.376 1.00 7.97 O
ATOM 491 CB PHE A 285 13.289 17.059 -8.610 1.00 5.64 C
ATOM 492 CG PHE A 285 12.436 17.111 -7.348 1.00 4.85 C
ATOM 493 CD1 PHE A 285 12.877 16.492 -6.190 1.00 5.15 C
ATOM 494 CD2 PHE A 285 11.232 17.790 -7.357 1.00 5.02 C
ATOM 495 CE1 PHE A 285 12.109 16.557 -5.042 1.00 4.77 C
ATOM 496 CE2 PHE A 285 10.472 17.849 -6.202 1.00 4.40 C
ATOM 497 CZ PHE A 285 10.909 17.235 -5.048 1.00 3.21 C
ATOM 498 N LEU A 286 11.306 16.202 -10.804 1.00 6.77 N
ATOM 499 CA LEU A 286 9.936 15.995 -11.226 1.00 7.70 C
ATOM 500 C LEU A 286 9.713 14.743 -12.053 1.00 7.50 C
ATOM 501 O LEU A 286 8.588 14.257 -12.151 1.00 6.40 O
ATOM 502 CB LEU A 286 9.466 17.215 -12.012 1.00 8.93 C
ATOM 503 CG LEU A 286 9.278 18.495 -11.205 1.00 9.06 C
ATOM 504 CD1 LEU A 286 8.956 19.655 -12.134 1.00 9.98 C
ATOM 505 CD2 LEU A 286 8.164 18.279 -10.186 1.00 11.68 C
ATOM 506 N ALA A 287 10.758 14.189 -12.668 1.00 6.66 N
ATOM 507 CA ALA A 287 10.582 12.960 -13.420 1.00 6.10 C
ATOM 508 C ALA A 287 9.968 11.866 -12.549 1.00 5.11 C
ATOM 509 O ALA A 287 9.210 11.015 -13.016 1.00 4.21 O
ATOM 510 CB ALA A 287 11.926 12.466 -13.939 1.00 6.43 C
ATOM 511 N GLU A 288 10.269 11.854 -11.252 1.00 4.60 N
ATOM 512 CA GLU A 288 9.668 10.855 -10.387 1.00 5.03 C
ATOM 513 C GLU A 288 8.152 11.027 -10.351 1.00 5.24 C
ATOM 514 O GLU A 288 7.379 10.068 -10.414 1.00 4.05 O
ATOM 515 CB GLU A 288 10.223 10.988 -8.974 1.00 5.36 C
ATOM 516 CG GLU A 288 9.574 9.963 -8.059 1.00 7.76 C
ATOM 517 CD GLU A 288 9.982 10.055 -6.596 1.00 9.72 C
ATOM 518 OE1 GLU A 288 10.546 11.070 -6.191 1.00 10.81 O
ATOM 519 OE2 GLU A 288 9.727 9.099 -5.864 1.00 11.92 O
ATOM 520 N ALA A 289 7.686 12.268 -10.236 1.00 5.01 N
ATOM 521 CA ALA A 289 6.251 12.489 -10.211 1.00 6.51 C
ATOM 522 C ALA A 289 5.623 12.071 -11.538 1.00 5.73 C
ATOM 523 O ALA A 289 4.565 11.442 -11.585 1.00 4.96 O
ATOM 524 CB ALA A 289 5.945 13.969 -9.970 1.00 5.96 C
ATOM 525 N ASN A 290 6.259 12.390 -12.662 1.00 6.92 N
ATOM 526 CA ASN A 290 5.689 11.988 -13.937 1.00 7.62 C
ATOM 527 C ASN A 290 5.554 10.475 -14.041 1.00 7.27 C
ATOM 528 O ASN A 290 4.573 9.943 -14.562 1.00 7.30 O
ATOM 529 CB ASN A 290 6.566 12.508 -15.066 1.00 10.94 C
ATOM 530 CG ASN A 290 6.497 14.024 -15.166 1.00 15.31 C
ATOM 531 OD1 ASN A 290 5.501 14.644 -14.787 1.00 17.01 O
ATOM 532 ND2 ASN A 290 7.547 14.662 -15.677 1.00 16.50 N
ATOM 533 N LEU A 291 6.529 9.734 -13.533 1.00 6.14 N
ATOM 534 CA LEU A 291 6.418 8.292 -13.574 1.00 7.27 C
ATOM 535 C LEU A 291 5.292 7.806 -12.667 1.00 5.89 C
ATOM 536 O LEU A 291 4.570 6.868 -12.994 1.00 6.07 O
ATOM 537 CB LEU A 291 7.752 7.693 -13.150 1.00 7.82 C
ATOM 538 CG LEU A 291 7.861 6.176 -13.071 1.00 10.33 C
ATOM 539 CD1 LEU A 291 9.286 5.756 -13.398 1.00 11.15 C
ATOM 540 CD2 LEU A 291 7.427 5.710 -11.690 1.00 10.28 C
ATOM 541 N MET A 292 5.091 8.426 -11.505 1.00 5.16 N
ATOM 542 CA MET A 292 4.019 7.991 -10.626 1.00 5.11 C
ATOM 543 C MET A 292 2.645 8.191 -11.244 1.00 5.29 C
ATOM 544 O MET A 292 1.691 7.487 -10.912 1.00 6.37 O
ATOM 545 CB MET A 292 4.094 8.752 -9.310 1.00 4.37 C
ATOM 546 CG MET A 292 5.356 8.397 -8.539 1.00 5.64 C
ATOM 547 SD MET A 292 5.540 9.322 -6.994 1.00 6.69 S
ATOM 548 CE MET A 292 4.301 8.520 -6.017 1.00 4.96 C
ATOM 549 N LYS A 293 2.489 9.151 -12.153 1.00 6.15 N
ATOM 550 CA LYS A 293 1.198 9.322 -12.795 1.00 8.49 C
ATOM 551 C LYS A 293 0.818 8.071 -13.577 1.00 9.36 C
ATOM 552 O LYS A 293 -0.359 7.765 -13.761 1.00 11.10 O
ATOM 553 CB LYS A 293 1.243 10.512 -13.745 1.00 8.13 C
ATOM 554 CG LYS A 293 1.527 11.815 -13.026 1.00 10.04 C
ATOM 555 CD LYS A 293 1.652 12.952 -14.028 1.00 10.89 C
ATOM 556 CE LYS A 293 2.012 14.235 -13.285 1.00 13.17 C
ATOM 557 NZ LYS A 293 2.300 15.313 -14.214 1.00 13.78 N
ATOM 558 N GLN A 294 1.826 7.320 -14.028 1.00 11.05 N
ATOM 559 CA GLN A 294 1.611 6.107 -14.812 1.00 11.74 C
ATOM 560 C GLN A 294 1.492 4.837 -13.984 1.00 11.70 C
ATOM 561 O GLN A 294 1.220 3.753 -14.503 1.00 11.34 O
ATOM 562 CB GLN A 294 2.759 5.915 -15.787 1.00 13.03 C
ATOM 563 CG GLN A 294 3.015 7.145 -16.641 1.00 16.78 C
ATOM 564 CD GLN A 294 1.809 7.528 -17.476 1.00 18.74 C
ATOM 565 OE1 GLN A 294 1.044 6.672 -17.919 1.00 23.41 O
ATOM 566 NE2 GLN A 294 1.590 8.817 -17.710 1.00 20.29 N
ATOM 567 N LEU A 295 1.730 4.933 -12.682 1.00 10.59 N
ATOM 568 CA LEU A 295 1.686 3.755 -11.840 1.00 11.20 C
ATOM 569 C LEU A 295 0.758 3.950 -10.658 1.00 10.98 C
ATOM 570 O LEU A 295 1.173 4.062 -9.505 1.00 11.29 O
ATOM 571 CB LEU A 295 3.081 3.432 -11.332 1.00 11.38 C
ATOM 572 CG LEU A 295 4.070 2.867 -12.332 1.00 11.53 C
ATOM 573 CD1 LEU A 295 5.432 2.715 -11.672 1.00 11.26 C
ATOM 574 CD2 LEU A 295 3.551 1.527 -12.844 1.00 10.94 C
ATOM 575 N GLN A 296 -0.534 3.990 -10.955 1.00 9.88 N
ATOM 576 CA GLN A 296 -1.510 4.166 -9.907 1.00 9.42 C
ATOM 577 C GLN A 296 -2.094 2.824 -9.505 1.00 7.71 C
ATOM 578 O GLN A 296 -2.678 2.111 -10.319 1.00 8.46 O
ATOM 579 CB GLN A 296 -2.608 5.088 -10.405 1.00 10.25 C
ATOM 580 CG GLN A 296 -2.062 6.447 -10.804 1.00 11.85 C
ATOM 581 CD GLN A 296 -3.152 7.371 -11.322 1.00 14.81 C
ATOM 582 OE1 GLN A 296 -4.246 7.452 -10.762 1.00 14.77 O
ATOM 583 NE2 GLN A 296 -2.887 8.093 -12.409 1.00 15.28 N
ATOM 584 N HIS A 297 -1.945 2.459 -8.235 1.00 5.49 N
ATOM 585 CA HIS A 297 -2.481 1.198 -7.761 1.00 4.27 C
ATOM 586 C HIS A 297 -2.607 1.282 -6.247 1.00 3.14 C
ATOM 587 O HIS A 297 -1.865 2.032 -5.615 1.00 3.80 O
ATOM 588 CB HIS A 297 -1.530 0.072 -8.165 1.00 3.62 C
ATOM 589 CG HIS A 297 -2.027 -1.314 -7.786 1.00 3.49 C
ATOM 590 ND1 HIS A 297 -1.960 -1.901 -6.595 1.00 3.44 N