HEADER HYDROLASE/TRANSFERASE 26-SEP-05 2B4S
TITLE CRYSTAL STRUCTURE OF A COMPLEX BETWEEN PTP1B AND THE INSULIN RECEPTOR
TITLE 2 TYROSINE KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE, NON-RECEPTOR TYPE 1;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE 1B, PTP-1B;
COMPND 5 EC: 3.1.3.48;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: INSULIN RECEPTOR;
COMPND 9 CHAIN: B, D;
COMPND 10 FRAGMENT: PROTEIN KINASE;
COMPND 11 SYNONYM: IR, CD220 ANTIGEN;
COMPND 12 EC: 2.7.1.112;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PTPN1, PTP1B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET19B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: INSR;
SOURCE 16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 17 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 19 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS HYDROLASE/TRANSFERASE, PHOSPHORYLATION, TYROSINE PROTEIN KINASE,
KEYWDS 2 HYDROLASE-TRANSFERASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LI,R.S.DEPETRIS,D.BARFORD,J.CHERNOFF,S.R.HUBBARD
REVDAT 5 15-NOV-23 2B4S 1 REMARK
REVDAT 4 23-AUG-23 2B4S 1 REMARK
REVDAT 3 20-OCT-21 2B4S 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2B4S 1 VERSN
REVDAT 1 15-NOV-05 2B4S 0
JRNL AUTH S.LI,R.S.DEPETRIS,D.BARFORD,J.CHERNOFF,S.R.HUBBARD
JRNL TITL CRYSTAL STRUCTURE OF A COMPLEX BETWEEN PROTEIN TYROSINE
JRNL TITL 2 PHOSPHATASE 1B AND THE INSULIN RECEPTOR TYROSINE KINASE.
JRNL REF STRUCTURE V. 13 1643 2005
JRNL REFN ISSN 0969-2126
JRNL PMID 16271887
JRNL DOI 10.1016/J.STR.2005.07.019
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 175542.240
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.3
REMARK 3 NUMBER OF REFLECTIONS : 58237
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) : 0.208
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2946
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8206
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE : 0.2900
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 497
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9214
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 377
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.27000
REMARK 3 B22 (A**2) : 0.28000
REMARK 3 B33 (A**2) : -4.55000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.24
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) : 0.31
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.30
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.740
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) : 0.830 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.430 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.310 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.050 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 28.27
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : PARAMCSDX.MISC
REMARK 3 PARAMETER FILE 5 : DNA-RNA.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2B4S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1000034674.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-APR-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.100
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60480
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.27200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 1IR3, 1G1H
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL, 1.9 M AMMONIUM
REMARK 280 SULFATE, 2% PEG 400, PH 7.5, TEMPERATURE 277K, VAPOR DIFFUSION,
REMARK 280 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 43.73600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 89.02000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.08250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 89.02000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.73600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.08250
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLU A 115
REMARK 465 LYS A 116
REMARK 465 GLU A 293
REMARK 465 LEU A 294
REMARK 465 SER A 295
REMARK 465 HIS A 296
REMARK 465 GLU A 297
REMARK 465 ASP A 298
REMARK 465 VAL B 978
REMARK 465 PHE B 979
REMARK 465 PRO B 980
REMARK 465 SER B 981
REMARK 465 SER B 982
REMARK 465 VAL B 983
REMARK 465 TYR B 984
REMARK 465 VAL B 985
REMARK 465 PRO B 986
REMARK 465 MET C 1
REMARK 465 GLU C 115
REMARK 465 LYS C 116
REMARK 465 GLY C 117
REMARK 465 GLY C 283
REMARK 465 ASP C 284
REMARK 465 SER C 285
REMARK 465 SER C 286
REMARK 465 VAL C 287
REMARK 465 GLN C 288
REMARK 465 ASP C 289
REMARK 465 GLN C 290
REMARK 465 TRP C 291
REMARK 465 LYS C 292
REMARK 465 GLU C 293
REMARK 465 LEU C 294
REMARK 465 SER C 295
REMARK 465 HIS C 296
REMARK 465 GLU C 297
REMARK 465 ASP C 298
REMARK 465 VAL D 978
REMARK 465 PHE D 979
REMARK 465 PRO D 980
REMARK 465 SER D 981
REMARK 465 SER D 982
REMARK 465 VAL D 983
REMARK 465 TYR D 984
REMARK 465 VAL D 985
REMARK 465 PRO D 986
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 2 CG CD OE1 OE2
REMARK 470 GLN A 9 CG CD OE1 NE2
REMARK 470 ARG A 33 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 41 CG CD CE NZ
REMARK 470 GLU A 62 CG CD OE1 OE2
REMARK 470 GLU A 75 CG CD OE1 OE2
REMARK 470 MET A 114 CG SD CE
REMARK 470 GLU A 186 CG CD OE1 OE2
REMARK 470 LYS A 239 CG CD CE NZ
REMARK 470 LYS A 279 CG CD CE NZ
REMARK 470 MET A 282 CG SD CE
REMARK 470 ASP A 284 CG OD1 OD2
REMARK 470 LYS A 292 CG CD CE NZ
REMARK 470 GLU B 988 CG CD OE1 OE2
REMARK 470 GLU B 994 CG CD OE1 OE2
REMARK 470 ARG B1000 CG CD NE CZ NH1 NH2
REMARK 470 GLU B1034 CG CD OE1 OE2
REMARK 470 ARG B1039 CG CD NE CZ NH1 NH2
REMARK 470 GLU B1096 CG CD OE1 OE2
REMARK 470 LYS B1165 CG CD CE NZ
REMARK 470 LYS B1168 CG CD CE NZ
REMARK 470 GLN B1211 CG CD OE1 NE2
REMARK 470 ARG B1243 CG CD NE CZ NH1 NH2
REMARK 470 GLU B1280 CG CD OE1 OE2
REMARK 470 LYS B1283 CG CD CE NZ
REMARK 470 LYS C 41 CG CD CE NZ
REMARK 470 GLU C 62 CG CD OE1 OE2
REMARK 470 ASP C 63 CG OD1 OD2
REMARK 470 GLU C 75 CG CD OE1 OE2
REMARK 470 MET C 114 CG SD CE
REMARK 470 GLU C 186 CG CD OE1 OE2
REMARK 470 LYS C 239 CG CD CE NZ
REMARK 470 MET C 282 CG SD CE
REMARK 470 GLU D 988 CG CD OE1 OE2
REMARK 470 GLU D1034 CG CD OE1 OE2
REMARK 470 GLU D1096 CG CD OE1 OE2
REMARK 470 GLN D1107 CG CD OE1 NE2
REMARK 470 LYS D1165 CG CD CE NZ
REMARK 470 LYS D1168 CG CD CE NZ
REMARK 470 GLN D1211 CG CD OE1 NE2
REMARK 470 ARG D1243 CG CD NE CZ NH1 NH2
REMARK 470 GLU D1280 CG CD OE1 OE2
REMARK 470 LYS D1283 CG CD CE NZ
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 ASP A 63 -75.88 -55.83
REMARK 500 CYS A 121 134.51 -172.66
REMARK 500 LYS A 131 77.62 -113.48
REMARK 500 ALA A 215 -109.49 -153.97
REMARK 500 ILE A 219 -39.48 -137.78
REMARK 500 ILE A 261 104.36 77.26
REMARK 500 ASN B1097 39.72 -96.68
REMARK 500 ARG B1131 -18.35 71.70
REMARK 500 ASP C 63 -75.36 -52.23
REMARK 500 LYS C 131 73.31 -119.47
REMARK 500 ALA C 215 -110.03 -146.14
REMARK 500 ILE C 219 -45.48 -136.19
REMARK 500 ILE C 261 109.06 82.17
REMARK 500 ASP D1017 67.78 38.59
REMARK 500 ARG D1131 -17.89 68.78
REMARK 500 ASN D1233 17.21 59.36
REMARK 500
REMARK 500 REMARK: NULL
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 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1284
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1008
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1009
DBREF 2B4S A 1 298 UNP P18031 PTN1_HUMAN 1 298
DBREF 2B4S C 1 298 UNP P18031 PTN1_HUMAN 1 298
DBREF 2B4S B 978 1283 UNP P06213 INSR_HUMAN 1005 1310
DBREF 2B4S D 978 1283 UNP P06213 INSR_HUMAN 1005 1310
SEQADV 2B4S ALA A 215 UNP P18031 CYS 215 ENGINEERED MUTATION
SEQADV 2B4S ALA C 215 UNP P18031 CYS 215 ENGINEERED MUTATION
SEQADV 2B4S SER B 981 UNP P06213 CYS 1008 ENGINEERED MUTATION
SEQADV 2B4S PTR B 1158 UNP P06213 TYR 1185 MODIFIED RESIDUE
SEQADV 2B4S PTR B 1162 UNP P06213 TYR 1189 MODIFIED RESIDUE
SEQADV 2B4S PTR B 1163 UNP P06213 TYR 1190 MODIFIED RESIDUE
SEQADV 2B4S ASN B 1251 UNP P06213 LYS 1278 VARIANT
SEQADV 2B4S SER D 981 UNP P06213 CYS 1008 ENGINEERED MUTATION
SEQADV 2B4S PTR D 1158 UNP P06213 TYR 1185 MODIFIED RESIDUE
SEQADV 2B4S PTR D 1162 UNP P06213 TYR 1189 MODIFIED RESIDUE
SEQADV 2B4S PTR D 1163 UNP P06213 TYR 1190 MODIFIED RESIDUE
SEQADV 2B4S ASN D 1251 UNP P06213 LYS 1278 VARIANT
SEQRES 1 A 298 MET GLU MET GLU LYS GLU PHE GLU GLN ILE ASP LYS SER
SEQRES 2 A 298 GLY SER TRP ALA ALA ILE TYR GLN ASP ILE ARG HIS GLU
SEQRES 3 A 298 ALA SER ASP PHE PRO CYS ARG VAL ALA LYS LEU PRO LYS
SEQRES 4 A 298 ASN LYS ASN ARG ASN ARG TYR ARG ASP VAL SER PRO PHE
SEQRES 5 A 298 ASP HIS SER ARG ILE LYS LEU HIS GLN GLU ASP ASN ASP
SEQRES 6 A 298 TYR ILE ASN ALA SER LEU ILE LYS MET GLU GLU ALA GLN
SEQRES 7 A 298 ARG SER TYR ILE LEU THR GLN GLY PRO LEU PRO ASN THR
SEQRES 8 A 298 CYS GLY HIS PHE TRP GLU MET VAL TRP GLU GLN LYS SER
SEQRES 9 A 298 ARG GLY VAL VAL MET LEU ASN ARG VAL MET GLU LYS GLY
SEQRES 10 A 298 SER LEU LYS CYS ALA GLN TYR TRP PRO GLN LYS GLU GLU
SEQRES 11 A 298 LYS GLU MET ILE PHE GLU ASP THR ASN LEU LYS LEU THR
SEQRES 12 A 298 LEU ILE SER GLU ASP ILE LYS SER TYR TYR THR VAL ARG
SEQRES 13 A 298 GLN LEU GLU LEU GLU ASN LEU THR THR GLN GLU THR ARG
SEQRES 14 A 298 GLU ILE LEU HIS PHE HIS TYR THR THR TRP PRO ASP PHE
SEQRES 15 A 298 GLY VAL PRO GLU SER PRO ALA SER PHE LEU ASN PHE LEU
SEQRES 16 A 298 PHE LYS VAL ARG GLU SER GLY SER LEU SER PRO GLU HIS
SEQRES 17 A 298 GLY PRO VAL VAL VAL HIS ALA SER ALA GLY ILE GLY ARG
SEQRES 18 A 298 SER GLY THR PHE CYS LEU ALA ASP THR CYS LEU LEU LEU
SEQRES 19 A 298 MET ASP LYS ARG LYS ASP PRO SER SER VAL ASP ILE LYS
SEQRES 20 A 298 LYS VAL LEU LEU GLU MET ARG LYS PHE ARG MET GLY LEU
SEQRES 21 A 298 ILE GLN THR ALA ASP GLN LEU ARG PHE SER TYR LEU ALA
SEQRES 22 A 298 VAL ILE GLU GLY ALA LYS PHE ILE MET GLY ASP SER SER
SEQRES 23 A 298 VAL GLN ASP GLN TRP LYS GLU LEU SER HIS GLU ASP
SEQRES 1 B 306 VAL PHE PRO SER SER VAL TYR VAL PRO ASP GLU TRP GLU
SEQRES 2 B 306 VAL SER ARG GLU LYS ILE THR LEU LEU ARG GLU LEU GLY
SEQRES 3 B 306 GLN GLY SER PHE GLY MET VAL TYR GLU GLY ASN ALA ARG
SEQRES 4 B 306 ASP ILE ILE LYS GLY GLU ALA GLU THR ARG VAL ALA VAL
SEQRES 5 B 306 LYS THR VAL ASN GLU SER ALA SER LEU ARG GLU ARG ILE
SEQRES 6 B 306 GLU PHE LEU ASN GLU ALA SER VAL MET LYS GLY PHE THR
SEQRES 7 B 306 CYS HIS HIS VAL VAL ARG LEU LEU GLY VAL VAL SER LYS
SEQRES 8 B 306 GLY GLN PRO THR LEU VAL VAL MET GLU LEU MET ALA HIS
SEQRES 9 B 306 GLY ASP LEU LYS SER TYR LEU ARG SER LEU ARG PRO GLU
SEQRES 10 B 306 ALA GLU ASN ASN PRO GLY ARG PRO PRO PRO THR LEU GLN
SEQRES 11 B 306 GLU MET ILE GLN MET ALA ALA GLU ILE ALA ASP GLY MET
SEQRES 12 B 306 ALA TYR LEU ASN ALA LYS LYS PHE VAL HIS ARG ASP LEU
SEQRES 13 B 306 ALA ALA ARG ASN CYS MET VAL ALA HIS ASP PHE THR VAL
SEQRES 14 B 306 LYS ILE GLY ASP PHE GLY MET THR ARG ASP ILE PTR GLU
SEQRES 15 B 306 THR ASP PTR PTR ARG LYS GLY GLY LYS GLY LEU LEU PRO
SEQRES 16 B 306 VAL ARG TRP MET ALA PRO GLU SER LEU LYS ASP GLY VAL
SEQRES 17 B 306 PHE THR THR SER SER ASP MET TRP SER PHE GLY VAL VAL
SEQRES 18 B 306 LEU TRP GLU ILE THR SER LEU ALA GLU GLN PRO TYR GLN
SEQRES 19 B 306 GLY LEU SER ASN GLU GLN VAL LEU LYS PHE VAL MET ASP
SEQRES 20 B 306 GLY GLY TYR LEU ASP GLN PRO ASP ASN CYS PRO GLU ARG
SEQRES 21 B 306 VAL THR ASP LEU MET ARG MET CYS TRP GLN PHE ASN PRO
SEQRES 22 B 306 ASN MET ARG PRO THR PHE LEU GLU ILE VAL ASN LEU LEU
SEQRES 23 B 306 LYS ASP ASP LEU HIS PRO SER PHE PRO GLU VAL SER PHE
SEQRES 24 B 306 PHE HIS SER GLU GLU ASN LYS
SEQRES 1 C 298 MET GLU MET GLU LYS GLU PHE GLU GLN ILE ASP LYS SER
SEQRES 2 C 298 GLY SER TRP ALA ALA ILE TYR GLN ASP ILE ARG HIS GLU
SEQRES 3 C 298 ALA SER ASP PHE PRO CYS ARG VAL ALA LYS LEU PRO LYS
SEQRES 4 C 298 ASN LYS ASN ARG ASN ARG TYR ARG ASP VAL SER PRO PHE
SEQRES 5 C 298 ASP HIS SER ARG ILE LYS LEU HIS GLN GLU ASP ASN ASP
SEQRES 6 C 298 TYR ILE ASN ALA SER LEU ILE LYS MET GLU GLU ALA GLN
SEQRES 7 C 298 ARG SER TYR ILE LEU THR GLN GLY PRO LEU PRO ASN THR
SEQRES 8 C 298 CYS GLY HIS PHE TRP GLU MET VAL TRP GLU GLN LYS SER
SEQRES 9 C 298 ARG GLY VAL VAL MET LEU ASN ARG VAL MET GLU LYS GLY
SEQRES 10 C 298 SER LEU LYS CYS ALA GLN TYR TRP PRO GLN LYS GLU GLU
SEQRES 11 C 298 LYS GLU MET ILE PHE GLU ASP THR ASN LEU LYS LEU THR
SEQRES 12 C 298 LEU ILE SER GLU ASP ILE LYS SER TYR TYR THR VAL ARG
SEQRES 13 C 298 GLN LEU GLU LEU GLU ASN LEU THR THR GLN GLU THR ARG
SEQRES 14 C 298 GLU ILE LEU HIS PHE HIS TYR THR THR TRP PRO ASP PHE
SEQRES 15 C 298 GLY VAL PRO GLU SER PRO ALA SER PHE LEU ASN PHE LEU
SEQRES 16 C 298 PHE LYS VAL ARG GLU SER GLY SER LEU SER PRO GLU HIS
SEQRES 17 C 298 GLY PRO VAL VAL VAL HIS ALA SER ALA GLY ILE GLY ARG
SEQRES 18 C 298 SER GLY THR PHE CYS LEU ALA ASP THR CYS LEU LEU LEU
SEQRES 19 C 298 MET ASP LYS ARG LYS ASP PRO SER SER VAL ASP ILE LYS
SEQRES 20 C 298 LYS VAL LEU LEU GLU MET ARG LYS PHE ARG MET GLY LEU
SEQRES 21 C 298 ILE GLN THR ALA ASP GLN LEU ARG PHE SER TYR LEU ALA
SEQRES 22 C 298 VAL ILE GLU GLY ALA LYS PHE ILE MET GLY ASP SER SER
SEQRES 23 C 298 VAL GLN ASP GLN TRP LYS GLU LEU SER HIS GLU ASP
SEQRES 1 D 306 VAL PHE PRO SER SER VAL TYR VAL PRO ASP GLU TRP GLU
SEQRES 2 D 306 VAL SER ARG GLU LYS ILE THR LEU LEU ARG GLU LEU GLY
SEQRES 3 D 306 GLN GLY SER PHE GLY MET VAL TYR GLU GLY ASN ALA ARG
SEQRES 4 D 306 ASP ILE ILE LYS GLY GLU ALA GLU THR ARG VAL ALA VAL
SEQRES 5 D 306 LYS THR VAL ASN GLU SER ALA SER LEU ARG GLU ARG ILE
SEQRES 6 D 306 GLU PHE LEU ASN GLU ALA SER VAL MET LYS GLY PHE THR
SEQRES 7 D 306 CYS HIS HIS VAL VAL ARG LEU LEU GLY VAL VAL SER LYS
SEQRES 8 D 306 GLY GLN PRO THR LEU VAL VAL MET GLU LEU MET ALA HIS
SEQRES 9 D 306 GLY ASP LEU LYS SER TYR LEU ARG SER LEU ARG PRO GLU
SEQRES 10 D 306 ALA GLU ASN ASN PRO GLY ARG PRO PRO PRO THR LEU GLN
SEQRES 11 D 306 GLU MET ILE GLN MET ALA ALA GLU ILE ALA ASP GLY MET
SEQRES 12 D 306 ALA TYR LEU ASN ALA LYS LYS PHE VAL HIS ARG ASP LEU
SEQRES 13 D 306 ALA ALA ARG ASN CYS MET VAL ALA HIS ASP PHE THR VAL
SEQRES 14 D 306 LYS ILE GLY ASP PHE GLY MET THR ARG ASP ILE PTR GLU
SEQRES 15 D 306 THR ASP PTR PTR ARG LYS GLY GLY LYS GLY LEU LEU PRO
SEQRES 16 D 306 VAL ARG TRP MET ALA PRO GLU SER LEU LYS ASP GLY VAL
SEQRES 17 D 306 PHE THR THR SER SER ASP MET TRP SER PHE GLY VAL VAL
SEQRES 18 D 306 LEU TRP GLU ILE THR SER LEU ALA GLU GLN PRO TYR GLN
SEQRES 19 D 306 GLY LEU SER ASN GLU GLN VAL LEU LYS PHE VAL MET ASP
SEQRES 20 D 306 GLY GLY TYR LEU ASP GLN PRO ASP ASN CYS PRO GLU ARG
SEQRES 21 D 306 VAL THR ASP LEU MET ARG MET CYS TRP GLN PHE ASN PRO
SEQRES 22 D 306 ASN MET ARG PRO THR PHE LEU GLU ILE VAL ASN LEU LEU
SEQRES 23 D 306 LYS ASP ASP LEU HIS PRO SER PHE PRO GLU VAL SER PHE
SEQRES 24 D 306 PHE HIS SER GLU GLU ASN LYS
MODRES 2B4S PTR B 1158 TYR O-PHOSPHOTYROSINE
MODRES 2B4S PTR B 1162 TYR O-PHOSPHOTYROSINE
MODRES 2B4S PTR B 1163 TYR O-PHOSPHOTYROSINE
MODRES 2B4S PTR D 1158 TYR O-PHOSPHOTYROSINE
MODRES 2B4S PTR D 1162 TYR O-PHOSPHOTYROSINE
MODRES 2B4S PTR D 1163 TYR O-PHOSPHOTYROSINE
HET PTR B1158 16
HET PTR B1162 16
HET PTR B1163 16
HET PTR D1158 16
HET PTR D1162 16
HET PTR D1163 16
HET SO4 A1000 5
HET SO4 A1001 5
HET SO4 A1004 5
HET SO4 A1007 5
HET SO4 A1008 5
HET SO4 B1284 5
HET SO4 C1002 5
HET SO4 C1003 5
HET SO4 C1005 5
HET SO4 C1009 5
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM SO4 SULFATE ION
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 2 PTR 6(C9 H12 N O6 P)
FORMUL 5 SO4 10(O4 S 2-)
FORMUL 15 HOH *377(H2 O)
HELIX 1 1 GLU A 2 GLY A 14 1 13
HELIX 2 2 SER A 15 ALA A 27 1 13
HELIX 3 3 LEU A 37 ASN A 44 5 8
HELIX 4 4 LEU A 88 ASN A 90 5 3
HELIX 5 5 THR A 91 LYS A 103 1 13
HELIX 6 6 SER A 187 GLY A 202 1 16
HELIX 7 7 GLY A 220 LYS A 237 1 18
HELIX 8 8 ASP A 240 VAL A 244 5 5
HELIX 9 9 ASP A 245 ARG A 254 1 10
HELIX 10 10 THR A 263 ALA A 278 1 16
HELIX 11 11 SER A 286 LYS A 292 1 7
HELIX 12 12 SER B 992 GLU B 994 5 3
HELIX 13 13 SER B 1037 LYS B 1052 1 16
HELIX 14 14 ASP B 1083 SER B 1090 1 8
HELIX 15 15 THR B 1105 LYS B 1126 1 22
HELIX 16 16 ALA B 1134 ARG B 1136 5 3
HELIX 17 17 PRO B 1172 MET B 1176 5 5
HELIX 18 18 ALA B 1177 GLY B 1184 1 8
HELIX 19 19 THR B 1187 SER B 1204 1 18
HELIX 20 20 SER B 1214 ASP B 1224 1 11
HELIX 21 21 PRO B 1235 TRP B 1246 1 12
HELIX 22 22 ASN B 1249 ARG B 1253 5 5
HELIX 23 23 THR B 1255 LYS B 1264 1 10
HELIX 24 24 ASP B 1265 LEU B 1267 5 3
HELIX 25 25 SER B 1270 SER B 1275 1 6
HELIX 26 26 GLU C 2 GLY C 14 1 13
HELIX 27 27 SER C 15 ALA C 27 1 13
HELIX 28 28 LEU C 37 ASN C 44 5 8
HELIX 29 29 PHE C 52 HIS C 54 5 3
HELIX 30 30 THR C 91 GLN C 102 1 12
HELIX 31 31 SER C 187 SER C 201 1 15
HELIX 32 32 ILE C 219 LYS C 237 1 19
HELIX 33 33 ASP C 240 VAL C 244 5 5
HELIX 34 34 ASP C 245 ARG C 254 1 10
HELIX 35 35 THR C 263 MET C 282 1 20
HELIX 36 36 SER D 992 GLU D 994 5 3
HELIX 37 37 SER D 1037 LYS D 1052 1 16
HELIX 38 38 ASP D 1083 SER D 1090 1 8
HELIX 39 39 THR D 1105 LYS D 1126 1 22
HELIX 40 40 ALA D 1134 ARG D 1136 5 3
HELIX 41 41 PRO D 1172 MET D 1176 5 5
HELIX 42 42 ALA D 1177 GLY D 1184 1 8
HELIX 43 43 THR D 1187 SER D 1204 1 18
HELIX 44 44 SER D 1214 ASP D 1224 1 11
HELIX 45 45 PRO D 1235 TRP D 1246 1 12
HELIX 46 46 ASN D 1249 ARG D 1253 5 5
HELIX 47 47 THR D 1255 LYS D 1264 1 10
HELIX 48 48 ASP D 1265 LEU D 1267 5 3
HELIX 49 49 SER D 1270 SER D 1275 1 6
SHEET 1 A 8 ALA A 69 MET A 74 0
SHEET 2 A 8 ARG A 79 THR A 84 -1 O TYR A 81 N ILE A 72
SHEET 3 A 8 VAL A 211 HIS A 214 1 O VAL A 213 N ILE A 82
SHEET 4 A 8 GLY A 106 MET A 109 1 N VAL A 108 O VAL A 212
SHEET 5 A 8 THR A 168 TYR A 176 1 O PHE A 174 N MET A 109
SHEET 6 A 8 TYR A 153 ASN A 162 -1 N LEU A 158 O ILE A 171
SHEET 7 A 8 LEU A 140 ILE A 149 -1 N LYS A 141 O GLU A 161
SHEET 8 A 8 MET A 133 PHE A 135 -1 N PHE A 135 O LEU A 140
SHEET 1 B 5 ILE B 996 GLN B1004 0
SHEET 2 B 5 MET B1009 ILE B1019 -1 O GLU B1012 N LEU B 999
SHEET 3 B 5 GLU B1022 LYS B1030 -1 O THR B1025 N ALA B1015
SHEET 4 B 5 LEU B1073 GLU B1077 -1 O MET B1076 N ALA B1028
SHEET 5 B 5 LEU B1062 VAL B1066 -1 N LEU B1063 O VAL B1075
SHEET 1 C 2 PHE B1128 VAL B1129 0
SHEET 2 C 2 ARG B1155 ASP B1156 -1 O ARG B1155 N VAL B1129
SHEET 1 D 2 CYS B1138 VAL B1140 0
SHEET 2 D 2 VAL B1146 ILE B1148 -1 O LYS B1147 N MET B1139
SHEET 1 E 2 PTR B1163 ARG B1164 0
SHEET 2 E 2 VAL B1185 PHE B1186 -1 O PHE B1186 N PTR B1163
SHEET 1 F 9 ARG C 56 LYS C 58 0
SHEET 2 F 9 TYR C 66 MET C 74 -1 O ALA C 69 N ILE C 57
SHEET 3 F 9 ARG C 79 THR C 84 -1 O TYR C 81 N ILE C 72
SHEET 4 F 9 VAL C 211 HIS C 214 1 O VAL C 213 N ILE C 82
SHEET 5 F 9 GLY C 106 MET C 109 1 N VAL C 108 O VAL C 212
SHEET 6 F 9 THR C 168 TYR C 176 1 O PHE C 174 N MET C 109
SHEET 7 F 9 TYR C 153 ASN C 162 -1 N ARG C 156 O HIS C 173
SHEET 8 F 9 LEU C 140 ILE C 149 -1 N SER C 146 O GLN C 157
SHEET 9 F 9 MET C 133 PHE C 135 -1 N MET C 133 O LEU C 142
SHEET 1 G 5 ILE D 996 GLN D1004 0
SHEET 2 G 5 MET D1009 ILE D1019 -1 O VAL D1010 N LEU D1002
SHEET 3 G 5 GLU D1022 LYS D1030 -1 O VAL D1029 N TYR D1011
SHEET 4 G 5 LEU D1073 GLU D1077 -1 O MET D1076 N ALA D1028
SHEET 5 G 5 LEU D1062 VAL D1066 -1 N LEU D1063 O VAL D1075
SHEET 1 H 2 PHE D1128 VAL D1129 0
SHEET 2 H 2 ARG D1155 ASP D1156 -1 O ARG D1155 N VAL D1129
SHEET 1 I 2 CYS D1138 VAL D1140 0
SHEET 2 I 2 VAL D1146 ILE D1148 -1 O LYS D1147 N MET D1139
SHEET 1 J 2 PTR D1163 ARG D1164 0
SHEET 2 J 2 VAL D1185 PHE D1186 -1 O PHE D1186 N PTR D1163
LINK C ILE B1157 N PTR B1158 1555 1555 1.33
LINK C PTR B1158 N GLU B1159 1555 1555 1.33
LINK C ASP B1161 N PTR B1162 1555 1555 1.33
LINK C PTR B1162 N PTR B1163 1555 1555 1.32
LINK C PTR B1163 N ARG B1164 1555 1555 1.33
LINK C ILE D1157 N PTR D1158 1555 1555 1.33
LINK C PTR D1158 N GLU D1159 1555 1555 1.33
LINK C ASP D1161 N PTR D1162 1555 1555 1.33
LINK C PTR D1162 N PTR D1163 1555 1555 1.33
LINK C PTR D1163 N ARG D1164 1555 1555 1.33
CISPEP 1 GLN B 1070 PRO B 1071 0 -0.30
CISPEP 2 GLN D 1070 PRO D 1071 0 -0.16
SITE 1 AC1 10 ALA A 215 SER A 216 ALA A 217 GLY A 218
SITE 2 AC1 10 ILE A 219 GLY A 220 ARG A 221 SER A 222
SITE 3 AC1 10 HOH A1016 HOH A1042
SITE 1 AC2 5 TYR A 20 ARG A 24 ARG A 254 GLY A 259
SITE 2 AC2 5 HOH A1015
SITE 1 AC3 10 ALA C 215 SER C 216 ALA C 217 GLY C 218
SITE 2 AC3 10 ILE C 219 GLY C 220 ARG C 221 SER C 222
SITE 3 AC3 10 HOH C1030 HOH C1058
SITE 1 AC4 5 TYR C 20 ARG C 24 ARG C 254 GLY C 259
SITE 2 AC4 5 HOH C1037
SITE 1 AC5 9 ASN A 111 ARG A 112 LEU A 119 LYS A 120
SITE 2 AC5 9 ASP A 181 SER A 216 ARG A 221 HOH A1094
SITE 3 AC5 9 HOH B 208
SITE 1 AC6 10 ASN C 111 ARG C 112 LEU C 119 LYS C 120
SITE 2 AC6 10 ASP C 181 SER C 216 ARG C 221 HOH C1061
SITE 3 AC6 10 HOH D 231 GLU D1273
SITE 1 AC7 6 PRO B1235 GLU B1236 HOH D 211 PRO D1235
SITE 2 AC7 6 GLU D1236 ARG D1237
SITE 1 AC8 3 ASN A 42 ARG A 43 ASN A 90
SITE 1 AC9 3 ARG A 45 CYS A 121 ALA A 122
SITE 1 BC1 6 ASN B1249 ASN B1251 ARG C 45 PRO C 89
SITE 2 BC1 6 CYS C 121 ALA C 122
CRYST1 87.472 88.165 178.040 90.00 90.00 90.00 P 21 21 21 8
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 0.011432 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011342 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005617 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
