HEADER TRANSFERASE 07-AUG-01 1JQH
TITLE IGF-1 RECEPTOR KINASE DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IGF-1 RECEPTOR KINASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: KINASE DOMAIN;
COMPND 5 EC: 2.7.1.112;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS PROTEIN KINASE FOLD, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.PAUTSCH,A.ZOEPHEL,H.AHORN,W.SPEVAK,R.HAUPTMANN,H.NAR
REVDAT 5 10-NOV-21 1JQH 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 1JQH 1 VERSN
REVDAT 3 01-APR-03 1JQH 1 JRNL
REVDAT 2 18-DEC-02 1JQH 1 REMARK
REVDAT 1 19-APR-02 1JQH 0
JRNL AUTH A.PAUTSCH,A.ZOEPHEL,H.AHORN,W.SPEVAK,R.HAUPTMANN,H.NAR
JRNL TITL CRYSTAL STRUCTURE OF BISPHOSPHORYLATED IGF-1 RECEPTOR
JRNL TITL 2 KINASE: INSIGHT INTO DOMAIN MOVEMENTS UPON KINASE
JRNL TITL 3 ACTIVATION.
JRNL REF STRUCTURE V. 9 955 2001
JRNL REFN ISSN 0969-2126
JRNL PMID 11591350
JRNL DOI 10.1016/S0969-2126(01)00655-4
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2000
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2019848.880
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 60343
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 + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 3121
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 63464
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.20
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 9864
REMARK 3 BIN R VALUE (WORKING SET) : 0.3172
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 379
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 : 6931
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 109
REMARK 3 SOLVENT ATOMS : 252
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.90000
REMARK 3 B22 (A**2) : -5.90000
REMARK 3 B33 (A**2) : 11.80000
REMARK 3 B12 (A**2) : -0.15000
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) : 0.38
REMARK 3 ESD FROM SIGMAA (A) : 0.47
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) : 0.39
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.45
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.040
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) : 2.390 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.530 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.390 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.780 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ANP_XPLO2D.PARAM
REMARK 3 PARAMETER FILE 5 : 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
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 CRYSTALS WERE TWINNED. REFINEMENT WAS AGAINST TWINNED DATA
REMARK 3 WITH A RESIDUAL THAT ACCOUNTS FOR TWINNING.
REMARK 4
REMARK 4 1JQH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-AUG-01.
REMARK 100 THE DEPOSITION ID IS D_1000014069.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAR-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MPG/DESY, HAMBURG
REMARK 200 BEAMLINE : BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.050
REMARK 200 MONOCHROMATOR : SI-111 CRYSTALS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
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 : 63650
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : 0.04700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.9000
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) : 2.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.44000
REMARK 200 R SYM FOR SHELL (I) : 0.44000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MAGNESIUM CHLORIDE, TRIS, AMMONIUM
REMARK 280 SULPHATE, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
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
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 88.13600
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 44.06800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 GLY A 979
REMARK 465 SER A 980
REMARK 465 PHE A 981
REMARK 465 SER A 982
REMARK 465 ALA A 983
REMARK 465 MET A 1098
REMARK 465 GLU A 1099
REMARK 465 ASN A 1100
REMARK 465 ASN A 1101
REMARK 465 PRO A 1102
REMARK 465 ARG A 1158
REMARK 465 ASP A 1159
REMARK 465 ILE A 1160
REMARK 465 TYR A 1161
REMARK 465 GLU A 1162
REMARK 465 THR A 1163
REMARK 465 ASP A 1164
REMARK 465 GLY B 979
REMARK 465 SER B 980
REMARK 465 PHE B 981
REMARK 465 SER B 982
REMARK 465 ALA B 983
REMARK 465 GLU B 1097
REMARK 465 MET B 1098
REMARK 465 GLU B 1099
REMARK 465 ASN B 1100
REMARK 465 ASN B 1101
REMARK 465 PRO B 1102
REMARK 465 VAL B 1103
REMARK 465 LEU B 1104
REMARK 465 ALA B 1105
REMARK 465 ARG B 1158
REMARK 465 ASP B 1159
REMARK 465 ILE B 1160
REMARK 465 TYR B 1161
REMARK 465 GLU B 1162
REMARK 465 THR B 1163
REMARK 465 ASP B 1164
REMARK 465 GLY C 979
REMARK 465 SER C 980
REMARK 465 PHE C 981
REMARK 465 SER C 982
REMARK 465 ALA C 983
REMARK 465 MET C 1098
REMARK 465 GLU C 1099
REMARK 465 ASN C 1100
REMARK 465 ASN C 1101
REMARK 465 PRO C 1102
REMARK 465 ARG C 1158
REMARK 465 ASP C 1159
REMARK 465 ILE C 1160
REMARK 465 TYR C 1161
REMARK 465 GLU C 1162
REMARK 465 THR C 1163
REMARK 465 ASP C 1164
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 C GLN C 1073 CD PRO C 1074 1.72
REMARK 500 C GLN A 1073 CD PRO A 1074 1.74
REMARK 500 C GLN B 1073 CD PRO B 1074 1.75
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 PRO A1074 C - N - CA ANGL. DEV. = 45.3 DEGREES
REMARK 500 PRO A1074 C - N - CD ANGL. DEV. = -52.9 DEGREES
REMARK 500 PRO A1074 CA - N - CD ANGL. DEV. = -11.8 DEGREES
REMARK 500 PRO A1107 C - N - CA ANGL. DEV. = -19.7 DEGREES
REMARK 500 PRO B1074 C - N - CA ANGL. DEV. = 42.7 DEGREES
REMARK 500 PRO B1074 C - N - CD ANGL. DEV. = -51.9 DEGREES
REMARK 500 PRO B1074 CA - N - CD ANGL. DEV. = -11.8 DEGREES
REMARK 500 PRO B1107 C - N - CA ANGL. DEV. = 11.4 DEGREES
REMARK 500 PRO C1074 C - N - CA ANGL. DEV. = 43.9 DEGREES
REMARK 500 PRO C1074 C - N - CD ANGL. DEV. = -52.5 DEGREES
REMARK 500 PRO C1074 CA - N - CD ANGL. DEV. = -10.2 DEGREES
REMARK 500 PRO C1107 C - N - CA ANGL. DEV. = -18.1 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 GLU A 991 -8.25 -59.65
REMARK 500 PRO A1074 80.69 103.99
REMARK 500 ARG A1095 127.31 -38.41
REMARK 500 PRO A1106 -175.62 -64.01
REMARK 500 ASN A1129 32.80 -93.03
REMARK 500 ARG A1134 -3.78 74.77
REMARK 500 ASP A1135 44.97 -148.32
REMARK 500 GLU B 991 -7.43 -59.56
REMARK 500 PRO B1074 78.51 99.10
REMARK 500 PRO B1107 153.69 -18.03
REMARK 500 ASN B1129 32.27 -92.05
REMARK 500 ARG B1134 -2.97 74.32
REMARK 500 ASP B1135 45.09 -148.33
REMARK 500 ARG B1177 -7.46 -59.25
REMARK 500 ALA B1209 60.44 61.39
REMARK 500 ASP C 985 77.17 -177.97
REMARK 500 PRO C1074 77.05 99.43
REMARK 500 PRO C1096 54.15 -48.96
REMARK 500 ASN C1129 32.51 -92.84
REMARK 500 ARG C1134 -2.63 74.59
REMARK 500 ASP C1135 44.98 -149.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG C1223 0.14 SIDE CHAIN
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 MG A 304 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 250 O
REMARK 620 2 HOH A 251 O 167.4
REMARK 620 3 ANP A 301 O2G 120.9 71.1
REMARK 620 4 ANP A 301 O1A 72.4 111.6 97.7
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 MG A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP C 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IRK RELATED DB: PDB
REMARK 900 1IRK CONTAINS INSULIN RECEPTOR (TYROSINE KINASE DOMAIN)
REMARK 900 RELATED ID: 1IR3 RELATED DB: PDB
REMARK 900 1IR3 CONTAINS PHOSPHORYLATED INSULIN RECEPTOR TYROSINE KINASE
REMARK 900 COMPLEXED WITH PEPTIDE SUBSTRATE AND ATP ANALOG
DBREF 1JQH A 979 1286 UNP P08069 IGF1R_HUMAN 979 1286
DBREF 1JQH B 979 1286 UNP P08069 IGF1R_HUMAN 979 1286
DBREF 1JQH C 979 1286 UNP P08069 IGF1R_HUMAN 979 1286
SEQADV 1JQH GLY A 979 UNP P08069 GLU 979 ENGINEERED MUTATION
SEQADV 1JQH SER A 980 UNP P08069 TYR 980 ENGINEERED MUTATION
SEQADV 1JQH GLY B 979 UNP P08069 GLU 979 ENGINEERED MUTATION
SEQADV 1JQH SER B 980 UNP P08069 TYR 980 ENGINEERED MUTATION
SEQADV 1JQH GLY C 979 UNP P08069 GLU 979 ENGINEERED MUTATION
SEQADV 1JQH SER C 980 UNP P08069 TYR 980 ENGINEERED MUTATION
SEQRES 1 A 308 GLY SER PHE SER ALA ALA ASP VAL TYR VAL PRO ASP GLU
SEQRES 2 A 308 TRP GLU VAL ALA ARG GLU LYS ILE THR MET SER ARG GLU
SEQRES 3 A 308 LEU GLY GLN GLY SER PHE GLY MET VAL TYR GLU GLY VAL
SEQRES 4 A 308 ALA LYS GLY VAL VAL LYS ASP GLU PRO GLU THR ARG VAL
SEQRES 5 A 308 ALA ILE LYS THR VAL ASN GLU ALA ALA SER MET ARG GLU
SEQRES 6 A 308 ARG ILE GLU PHE LEU ASN GLU ALA SER VAL MET LYS GLU
SEQRES 7 A 308 PHE ASN CYS HIS HIS VAL VAL ARG LEU LEU GLY VAL VAL
SEQRES 8 A 308 SER GLN GLY GLN PRO THR LEU VAL ILE MET GLU LEU MET
SEQRES 9 A 308 THR ARG GLY ASP LEU LYS SER TYR LEU ARG SER LEU ARG
SEQRES 10 A 308 PRO GLU MET GLU ASN ASN PRO VAL LEU ALA PRO PRO SER
SEQRES 11 A 308 LEU SER LYS MET ILE GLN MET ALA GLY GLU ILE ALA ASP
SEQRES 12 A 308 GLY MET ALA TYR LEU ASN ALA ASN LYS PHE VAL HIS ARG
SEQRES 13 A 308 ASP LEU ALA ALA ARG ASN CYS MET VAL ALA GLU ASP PHE
SEQRES 14 A 308 THR VAL LYS ILE GLY ASP PHE GLY MET THR ARG ASP ILE
SEQRES 15 A 308 TYR GLU THR ASP TYR TYR ARG LYS GLY GLY LYS GLY LEU
SEQRES 16 A 308 LEU PRO VAL ARG TRP MET SER PRO GLU SER LEU LYS ASP
SEQRES 17 A 308 GLY VAL PHE THR THR TYR SER ASP VAL TRP SER PHE GLY
SEQRES 18 A 308 VAL VAL LEU TRP GLU ILE ALA THR LEU ALA GLU GLN PRO
SEQRES 19 A 308 TYR GLN GLY LEU SER ASN GLU GLN VAL LEU ARG PHE VAL
SEQRES 20 A 308 MET GLU GLY GLY LEU LEU ASP LYS PRO ASP ASN CYS PRO
SEQRES 21 A 308 ASP MET LEU PHE GLU LEU MET ARG MET CYS TRP GLN TYR
SEQRES 22 A 308 ASN PRO LYS MET ARG PRO SER PHE LEU GLU ILE ILE SER
SEQRES 23 A 308 SER ILE LYS GLU GLU MET GLU PRO GLY PHE ARG GLU VAL
SEQRES 24 A 308 SER PHE TYR TYR SER GLU GLU ASN LYS
SEQRES 1 B 308 GLY SER PHE SER ALA ALA ASP VAL TYR VAL PRO ASP GLU
SEQRES 2 B 308 TRP GLU VAL ALA ARG GLU LYS ILE THR MET SER ARG GLU
SEQRES 3 B 308 LEU GLY GLN GLY SER PHE GLY MET VAL TYR GLU GLY VAL
SEQRES 4 B 308 ALA LYS GLY VAL VAL LYS ASP GLU PRO GLU THR ARG VAL
SEQRES 5 B 308 ALA ILE LYS THR VAL ASN GLU ALA ALA SER MET ARG GLU
SEQRES 6 B 308 ARG ILE GLU PHE LEU ASN GLU ALA SER VAL MET LYS GLU
SEQRES 7 B 308 PHE ASN CYS HIS HIS VAL VAL ARG LEU LEU GLY VAL VAL
SEQRES 8 B 308 SER GLN GLY GLN PRO THR LEU VAL ILE MET GLU LEU MET
SEQRES 9 B 308 THR ARG GLY ASP LEU LYS SER TYR LEU ARG SER LEU ARG
SEQRES 10 B 308 PRO GLU MET GLU ASN ASN PRO VAL LEU ALA PRO PRO SER
SEQRES 11 B 308 LEU SER LYS MET ILE GLN MET ALA GLY GLU ILE ALA ASP
SEQRES 12 B 308 GLY MET ALA TYR LEU ASN ALA ASN LYS PHE VAL HIS ARG
SEQRES 13 B 308 ASP LEU ALA ALA ARG ASN CYS MET VAL ALA GLU ASP PHE
SEQRES 14 B 308 THR VAL LYS ILE GLY ASP PHE GLY MET THR ARG ASP ILE
SEQRES 15 B 308 TYR GLU THR ASP TYR TYR ARG LYS GLY GLY LYS GLY LEU
SEQRES 16 B 308 LEU PRO VAL ARG TRP MET SER PRO GLU SER LEU LYS ASP
SEQRES 17 B 308 GLY VAL PHE THR THR TYR SER ASP VAL TRP SER PHE GLY
SEQRES 18 B 308 VAL VAL LEU TRP GLU ILE ALA THR LEU ALA GLU GLN PRO
SEQRES 19 B 308 TYR GLN GLY LEU SER ASN GLU GLN VAL LEU ARG PHE VAL
SEQRES 20 B 308 MET GLU GLY GLY LEU LEU ASP LYS PRO ASP ASN CYS PRO
SEQRES 21 B 308 ASP MET LEU PHE GLU LEU MET ARG MET CYS TRP GLN TYR
SEQRES 22 B 308 ASN PRO LYS MET ARG PRO SER PHE LEU GLU ILE ILE SER
SEQRES 23 B 308 SER ILE LYS GLU GLU MET GLU PRO GLY PHE ARG GLU VAL
SEQRES 24 B 308 SER PHE TYR TYR SER GLU GLU ASN LYS
SEQRES 1 C 308 GLY SER PHE SER ALA ALA ASP VAL TYR VAL PRO ASP GLU
SEQRES 2 C 308 TRP GLU VAL ALA ARG GLU LYS ILE THR MET SER ARG GLU
SEQRES 3 C 308 LEU GLY GLN GLY SER PHE GLY MET VAL TYR GLU GLY VAL
SEQRES 4 C 308 ALA LYS GLY VAL VAL LYS ASP GLU PRO GLU THR ARG VAL
SEQRES 5 C 308 ALA ILE LYS THR VAL ASN GLU ALA ALA SER MET ARG GLU
SEQRES 6 C 308 ARG ILE GLU PHE LEU ASN GLU ALA SER VAL MET LYS GLU
SEQRES 7 C 308 PHE ASN CYS HIS HIS VAL VAL ARG LEU LEU GLY VAL VAL
SEQRES 8 C 308 SER GLN GLY GLN PRO THR LEU VAL ILE MET GLU LEU MET
SEQRES 9 C 308 THR ARG GLY ASP LEU LYS SER TYR LEU ARG SER LEU ARG
SEQRES 10 C 308 PRO GLU MET GLU ASN ASN PRO VAL LEU ALA PRO PRO SER
SEQRES 11 C 308 LEU SER LYS MET ILE GLN MET ALA GLY GLU ILE ALA ASP
SEQRES 12 C 308 GLY MET ALA TYR LEU ASN ALA ASN LYS PHE VAL HIS ARG
SEQRES 13 C 308 ASP LEU ALA ALA ARG ASN CYS MET VAL ALA GLU ASP PHE
SEQRES 14 C 308 THR VAL LYS ILE GLY ASP PHE GLY MET THR ARG ASP ILE
SEQRES 15 C 308 TYR GLU THR ASP TYR TYR ARG LYS GLY GLY LYS GLY LEU
SEQRES 16 C 308 LEU PRO VAL ARG TRP MET SER PRO GLU SER LEU LYS ASP
SEQRES 17 C 308 GLY VAL PHE THR THR TYR SER ASP VAL TRP SER PHE GLY
SEQRES 18 C 308 VAL VAL LEU TRP GLU ILE ALA THR LEU ALA GLU GLN PRO
SEQRES 19 C 308 TYR GLN GLY LEU SER ASN GLU GLN VAL LEU ARG PHE VAL
SEQRES 20 C 308 MET GLU GLY GLY LEU LEU ASP LYS PRO ASP ASN CYS PRO
SEQRES 21 C 308 ASP MET LEU PHE GLU LEU MET ARG MET CYS TRP GLN TYR
SEQRES 22 C 308 ASN PRO LYS MET ARG PRO SER PHE LEU GLU ILE ILE SER
SEQRES 23 C 308 SER ILE LYS GLU GLU MET GLU PRO GLY PHE ARG GLU VAL
SEQRES 24 C 308 SER PHE TYR TYR SER GLU GLU ASN LYS
HET MG A 304 1
HET SO4 A 305 5
HET ANP A 301 31
HET SO4 B 307 5
HET ANP B 302 31
HET SO4 C 306 5
HET ANP C 303 31
HETNAM MG MAGNESIUM ION
HETNAM SO4 SULFATE ION
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
FORMUL 4 MG MG 2+
FORMUL 5 SO4 3(O4 S 2-)
FORMUL 6 ANP 3(C10 H17 N6 O12 P3)
FORMUL 11 HOH *252(H2 O)
HELIX 1 1 SER A 1040 SER A 1052 1 13
HELIX 2 2 VAL A 1053 PHE A 1057 5 5
HELIX 3 3 ASP A 1086 ARG A 1095 1 10
HELIX 4 4 SER A 1108 ASN A 1129 1 22
HELIX 5 5 ALA A 1137 ARG A 1139 5 3
HELIX 6 6 PRO A 1175 MET A 1179 5 5
HELIX 7 7 SER A 1180 GLY A 1187 1 8
HELIX 8 8 THR A 1190 THR A 1207 1 18
HELIX 9 9 SER A 1217 GLU A 1227 1 11
HELIX 10 10 PRO A 1238 TRP A 1249 1 12
HELIX 11 11 ASN A 1252 ARG A 1256 5 5
HELIX 12 12 SER A 1258 SER A 1265 1 8
HELIX 13 13 ILE A 1266 MET A 1270 5 5
HELIX 14 14 GLU A 1271 PRO A 1272 5 2
HELIX 15 15 GLY A 1273 SER A 1278 1 6
HELIX 16 16 SER B 1040 SER B 1052 1 13
HELIX 17 17 VAL B 1053 PHE B 1057 5 5
HELIX 18 18 ASP B 1086 SER B 1093 1 8
HELIX 19 19 SER B 1108 ASN B 1129 1 22
HELIX 20 20 ALA B 1137 ARG B 1139 5 3
HELIX 21 21 PRO B 1175 MET B 1179 5 5
HELIX 22 22 SER B 1180 GLY B 1187 1 8
HELIX 23 23 THR B 1190 THR B 1207 1 18
HELIX 24 24 SER B 1217 GLU B 1227 1 11
HELIX 25 25 PRO B 1238 TRP B 1249 1 12
HELIX 26 26 ASN B 1252 ARG B 1256 5 5
HELIX 27 27 SER B 1258 SER B 1265 1 8
HELIX 28 28 ILE B 1266 MET B 1270 5 5
HELIX 29 29 GLU B 1271 PRO B 1272 5 2
HELIX 30 30 GLY B 1273 SER B 1278 1 6
HELIX 31 31 SER C 1040 SER C 1052 1 13
HELIX 32 32 VAL C 1053 PHE C 1057 5 5
HELIX 33 33 ASP C 1086 SER C 1093 1 8
HELIX 34 34 SER C 1108 ASN C 1129 1 22
HELIX 35 35 ALA C 1137 ARG C 1139 5 3
HELIX 36 36 PRO C 1175 MET C 1179 5 5
HELIX 37 37 SER C 1180 GLY C 1187 1 8
HELIX 38 38 THR C 1190 THR C 1207 1 18
HELIX 39 39 SER C 1217 GLU C 1227 1 11
HELIX 40 40 PRO C 1238 TRP C 1249 1 12
HELIX 41 41 ASN C 1252 ARG C 1256 5 5
HELIX 42 42 SER C 1258 SER C 1265 1 8
HELIX 43 43 ILE C 1266 MET C 1270 5 5
HELIX 44 44 GLU C 1271 PRO C 1272 5 2
HELIX 45 45 GLY C 1273 SER C 1278 1 6
SHEET 1 A 2 VAL A 986 TYR A 987 0
SHEET 2 A 2 GLY B1172 LEU B1173 1 O GLY B1172 N TYR A 987
SHEET 1 B 5 ILE A 999 GLN A1007 0
SHEET 2 B 5 MET A1012 VAL A1022 -1 O VAL A1013 N LEU A1005
SHEET 3 B 5 GLU A1025 THR A1034 -1 N GLU A1025 O VAL A1022
SHEET 4 B 5 LEU A1076 GLU A1080 -1 O VAL A1077 N LYS A1033
SHEET 5 B 5 LEU A1065 VAL A1069 -1 N LEU A1066 O ILE A1078
SHEET 1 C 2 PHE A1131 VAL A1132 0
SHEET 2 C 2 ARG A1167 LYS A1168 1 O ARG A1167 N VAL A1132
SHEET 1 D 2 CYS A1141 VAL A1143 0
SHEET 2 D 2 VAL A1149 ILE A1151 -1 O LYS A1150 N MET A1142
SHEET 1 E 2 GLY A1172 LEU A1173 0
SHEET 2 E 2 VAL C 986 TYR C 987 1 N TYR C 987 O GLY A1172
SHEET 1 F 2 VAL B 986 TYR B 987 0
SHEET 2 F 2 GLY C1172 LEU C1173 1 O GLY C1172 N TYR B 987
SHEET 1 G 5 ILE B 999 GLN B1007 0
SHEET 2 G 5 MET B1012 VAL B1022 -1 O VAL B1013 N LEU B1005
SHEET 3 G 5 GLU B1025 THR B1034 -1 N GLU B1025 O VAL B1022
SHEET 4 G 5 LEU B1076 GLU B1080 -1 O VAL B1077 N LYS B1033
SHEET 5 G 5 LEU B1065 VAL B1069 -1 N LEU B1066 O ILE B1078
SHEET 1 H 2 PHE B1131 VAL B1132 0
SHEET 2 H 2 ARG B1167 LYS B1168 1 O ARG B1167 N VAL B1132
SHEET 1 I 2 CYS B1141 VAL B1143 0
SHEET 2 I 2 VAL B1149 ILE B1151 -1 O LYS B1150 N MET B1142
SHEET 1 J 5 ILE C 999 GLN C1007 0
SHEET 2 J 5 MET C1012 VAL C1022 -1 O VAL C1013 N LEU C1005
SHEET 3 J 5 GLU C1025 THR C1034 -1 N GLU C1025 O VAL C1022
SHEET 4 J 5 LEU C1076 GLU C1080 -1 O VAL C1077 N LYS C1033
SHEET 5 J 5 LEU C1065 VAL C1069 -1 N LEU C1066 O ILE C1078
SHEET 1 K 2 PHE C1131 VAL C1132 0
SHEET 2 K 2 ARG C1167 LYS C1168 1 O ARG C1167 N VAL C1132
SHEET 1 L 2 CYS C1141 VAL C1143 0
SHEET 2 L 2 VAL C1149 ILE C1151 -1 O LYS C1150 N MET C1142
LINK O3 SO4 A 305 NH1 ARG C1223 1555 1565 1.79
LINK O HOH A 250 MG MG A 304 1555 1555 2.39
LINK O HOH A 251 MG MG A 304 1555 1555 2.41
LINK O2G ANP A 301 MG MG A 304 1555 1555 2.06
LINK O1A ANP A 301 MG MG A 304 1555 1555 2.27
SITE 1 AC1 3 HOH A 250 HOH A 251 ANP A 301
SITE 1 AC2 7 HOH A 36 HOH A 219 HOH A 241 LEU A1104
SITE 2 AC2 7 ALA A1105 GLN C1220 ARG C1223
SITE 1 AC3 5 GLN B1220 ARG B1223 HOH C 142 LEU C1104
SITE 2 AC3 5 ALA C1105
SITE 1 AC4 4 HOH B 56 ARG B1177 GLN B1211 ASN B1218
SITE 1 AC5 19 HOH A 105 HOH A 106 HOH A 107 HOH A 206
SITE 2 AC5 19 HOH A 250 HOH A 251 MG A 304 LEU A1005
SITE 3 AC5 19 GLY A1006 GLN A1007 GLY A1008 SER A1009
SITE 4 AC5 19 VAL A1013 ALA A1031 LYS A1033 GLU A1080
SITE 5 AC5 19 LEU A1081 MET A1082 MET A1142
SITE 1 AC6 14 HOH B 102 HOH B 155 LEU B1005 GLY B1006
SITE 2 AC6 14 GLN B1007 GLY B1008 SER B1009 VAL B1013
SITE 3 AC6 14 ALA B1031 LYS B1033 GLU B1080 LEU B1081
SITE 4 AC6 14 MET B1082 MET B1142
SITE 1 AC7 15 HOH C 252 LEU C1005 GLY C1006 GLN C1007
SITE 2 AC7 15 GLY C1008 SER C1009 VAL C1013 ALA C1031
SITE 3 AC7 15 LYS C1033 MET C1079 GLU C1080 LEU C1081
SITE 4 AC7 15 MET C1082 MET C1142 LYS C1171
CRYST1 85.963 85.963 132.204 90.00 90.00 120.00 P 32 9
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 0.011633 0.006716 0.000000 0.00000
SCALE2 0.000000 0.013433 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007564 0.00000
(ATOM LINES ARE NOT SHOWN.)
END