HEADER TRANSFERASE 02-MAR-16 5FXR
TITLE IGFR-1R COMPLEX WITH A PYRIMIDINE INHIBITOR.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN-LIKE GROWTH FACTOR 1 RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE, UNP RESIDUES 980-1286;
COMPND 5 SYNONYM: INSULIN-LIKE GROWTH FACTOR I RECEPTOR, IGF-I RECEPTOR, IGFR-
COMPND 6 1R;
COMPND 7 EC: 2.7.10.1;
COMPND 8 ENGINEERED: 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: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.DEGORCE,S.BOYD,J.CURWEN,R.DUCRAY,C.HALSALL,C.JONES,F.LACH,E.LENZ,
AUTHOR 2 M.PASS,S.PASS,C.TRIGWELL,R.NORMAN,C.PHILLIPS
REVDAT 3 11-JUL-18 5FXR 1 JRNL
REVDAT 2 16-MAY-18 5FXR 1 JRNL
REVDAT 1 19-OCT-16 5FXR 0
JRNL AUTH S.L.DEGORCE,S.BOYD,J.O.CURWEN,R.DUCRAY,C.T.HALSALL,
JRNL AUTH 2 C.D.JONES,F.LACH,E.M.LENZ,M.PASS,S.PASS,C.TRIGWELL
JRNL TITL DISCOVERY OF A POTENT, SELECTIVE, ORALLY BIOAVAILABLE, AND
JRNL TITL 2 EFFICACIOUS NOVEL 2-(PYRAZOL-4-YLAMINO)-PYRIMIDINE INHIBITOR
JRNL TITL 3 OF THE INSULIN-LIKE GROWTH FACTOR-1 RECEPTOR (IGF-1R).
JRNL REF J. MED. CHEM. V. 59 4859 2016
JRNL REFN ISSN 1520-4804
JRNL PMID 27078757
JRNL DOI 10.1021/ACS.JMEDCHEM.6B00203
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0069
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 13146
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) : 0.230
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 693
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 934
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.50
REMARK 3 BIN R VALUE (WORKING SET) : 0.2380
REMARK 3 BIN FREE R VALUE SET COUNT : 61
REMARK 3 BIN FREE R VALUE : 0.3590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2353
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 194
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.12000
REMARK 3 B22 (A**2) : 0.15000
REMARK 3 B33 (A**2) : -0.27000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.540
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.320
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.226
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.716
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.921
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.874
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2464 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1651 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3339 ; 1.475 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4014 ; 1.675 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 302 ; 8.036 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 111 ;34.496 ;24.054
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 413 ;17.546 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;19.286 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 357 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2775 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 503 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1502 ; 0.441 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 608 ; 0.074 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2418 ; 0.826 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 962 ; 1.273 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 919 ; 2.009 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 979 A 1283
REMARK 3 ORIGIN FOR THE GROUP (A): 33.2280 -7.0278 62.3130
REMARK 3 T TENSOR
REMARK 3 T11: 0.1570 T22: 0.0072
REMARK 3 T33: -0.0014 T12: 0.0126
REMARK 3 T13: -0.0475 T23: 0.0562
REMARK 3 L TENSOR
REMARK 3 L11: 2.5989 L22: 0.1463
REMARK 3 L33: 1.4534 L12: 0.0748
REMARK 3 L13: -1.7545 L23: 0.1086
REMARK 3 S TENSOR
REMARK 3 S11: -0.3695 S12: -0.3011 S13: -0.1060
REMARK 3 S21: 0.1118 S22: 0.1022 S23: -0.0473
REMARK 3 S31: 0.2683 S32: 0.4954 S33: 0.2672
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2284 A 2284
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0004 -4.4477 52.7598
REMARK 3 T TENSOR
REMARK 3 T11: 0.0003 T22: -0.0175
REMARK 3 T33: 0.0809 T12: 0.0221
REMARK 3 T13: -0.0510 T23: -0.0488
REMARK 3 L TENSOR
REMARK 3 L11: 1.7347 L22: 3.5903
REMARK 3 L33: 9.5597 L12: -0.2301
REMARK 3 L13: -2.7633 L23: -3.9184
REMARK 3 S TENSOR
REMARK 3 S11: 0.1617 S12: 1.3692 S13: -0.3430
REMARK 3 S21: 0.4555 S22: -0.4633 S23: 0.6045
REMARK 3 S31: 0.3535 S32: 0.4984 S33: 0.3016
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 5FXR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1290066340.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
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 : 13146
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 29.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.08000
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 20.62600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.08300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.66550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.08300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.62600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.66550
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 983
REMARK 465 ASN A 1036
REMARK 465 GLY A 1169
REMARK 465 GLY A 1170
REMARK 465 LYS A 1171
REMARK 465 GLU A 1284
REMARK 465 ASN A 1285
REMARK 465 LYS A 1286
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 ARG A1003 CD NE CZ NH1 NH2
REMARK 470 SER A1009 OG
REMARK 470 LYS A1023 CG CD CE NZ
REMARK 470 GLU A1037 CB CG CD OE1 OE2
REMARK 470 MET A1098 CG SD CE
REMARK 470 GLU A1099 CG CD OE1 OE2
REMARK 470 ARG A1158 CD NE CZ NH1 NH2
REMARK 470 LYS A1185 CD CE NZ
REMARK 470 ARG A1223 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1254 CD CE NZ
REMARK 470 GLU A1271 CG CD OE1 OE2
REMARK 470 GLU A1276 CG CD OE1 OE2
REMARK 470 GLU A1283 CG CD OE1 OE2
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 OH TYR A 1166 OE2 GLU A 1219 2.08
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 ASP A 990 -155.51 -142.12
REMARK 500 GLU A 997 5.04 -69.93
REMARK 500 SER A1002 -103.89 -132.15
REMARK 500 ALA A1038 -54.55 12.80
REMARK 500 MET A1098 34.72 -89.54
REMARK 500 ARG A1134 -12.94 82.75
REMARK 500 PHE A1147 -6.90 89.03
REMARK 500 TYR A1161 49.11 -99.45
REMARK 500 ALA A1209 42.96 73.31
REMARK 500 GLN A1214 -62.93 -12.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A 1037 ALA A 1038 83.71
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 A2194 DISTANCE = 5.86 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 8LN A 2284
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FXQ RELATED DB: PDB
REMARK 900 IGFR-1R COMPLEX WITH A PYRIMIDINE INHIBITOR.
REMARK 900 RELATED ID: 5FXS RELATED DB: PDB
REMARK 900 IGFR-1R COMPLEX WITH A PYRIMIDINE INHIBITOR.
DBREF 5FXR A 980 1286 UNP P08069 IGF1R_HUMAN 980 1286
SEQADV 5FXR GLY A 979 UNP P08069 EXPRESSION TAG
SEQRES 1 A 308 GLY TYR 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
HET 8LN A2284 29
HETNAM 8LN 5-CHLORANYL-4-IMIDAZO[1,2-A]PYRIDIN-3-YL-N-(3-METHYL-1-
HETNAM 2 8LN PIPERIDIN-4-YL-PYRAZOL-4-YL)PYRIMIDIN-2-AMINE
FORMUL 2 8LN C20 H21 CL N8
FORMUL 3 HOH *194(H2 O)
HELIX 1 1 ALA A 995 GLU A 997 5 3
HELIX 2 2 SER A 1040 SER A 1052 1 13
HELIX 3 3 VAL A 1053 PHE A 1057 5 5
HELIX 4 4 ASP A 1086 SER A 1093 1 8
HELIX 5 5 SER A 1108 ASN A 1129 1 22
HELIX 6 6 ALA A 1137 ARG A 1139 5 3
HELIX 7 7 TYR A 1161 TYR A 1165 5 5
HELIX 8 8 PRO A 1175 MET A 1179 5 5
HELIX 9 9 SER A 1180 GLY A 1187 1 8
HELIX 10 10 THR A 1190 LEU A 1208 1 19
HELIX 11 11 SER A 1217 GLU A 1227 1 11
HELIX 12 12 PRO A 1238 TRP A 1249 1 12
HELIX 13 13 ASN A 1252 ARG A 1256 5 5
HELIX 14 14 SER A 1258 LYS A 1267 1 10
HELIX 15 15 GLU A 1268 MET A 1270 5 3
HELIX 16 16 GLY A 1273 SER A 1278 1 6
SHEET 1 AA 5 ILE A 999 GLN A1007 0
SHEET 2 AA 5 MET A1012 VAL A1022 -1 O VAL A1013 N LEU A1005
SHEET 3 AA 5 GLU A1025 THR A1034 -1 O GLU A1025 N VAL A1022
SHEET 4 AA 5 LEU A1076 GLU A1080 -1 O VAL A1077 N LYS A1033
SHEET 5 AA 5 LEU A1065 VAL A1069 -1 N LEU A1066 O ILE A1078
SHEET 1 AB 2 CYS A1141 VAL A1143 0
SHEET 2 AB 2 VAL A1149 ILE A1151 -1 O LYS A1150 N MET A1142
SHEET 1 AC 2 TYR A1166 ARG A1167 0
SHEET 2 AC 2 LEU A1173 LEU A1174 -1 O LEU A1174 N TYR A1166
CISPEP 1 GLN A 1073 PRO A 1074 0 4.01
SITE 1 AC1 9 PHE A 981 SER A 982 LEU A1005 VAL A1013
SITE 2 AC1 9 ALA A1031 GLU A1080 MET A1082 GLY A1085
SITE 3 AC1 9 HOH A2061
CRYST1 41.252 67.331 122.166 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 0.024241 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014852 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008186 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
