HEADER TRANSFERASE 03-JUN-19 6P69
TITLE CRYSTAL STRUCTURE OF FGFR1-Y563C (FGFR4 SURROGATE) COVALENTLY BOUND TO
TITLE 2 COMPOUND 11.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBROBLAST GROWTH FACTOR RECEPTOR 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: FGFR-1,BASIC FIBROBLAST GROWTH FACTOR RECEPTOR 1,BFGF-R-1,
COMPND 5 FMS-LIKE TYROSINE KINASE 2,FLT-2,N-SAM,PROTO-ONCOGENE C-FGR;
COMPND 6 EC: 2.7.10.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: FGFR1, BFGFR, CEK, FGFBR, FLG, FLT2, HBGFR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FGFR, INHIBITOR COMPLEX, COVALENT INHIBITOR, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.A.LARSEN
REVDAT 1 19-JUN-19 6P69 0
JRNL AUTH S.PRAJAPATI
JRNL TITL TO BE PUBLISHED
JRNL REF TBD
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.11
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 36264
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1950
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2651
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.2110
REMARK 3 BIN FREE R VALUE SET COUNT : 144
REMARK 3 BIN FREE R VALUE : 0.2740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4562
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 115
REMARK 3 SOLVENT ATOMS : 248
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.07000
REMARK 3 B22 (A**2) : -0.03000
REMARK 3 B33 (A**2) : -0.06000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.06000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.227
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.203
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.146
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.693
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4785 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4534 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6463 ; 1.854 ; 2.000
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10524 ; 1.242 ; 3.009
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 574 ; 6.939 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 206 ;38.515 ;24.078
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 855 ;16.193 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;15.534 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 702 ; 0.105 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5177 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 927 ; 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): 2296 ; 2.942 ; 3.188
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2295 ; 2.938 ; 3.187
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2861 ; 4.570 ; 4.759
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2862 ; 4.569 ; 4.760
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2489 ; 3.669 ; 3.656
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2490 ; 3.668 ; 3.656
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3600 ; 5.678 ; 5.314
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5391 ; 7.632 ;36.853
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5392 ; 7.636 ;36.861
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 6P69 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-19.
REMARK 100 THE DEPOSITION ID IS D_1000241957.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36364
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.43900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3RHX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1:1 MIX OF PROTEIN + RESERVOIR PROTEIN
REMARK 280 AT ~15 MG/ML FORMULATED IN: 20MM TRIS PH 8, 20MM NACL, 2MM TCEP
REMARK 280 RESERVOIR: 14-18% PEG 10K 0.3 M (NH4)2SO4 0.1 M MES PH 6.5 5%
REMARK 280 ETHYLENE GLYCOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 102.68250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.25800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 102.68250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.25800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 990 LIES ON A SPECIAL POSITION.
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 457
REMARK 465 ALA A 458
REMARK 465 GLY A 459
REMARK 465 VAL A 460
REMARK 465 SER A 461
REMARK 465 ASP A 501
REMARK 465 LYS A 502
REMARK 465 ASP A 503
REMARK 465 LYS A 504
REMARK 465 GLY A 580
REMARK 465 LEU A 581
REMARK 465 GLU A 582
REMARK 465 TYR A 583
REMARK 465 SER A 584
REMARK 465 TYR A 585
REMARK 465 ASN A 586
REMARK 465 PRO A 587
REMARK 465 SER A 588
REMARK 465 HIS A 589
REMARK 465 ASN A 590
REMARK 465 PRO A 591
REMARK 465 GLY B 457
REMARK 465 ALA B 458
REMARK 465 GLY B 459
REMARK 465 VAL B 460
REMARK 465 ASP B 501
REMARK 465 LYS B 502
REMARK 465 ASP B 503
REMARK 465 LYS B 504
REMARK 465 GLY B 580
REMARK 465 LEU B 581
REMARK 465 GLU B 582
REMARK 465 TYR B 583
REMARK 465 SER B 584
REMARK 465 TYR B 585
REMARK 465 ASN B 586
REMARK 465 PRO B 587
REMARK 465 SER B 588
REMARK 465 HIS B 589
REMARK 465 ASN B 590
REMARK 465 PRO B 591
REMARK 465 ASN B 763
REMARK 465 GLN B 764
REMARK 465 GLU B 765
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 A 675 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 592 CG CD OE1 OE2
REMARK 470 ARG B 675 CG CD NE CZ NH1 NH2
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 CYS A 603 CB CYS A 603 SG -0.550
REMARK 500 CYS B 603 CB CYS B 603 SG -0.203
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 ARG A 470 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 MET A 534 CG - SD - CE ANGL. DEV. = -9.9 DEGREES
REMARK 500 CYS A 603 CA - CB - SG ANGL. DEV. = 11.0 DEGREES
REMARK 500 ASP A 682 CB - CG - OD2 ANGL. DEV. = -5.5 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 593 120.84 119.13
REMARK 500 ARG A 622 -13.30 79.25
REMARK 500 ASP A 623 53.99 -141.97
REMARK 500 HIS A 649 100.26 -55.18
REMARK 500 HIS A 650 69.82 -113.93
REMARK 500 PHE B 489 42.07 -100.19
REMARK 500 ARG B 622 -25.42 79.15
REMARK 500 ARG B 675 10.19 48.71
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 ILE A 648 HIS A 649 -134.33
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 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue O21 A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide O21 B 804 and CYS B
REMARK 800 563
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6P68 RELATED DB: PDB
DBREF 6P69 A 458 765 UNP P11362 FGFR1_HUMAN 458 765
DBREF 6P69 B 458 765 UNP P11362 FGFR1_HUMAN 458 765
SEQADV 6P69 GLY A 457 UNP P11362 EXPRESSION TAG
SEQADV 6P69 ALA A 488 UNP P11362 CYS 488 ENGINEERED MUTATION
SEQADV 6P69 CYS A 563 UNP P11362 TYR 563 ENGINEERED MUTATION
SEQADV 6P69 SER A 584 UNP P11362 CYS 584 CONFLICT
SEQADV 6P69 GLY B 457 UNP P11362 EXPRESSION TAG
SEQADV 6P69 ALA B 488 UNP P11362 CYS 488 ENGINEERED MUTATION
SEQADV 6P69 CYS B 563 UNP P11362 TYR 563 ENGINEERED MUTATION
SEQADV 6P69 SER B 584 UNP P11362 CYS 584 CONFLICT
SEQRES 1 A 309 GLY ALA GLY VAL SER GLU TYR GLU LEU PRO GLU ASP PRO
SEQRES 2 A 309 ARG TRP GLU LEU PRO ARG ASP ARG LEU VAL LEU GLY LYS
SEQRES 3 A 309 PRO LEU GLY GLU GLY ALA PHE GLY GLN VAL VAL LEU ALA
SEQRES 4 A 309 GLU ALA ILE GLY LEU ASP LYS ASP LYS PRO ASN ARG VAL
SEQRES 5 A 309 THR LYS VAL ALA VAL LYS MET LEU LYS SER ASP ALA THR
SEQRES 6 A 309 GLU LYS ASP LEU SER ASP LEU ILE SER GLU MET GLU MET
SEQRES 7 A 309 MET LYS MET ILE GLY LYS HIS LYS ASN ILE ILE ASN LEU
SEQRES 8 A 309 LEU GLY ALA CYS THR GLN ASP GLY PRO LEU TYR VAL ILE
SEQRES 9 A 309 VAL GLU CYS ALA SER LYS GLY ASN LEU ARG GLU TYR LEU
SEQRES 10 A 309 GLN ALA ARG ARG PRO PRO GLY LEU GLU TYR SER TYR ASN
SEQRES 11 A 309 PRO SER HIS ASN PRO GLU GLU GLN LEU SER SER LYS ASP
SEQRES 12 A 309 LEU VAL SER CYS ALA TYR GLN VAL ALA ARG GLY MET GLU
SEQRES 13 A 309 TYR LEU ALA SER LYS LYS CYS ILE HIS ARG ASP LEU ALA
SEQRES 14 A 309 ALA ARG ASN VAL LEU VAL THR GLU ASP ASN VAL MET LYS
SEQRES 15 A 309 ILE ALA ASP PHE GLY LEU ALA ARG ASP ILE HIS HIS ILE
SEQRES 16 A 309 ASP TYR TYR LYS LYS THR THR ASN GLY ARG LEU PRO VAL
SEQRES 17 A 309 LYS TRP MET ALA PRO GLU ALA LEU PHE ASP ARG ILE TYR
SEQRES 18 A 309 THR HIS GLN SER ASP VAL TRP SER PHE GLY VAL LEU LEU
SEQRES 19 A 309 TRP GLU ILE PHE THR LEU GLY GLY SER PRO TYR PRO GLY
SEQRES 20 A 309 VAL PRO VAL GLU GLU LEU PHE LYS LEU LEU LYS GLU GLY
SEQRES 21 A 309 HIS ARG MET ASP LYS PRO SER ASN CYS THR ASN GLU LEU
SEQRES 22 A 309 TYR MET MET MET ARG ASP CYS TRP HIS ALA VAL PRO SER
SEQRES 23 A 309 GLN ARG PRO THR PHE LYS GLN LEU VAL GLU ASP LEU ASP
SEQRES 24 A 309 ARG ILE VAL ALA LEU THR SER ASN GLN GLU
SEQRES 1 B 309 GLY ALA GLY VAL SER GLU TYR GLU LEU PRO GLU ASP PRO
SEQRES 2 B 309 ARG TRP GLU LEU PRO ARG ASP ARG LEU VAL LEU GLY LYS
SEQRES 3 B 309 PRO LEU GLY GLU GLY ALA PHE GLY GLN VAL VAL LEU ALA
SEQRES 4 B 309 GLU ALA ILE GLY LEU ASP LYS ASP LYS PRO ASN ARG VAL
SEQRES 5 B 309 THR LYS VAL ALA VAL LYS MET LEU LYS SER ASP ALA THR
SEQRES 6 B 309 GLU LYS ASP LEU SER ASP LEU ILE SER GLU MET GLU MET
SEQRES 7 B 309 MET LYS MET ILE GLY LYS HIS LYS ASN ILE ILE ASN LEU
SEQRES 8 B 309 LEU GLY ALA CYS THR GLN ASP GLY PRO LEU TYR VAL ILE
SEQRES 9 B 309 VAL GLU CYS ALA SER LYS GLY ASN LEU ARG GLU TYR LEU
SEQRES 10 B 309 GLN ALA ARG ARG PRO PRO GLY LEU GLU TYR SER TYR ASN
SEQRES 11 B 309 PRO SER HIS ASN PRO GLU GLU GLN LEU SER SER LYS ASP
SEQRES 12 B 309 LEU VAL SER CYS ALA TYR GLN VAL ALA ARG GLY MET GLU
SEQRES 13 B 309 TYR LEU ALA SER LYS LYS CYS ILE HIS ARG ASP LEU ALA
SEQRES 14 B 309 ALA ARG ASN VAL LEU VAL THR GLU ASP ASN VAL MET LYS
SEQRES 15 B 309 ILE ALA ASP PHE GLY LEU ALA ARG ASP ILE HIS HIS ILE
SEQRES 16 B 309 ASP TYR TYR LYS LYS THR THR ASN GLY ARG LEU PRO VAL
SEQRES 17 B 309 LYS TRP MET ALA PRO GLU ALA LEU PHE ASP ARG ILE TYR
SEQRES 18 B 309 THR HIS GLN SER ASP VAL TRP SER PHE GLY VAL LEU LEU
SEQRES 19 B 309 TRP GLU ILE PHE THR LEU GLY GLY SER PRO TYR PRO GLY
SEQRES 20 B 309 VAL PRO VAL GLU GLU LEU PHE LYS LEU LEU LYS GLU GLY
SEQRES 21 B 309 HIS ARG MET ASP LYS PRO SER ASN CYS THR ASN GLU LEU
SEQRES 22 B 309 TYR MET MET MET ARG ASP CYS TRP HIS ALA VAL PRO SER
SEQRES 23 B 309 GLN ARG PRO THR PHE LYS GLN LEU VAL GLU ASP LEU ASP
SEQRES 24 B 309 ARG ILE VAL ALA LEU THR SER ASN GLN GLU
HET SO4 A 801 5
HET EDO A 802 4
HET EDO A 803 4
HET O21 A 804 44
HET SO4 B 801 5
HET SO4 B 802 5
HET EDO B 803 4
HET O21 B 804 44
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM O21 N-{2-[(6-{[(2,6-DICHLORO-3,5-DIMETHOXYPHENYL)
HETNAM 2 O21 CARBAMOYL][3-(4-METHYLPIPERAZIN-1-YL)
HETNAM 3 O21 PROPYL]AMINO}PYRIMIDIN-4-YL)AMINO]PHENYL}PROP-2-
HETNAM 4 O21 ENAMIDE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 SO4 3(O4 S 2-)
FORMUL 4 EDO 3(C2 H6 O2)
FORMUL 6 O21 2(C30 H36 CL2 N8 O4)
FORMUL 11 HOH *248(H2 O)
HELIX 1 AA1 PRO A 474 ASP A 476 5 3
HELIX 2 AA2 THR A 521 GLY A 539 1 19
HELIX 3 AA3 ASN A 568 ALA A 575 1 8
HELIX 4 AA4 SER A 596 LYS A 617 1 22
HELIX 5 AA5 ALA A 625 ARG A 627 5 3
HELIX 6 AA6 LEU A 662 MET A 667 5 6
HELIX 7 AA7 ALA A 668 ARG A 675 1 8
HELIX 8 AA8 THR A 678 THR A 695 1 18
HELIX 9 AA9 PRO A 705 GLU A 715 1 11
HELIX 10 AB1 THR A 726 TRP A 737 1 12
HELIX 11 AB2 VAL A 740 ARG A 744 5 5
HELIX 12 AB3 THR A 746 THR A 761 1 16
HELIX 13 AB4 PRO B 474 ASP B 476 5 3
HELIX 14 AB5 THR B 521 GLY B 539 1 19
HELIX 15 AB6 ASN B 568 ARG B 576 1 9
HELIX 16 AB7 SER B 596 LYS B 617 1 22
HELIX 17 AB8 ALA B 625 ARG B 627 5 3
HELIX 18 AB9 LEU B 662 MET B 667 5 6
HELIX 19 AC1 ALA B 668 ASP B 674 1 7
HELIX 20 AC2 THR B 678 THR B 695 1 18
HELIX 21 AC3 PRO B 705 GLU B 715 1 11
HELIX 22 AC4 THR B 726 TRP B 737 1 12
HELIX 23 AC5 VAL B 740 ARG B 744 5 5
HELIX 24 AC6 THR B 746 LEU B 760 1 15
SHEET 1 AA1 5 LEU A 478 GLU A 486 0
SHEET 2 AA1 5 GLY A 490 ILE A 498 -1 O GLU A 496 N VAL A 479
SHEET 3 AA1 5 VAL A 508 LEU A 516 -1 O THR A 509 N ALA A 497
SHEET 4 AA1 5 TYR A 558 GLU A 562 -1 O VAL A 561 N ALA A 512
SHEET 5 AA1 5 LEU A 547 CYS A 551 -1 N LEU A 548 O ILE A 560
SHEET 1 AA2 2 VAL A 629 VAL A 631 0
SHEET 2 AA2 2 MET A 637 ILE A 639 -1 O LYS A 638 N LEU A 630
SHEET 1 AA3 5 LEU B 478 GLU B 486 0
SHEET 2 AA3 5 GLY B 490 ILE B 498 -1 O VAL B 492 N LEU B 484
SHEET 3 AA3 5 VAL B 508 LEU B 516 -1 O THR B 509 N ALA B 497
SHEET 4 AA3 5 TYR B 558 GLU B 562 -1 O VAL B 561 N ALA B 512
SHEET 5 AA3 5 LEU B 547 CYS B 551 -1 N GLY B 549 O ILE B 560
SHEET 1 AA4 2 VAL B 629 VAL B 631 0
SHEET 2 AA4 2 MET B 637 ILE B 639 -1 O LYS B 638 N LEU B 630
LINK SG CYS A 563 C28 O21 A 804 1555 1555 1.61
LINK SG CYS B 563 C28 O21 B 804 1555 1555 1.62
CISPEP 1 ALA B 488 PHE B 489 0 -20.06
SITE 1 AC1 6 ARG A 570 ARG A 627 THR A 657 ASN A 659
SITE 2 AC1 6 ARG A 661 HOH A 948
SITE 1 AC2 5 ALA A 615 THR A 746 PHE A 747 LYS A 748
SITE 2 AC2 5 HOH A 902
SITE 1 AC3 6 TRP A 684 TYR A 701 ARG A 718 MET A 719
SITE 2 AC3 6 TRP A 737 HOH A 919
SITE 1 AC4 16 LEU A 484 GLU A 486 GLY A 487 VAL A 492
SITE 2 AC4 16 LEU A 494 ALA A 512 LYS A 514 GLU A 531
SITE 3 AC4 16 VAL A 559 VAL A 561 GLU A 562 CYS A 563
SITE 4 AC4 16 ALA A 564 LEU A 630 ALA A 640 ASP A 641
SITE 1 AC5 6 ARG B 570 ARG B 627 THR B 657 ASN B 659
SITE 2 AC5 6 ARG B 661 HOH B 926
SITE 1 AC6 4 GLN B 574 ASN B 659 ARG B 661 SER B 699
SITE 1 AC7 7 TRP B 684 TYR B 701 LEU B 713 ARG B 718
SITE 2 AC7 7 MET B 719 TRP B 737 HOH B 919
SITE 1 AC8 21 LEU B 484 VAL B 492 LEU B 494 LYS B 510
SITE 2 AC8 21 LYS B 514 GLU B 531 MET B 535 VAL B 559
SITE 3 AC8 21 VAL B 561 GLU B 562 ALA B 564 SER B 565
SITE 4 AC8 21 LEU B 630 ALA B 640 ASP B 641 PHE B 642
SITE 5 AC8 21 HOH B 909 HOH B 933 HOH B 952 HOH B 953
SITE 6 AC8 21 HOH B1000
CRYST1 205.365 58.516 66.131 90.00 107.31 90.00 C 1 2 1 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 0.004869 0.000000 0.001517 0.00000
SCALE2 0.000000 0.017089 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015839 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
