HEADER TRANSFERASE 15-MAY-07 2PY3
TITLE CRYSTAL STRUCTURE OF FGF RECEPTOR 2 (FGFR2) KINASE DOMAIN HARBORING
TITLE 2 THE PATHOGENIC E565G MUTATION RESPONSIBLE FOR PFEIFFER SYNDROME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBROBLAST GROWTH FACTOR RECEPTOR 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: KINASE DOMAIN;
COMPND 5 SYNONYM: FGFR-2, KERATINOCYTE GROWTH FACTOR RECEPTOR 2, CD332
COMPND 6 ANTIGEN;
COMPND 7 EC: 2.7.10.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 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: FGFR2, BEK, KSAM;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYS-S
KEYWDS KINASE DOMAIN FOLD CONSISTING OF N- AND C-LOBES, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.CHEN,M.MOHAMMADI
REVDAT 6 30-AUG-23 2PY3 1 REMARK
REVDAT 5 20-OCT-21 2PY3 1 REMARK SEQADV LINK
REVDAT 4 21-DEC-16 2PY3 1 TITLE
REVDAT 3 07-MAR-12 2PY3 1 HET HETATM VERSN
REVDAT 2 24-FEB-09 2PY3 1 VERSN
REVDAT 1 25-SEP-07 2PY3 0
JRNL AUTH H.CHEN,J.MA,W.LI,A.V.ELISEENKOVA,C.XU,T.A.NEUBERT,
JRNL AUTH 2 W.T.MILLER,M.MOHAMMADI
JRNL TITL A MOLECULAR BRAKE IN THE KINASE HINGE REGION REGULATES THE
JRNL TITL 2 ACTIVITY OF RECEPTOR TYROSINE KINASES.
JRNL REF MOL.CELL V. 27 717 2007
JRNL REFN ISSN 1097-2765
JRNL PMID 17803937
JRNL DOI 10.1016/J.MOLCEL.2007.06.028
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 33959
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) : 0.217
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1684
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4440
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 172
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.71100
REMARK 3 B22 (A**2) : -0.43600
REMARK 3 B33 (A**2) : -2.27500
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.839
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2PY3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1000042910.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-SEP-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97928
REMARK 200 MONOCHROMATOR : KOHZU DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34867
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.3000
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) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.22600
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2PSQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES PH7.5, 25% PEG 4000, 200MM
REMARK 280 (NH4)2SO4, 2% C3H5(OH)3, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 52.44850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.37400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 52.44850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.37400
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 445
REMARK 465 GLY A 446
REMARK 465 SER A 447
REMARK 465 SER A 448
REMARK 465 HIS A 449
REMARK 465 HIS A 450
REMARK 465 HIS A 451
REMARK 465 HIS A 452
REMARK 465 HIS A 453
REMARK 465 HIS A 454
REMARK 465 SER A 455
REMARK 465 GLN A 456
REMARK 465 ASP A 457
REMARK 465 PRO A 458
REMARK 465 MET A 459
REMARK 465 LEU A 460
REMARK 465 ALA A 461
REMARK 465 GLY A 462
REMARK 465 VAL A 463
REMARK 465 SER A 464
REMARK 465 GLU A 465
REMARK 465 TYR A 466
REMARK 465 GLU A 467
REMARK 465 GLY A 488
REMARK 465 GLU A 489
REMARK 465 GLY A 490
REMARK 465 ALA A 491
REMARK 465 PRO A 582
REMARK 465 GLY A 583
REMARK 465 MET A 584
REMARK 465 GLU A 585
REMARK 465 TYR A 586
REMARK 465 SER A 587
REMARK 465 TYR A 588
REMARK 465 ASP A 589
REMARK 465 ILE A 590
REMARK 465 ASN A 591
REMARK 465 ARG A 592
REMARK 465 VAL A 593
REMARK 465 PRO A 594
REMARK 465 GLU A 767
REMARK 465 GLU A 768
REMARK 465 MET B 445
REMARK 465 GLY B 446
REMARK 465 SER B 447
REMARK 465 SER B 448
REMARK 465 HIS B 449
REMARK 465 HIS B 450
REMARK 465 HIS B 451
REMARK 465 HIS B 452
REMARK 465 HIS B 453
REMARK 465 HIS B 454
REMARK 465 SER B 455
REMARK 465 GLN B 456
REMARK 465 ASP B 457
REMARK 465 PRO B 458
REMARK 465 MET B 459
REMARK 465 LEU B 460
REMARK 465 ALA B 461
REMARK 465 GLY B 462
REMARK 465 VAL B 463
REMARK 465 SER B 464
REMARK 465 GLU B 465
REMARK 465 TYR B 466
REMARK 465 GLU B 467
REMARK 465 GLU B 489
REMARK 465 GLY B 490
REMARK 465 ALA B 491
REMARK 465 PHE B 492
REMARK 465 MET B 584
REMARK 465 GLU B 585
REMARK 465 TYR B 586
REMARK 465 SER B 587
REMARK 465 TYR B 588
REMARK 465 ASP B 589
REMARK 465 ILE B 590
REMARK 465 ASN B 591
REMARK 465 ARG B 592
REMARK 465 VAL B 593
REMARK 465 PRO B 594
REMARK 465 GLU B 767
REMARK 465 GLU B 768
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 LYS A 485 CG CD CE NZ
REMARK 470 PHE A 492 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 507 CG CD CE NZ
REMARK 470 LYS A 509 CG CD CE NZ
REMARK 470 LYS A 543 CG CD CE NZ
REMARK 470 LYS A 545 CG CD CE NZ
REMARK 470 GLU A 574 CG CD OE1 OE2
REMARK 470 GLU A 595 CG CD OE1 OE2
REMARK 470 GLU A 596 CG CD OE1 OE2
REMARK 470 GLN A 597 CG CD OE1 NE2
REMARK 470 LYS A 659 CG CD CE NZ
REMARK 470 GLU B 470 CG CD OE1 OE2
REMARK 470 LYS B 485 CG CD CE NZ
REMARK 470 LYS B 507 CG CD CE NZ
REMARK 470 LYS B 509 CG CD CE NZ
REMARK 470 GLU B 510 CG CD OE1 OE2
REMARK 470 LYS B 543 CG CD CE NZ
REMARK 470 GLU B 574 CG CD OE1 OE2
REMARK 470 GLU B 636 CG CD OE1 OE2
REMARK 470 LYS B 659 CG CD CE NZ
REMARK 470 LYS B 714 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 557 65.31 37.61
REMARK 500 GLN A 597 138.10 -28.33
REMARK 500 ARG A 625 -7.92 73.37
REMARK 500 ASP A 644 77.90 46.92
REMARK 500 ASN A 727 37.78 -78.18
REMARK 500 GLN B 494 119.17 5.63
REMARK 500 LYS B 505 -29.18 -38.86
REMARK 500 PRO B 508 -26.75 -38.73
REMARK 500 ASP B 557 60.91 39.43
REMARK 500 PRO B 582 -15.51 -43.68
REMARK 500 ARG B 625 -10.27 71.33
REMARK 500 ASP B 644 73.70 51.90
REMARK 500 ASN B 653 60.27 -102.65
REMARK 500 TYR B 657 -0.53 76.26
REMARK 500 ALA B 726 -77.04 -33.09
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 803 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 631 ND2
REMARK 620 2 ASP A 644 OD2 94.1
REMARK 620 3 ACP A 805 O1G 153.9 92.3
REMARK 620 4 ACP A 805 O2A 105.8 66.6 99.9
REMARK 620 5 ACP A 805 O1A 93.9 87.9 111.6 24.2
REMARK 620 6 ACP A 805 O3G 159.9 102.5 17.2 91.3 97.9
REMARK 620 7 HOH A 934 O 79.2 168.5 97.8 105.9 83.2 86.0
REMARK 620 8 HOH A 946 O 85.3 99.2 68.7 162.1 172.8 81.0 89.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 804 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 644 OD1
REMARK 620 2 ASP A 644 OD2 53.9
REMARK 620 3 ACP A 805 O2G 138.3 84.4
REMARK 620 4 ACP A 805 O2B 103.1 100.2 83.9
REMARK 620 5 ACP A 805 O1B 84.3 89.4 98.1 18.8
REMARK 620 6 HOH A 922 O 106.0 159.8 115.5 85.9 90.8
REMARK 620 7 HOH A 932 O 87.7 94.2 94.7 165.3 166.9 81.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 803 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 631 ND2
REMARK 620 2 ASP B 644 OD2 89.1
REMARK 620 3 ACP B 805 O1G 142.5 64.4
REMARK 620 4 ACP B 805 O2A 93.1 89.6 111.6
REMARK 620 5 ACP B 805 O2G 163.4 104.4 43.6 96.5
REMARK 620 6 HOH B 979 O 76.9 163.4 132.2 82.5 91.0
REMARK 620 7 HOH B 988 O 86.2 92.2 69.8 178.1 83.7 95.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 804 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 644 OD1
REMARK 620 2 ASP B 644 OD2 53.1
REMARK 620 3 ACP B 805 O2B 103.3 101.9
REMARK 620 4 ACP B 805 O2G 110.2 63.0 63.8
REMARK 620 5 ACP B 805 O1B 90.3 94.8 13.1 68.9
REMARK 620 6 ACP B 805 O1G 139.1 86.1 80.9 35.0 91.4
REMARK 620 7 HOH B 961 O 107.0 159.3 87.5 137.0 90.5 113.8
REMARK 620 8 HOH B 980 O 92.7 88.1 163.9 111.3 176.7 87.3 87.2
REMARK 620 N 1 2 3 4 5 6 7
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 SO4 A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP B 805
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PSQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF UNPHOSPHORYLATED UNACTIVATED WILD TYPE FGF
REMARK 900 RECEPTOR 2 (FGFR2) KINASE DOMAIN
REMARK 900 RELATED ID: 2PVF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TYROSINE PHOSPHORYLATED ACTIVATED WILD TYPE
REMARK 900 FGF RECEPTOR 2 (FGFR2) KINASE DOMAIN IN COMPLEX WITH ATP ANALOG AND
REMARK 900 SUBSTRATE PEPTIDE
REMARK 900 RELATED ID: 2PVY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCURE OF FGF RECEPTOR 2 (FGFR2) KINASE DOMAIN HARBORING
REMARK 900 THE PATHOGENIC K659N MUTATION RESPONSIBLE FOR AN UNCLASSIFIED
REMARK 900 CRANIOSYNOSTOSIS SYNDROME.
REMARK 900 RELATED ID: 2PWL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCURE OF FGF RECEPTOR 2 (FGFR2) KINASE DOMAIN HARBORING
REMARK 900 THE PATHOGENIC N549H MUTATION RESPONSIBLE FOR CROUZON SYNDROME.
REMARK 900 RELATED ID: 2PZ5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCURE OF FGF RECEPTOR 2 (FGFR2) KINASE DOMAIN HARBORING
REMARK 900 THE PATHOGENIC N549T MUTATION RESPONSIBLE FOR PFEIFFER SYNDROME
REMARK 900 RELATED ID: 2PZP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCURE OF FGF RECEPTOR 2 (FGFR2) KINASE DOMAIN HARBORING
REMARK 900 THE PATHOGENIC K526E MUTATION RESPONSIBLE FOR CROUZON SYNDROME
REMARK 900 RELATED ID: 2PZR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCURE OF FGF RECEPTOR 2 (FGFR2) KINASE DOMAIN HARBORING
REMARK 900 THE PATHOGENIC K641R MUTATION RESPONSIBLE FOR PFEIFFER SYNDROME
REMARK 900 RELATED ID: 2Q0B RELATED DB: PDB
REMARK 900 CRYSTAL STRUCURE OF FGF RECEPTOR 2 (FGFR2) KINASE DOMAIN HARBORING
REMARK 900 THE PATHOGENIC E565A MUTATION RESPONSIBLE FOR PFEIFFER SYNDROME
DBREF 2PY3 A 458 768 UNP P21802 FGFR2_HUMAN 458 768
DBREF 2PY3 B 458 768 UNP P21802 FGFR2_HUMAN 458 768
SEQADV 2PY3 MET A 445 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 GLY A 446 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 SER A 447 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 SER A 448 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 HIS A 449 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 HIS A 450 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 HIS A 451 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 HIS A 452 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 HIS A 453 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 HIS A 454 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 SER A 455 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 GLN A 456 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 ASP A 457 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 ALA A 491 UNP P21802 CYS 491 ENGINEERED MUTATION
SEQADV 2PY3 GLY A 565 UNP P21802 GLU 565 ENGINEERED MUTATION
SEQADV 2PY3 MET B 445 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 GLY B 446 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 SER B 447 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 SER B 448 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 HIS B 449 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 HIS B 450 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 HIS B 451 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 HIS B 452 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 HIS B 453 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 HIS B 454 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 SER B 455 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 GLN B 456 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 ASP B 457 UNP P21802 EXPRESSION TAG
SEQADV 2PY3 ALA B 491 UNP P21802 CYS 491 ENGINEERED MUTATION
SEQADV 2PY3 GLY B 565 UNP P21802 GLU 565 ENGINEERED MUTATION
SEQRES 1 A 324 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 A 324 PRO MET LEU ALA GLY VAL SER GLU TYR GLU LEU PRO GLU
SEQRES 3 A 324 ASP PRO LYS TRP GLU PHE PRO ARG ASP LYS LEU THR LEU
SEQRES 4 A 324 GLY LYS PRO LEU GLY GLU GLY ALA PHE GLY GLN VAL VAL
SEQRES 5 A 324 MET ALA GLU ALA VAL GLY ILE ASP LYS ASP LYS PRO LYS
SEQRES 6 A 324 GLU ALA VAL THR VAL ALA VAL LYS MET LEU LYS ASP ASP
SEQRES 7 A 324 ALA THR GLU LYS ASP LEU SER ASP LEU VAL SER GLU MET
SEQRES 8 A 324 GLU MET MET LYS MET ILE GLY LYS HIS LYS ASN ILE ILE
SEQRES 9 A 324 ASN LEU LEU GLY ALA CYS THR GLN ASP GLY PRO LEU TYR
SEQRES 10 A 324 VAL ILE VAL GLY TYR ALA SER LYS GLY ASN LEU ARG GLU
SEQRES 11 A 324 TYR LEU ARG ALA ARG ARG PRO PRO GLY MET GLU TYR SER
SEQRES 12 A 324 TYR ASP ILE ASN ARG VAL PRO GLU GLU GLN MET THR PHE
SEQRES 13 A 324 LYS ASP LEU VAL SER CYS THR TYR GLN LEU ALA ARG GLY
SEQRES 14 A 324 MET GLU TYR LEU ALA SER GLN LYS CYS ILE HIS ARG ASP
SEQRES 15 A 324 LEU ALA ALA ARG ASN VAL LEU VAL THR GLU ASN ASN VAL
SEQRES 16 A 324 MET LYS ILE ALA ASP PHE GLY LEU ALA ARG ASP ILE ASN
SEQRES 17 A 324 ASN ILE ASP TYR TYR LYS LYS THR THR ASN GLY ARG LEU
SEQRES 18 A 324 PRO VAL LYS TRP MET ALA PRO GLU ALA LEU PHE ASP ARG
SEQRES 19 A 324 VAL TYR THR HIS GLN SER ASP VAL TRP SER PHE GLY VAL
SEQRES 20 A 324 LEU MET TRP GLU ILE PHE THR LEU GLY GLY SER PRO TYR
SEQRES 21 A 324 PRO GLY ILE PRO VAL GLU GLU LEU PHE LYS LEU LEU LYS
SEQRES 22 A 324 GLU GLY HIS ARG MET ASP LYS PRO ALA ASN CYS THR ASN
SEQRES 23 A 324 GLU LEU TYR MET MET MET ARG ASP CYS TRP HIS ALA VAL
SEQRES 24 A 324 PRO SER GLN ARG PRO THR PHE LYS GLN LEU VAL GLU ASP
SEQRES 25 A 324 LEU ASP ARG ILE LEU THR LEU THR THR ASN GLU GLU
SEQRES 1 B 324 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 B 324 PRO MET LEU ALA GLY VAL SER GLU TYR GLU LEU PRO GLU
SEQRES 3 B 324 ASP PRO LYS TRP GLU PHE PRO ARG ASP LYS LEU THR LEU
SEQRES 4 B 324 GLY LYS PRO LEU GLY GLU GLY ALA PHE GLY GLN VAL VAL
SEQRES 5 B 324 MET ALA GLU ALA VAL GLY ILE ASP LYS ASP LYS PRO LYS
SEQRES 6 B 324 GLU ALA VAL THR VAL ALA VAL LYS MET LEU LYS ASP ASP
SEQRES 7 B 324 ALA THR GLU LYS ASP LEU SER ASP LEU VAL SER GLU MET
SEQRES 8 B 324 GLU MET MET LYS MET ILE GLY LYS HIS LYS ASN ILE ILE
SEQRES 9 B 324 ASN LEU LEU GLY ALA CYS THR GLN ASP GLY PRO LEU TYR
SEQRES 10 B 324 VAL ILE VAL GLY TYR ALA SER LYS GLY ASN LEU ARG GLU
SEQRES 11 B 324 TYR LEU ARG ALA ARG ARG PRO PRO GLY MET GLU TYR SER
SEQRES 12 B 324 TYR ASP ILE ASN ARG VAL PRO GLU GLU GLN MET THR PHE
SEQRES 13 B 324 LYS ASP LEU VAL SER CYS THR TYR GLN LEU ALA ARG GLY
SEQRES 14 B 324 MET GLU TYR LEU ALA SER GLN LYS CYS ILE HIS ARG ASP
SEQRES 15 B 324 LEU ALA ALA ARG ASN VAL LEU VAL THR GLU ASN ASN VAL
SEQRES 16 B 324 MET LYS ILE ALA ASP PHE GLY LEU ALA ARG ASP ILE ASN
SEQRES 17 B 324 ASN ILE ASP TYR TYR LYS LYS THR THR ASN GLY ARG LEU
SEQRES 18 B 324 PRO VAL LYS TRP MET ALA PRO GLU ALA LEU PHE ASP ARG
SEQRES 19 B 324 VAL TYR THR HIS GLN SER ASP VAL TRP SER PHE GLY VAL
SEQRES 20 B 324 LEU MET TRP GLU ILE PHE THR LEU GLY GLY SER PRO TYR
SEQRES 21 B 324 PRO GLY ILE PRO VAL GLU GLU LEU PHE LYS LEU LEU LYS
SEQRES 22 B 324 GLU GLY HIS ARG MET ASP LYS PRO ALA ASN CYS THR ASN
SEQRES 23 B 324 GLU LEU TYR MET MET MET ARG ASP CYS TRP HIS ALA VAL
SEQRES 24 B 324 PRO SER GLN ARG PRO THR PHE LYS GLN LEU VAL GLU ASP
SEQRES 25 B 324 LEU ASP ARG ILE LEU THR LEU THR THR ASN GLU GLU
HET SO4 A 801 5
HET SO4 A 802 5
HET MG A 803 1
HET MG A 804 1
HET ACP A 805 31
HET SO4 B 801 5
HET SO4 B 802 5
HET MG B 803 1
HET MG B 804 1
HET ACP B 805 31
HETNAM SO4 SULFATE ION
HETNAM MG MAGNESIUM ION
HETNAM ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER
HETSYN ACP ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 5 MG 4(MG 2+)
FORMUL 7 ACP 2(C11 H18 N5 O12 P3)
FORMUL 13 HOH *172(H2 O)
HELIX 1 1 PRO A 477 ASP A 479 5 3
HELIX 2 2 THR A 524 GLY A 542 1 19
HELIX 3 3 ASN A 571 ARG A 579 1 9
HELIX 4 4 THR A 599 GLN A 620 1 22
HELIX 5 5 ALA A 628 ARG A 630 5 3
HELIX 6 6 PRO A 666 MET A 670 5 5
HELIX 7 7 ALA A 671 ASP A 677 1 7
HELIX 8 8 THR A 681 THR A 698 1 18
HELIX 9 9 PRO A 708 GLY A 719 1 12
HELIX 10 10 THR A 729 TRP A 740 1 12
HELIX 11 11 VAL A 743 ARG A 747 5 5
HELIX 12 12 THR A 749 ASN A 766 1 18
HELIX 13 13 PRO B 477 ASP B 479 5 3
HELIX 14 14 THR B 524 GLY B 542 1 19
HELIX 15 15 ASN B 571 ARG B 579 1 9
HELIX 16 16 THR B 599 GLN B 620 1 22
HELIX 17 17 ALA B 628 ARG B 630 5 3
HELIX 18 18 PRO B 666 MET B 670 5 5
HELIX 19 19 ALA B 671 ASP B 677 1 7
HELIX 20 20 THR B 681 THR B 698 1 18
HELIX 21 21 PRO B 708 GLU B 718 1 11
HELIX 22 22 THR B 729 TRP B 740 1 12
HELIX 23 23 VAL B 743 ARG B 747 5 5
HELIX 24 24 THR B 749 ASN B 766 1 18
SHEET 1 A 5 LEU A 481 PRO A 486 0
SHEET 2 A 5 GLN A 494 VAL A 501 -1 O MET A 497 N LYS A 485
SHEET 3 A 5 ALA A 511 MET A 518 -1 O VAL A 514 N ALA A 498
SHEET 4 A 5 TYR A 561 GLY A 565 -1 O VAL A 564 N ALA A 515
SHEET 5 A 5 LEU A 550 CYS A 554 -1 N LEU A 551 O ILE A 563
SHEET 1 B 2 CYS A 622 ILE A 623 0
SHEET 2 B 2 ARG A 649 ASP A 650 -1 O ARG A 649 N ILE A 623
SHEET 1 C 2 VAL A 632 VAL A 634 0
SHEET 2 C 2 MET A 640 ILE A 642 -1 O LYS A 641 N LEU A 633
SHEET 1 D 5 LEU B 481 LEU B 487 0
SHEET 2 D 5 VAL B 495 VAL B 501 -1 O MET B 497 N LYS B 485
SHEET 3 D 5 ALA B 511 LYS B 517 -1 O VAL B 514 N ALA B 498
SHEET 4 D 5 TYR B 561 GLY B 565 -1 O VAL B 562 N LYS B 517
SHEET 5 D 5 LEU B 550 CYS B 554 -1 N LEU B 551 O ILE B 563
SHEET 1 E 2 CYS B 622 ILE B 623 0
SHEET 2 E 2 ARG B 649 ASP B 650 -1 O ARG B 649 N ILE B 623
SHEET 1 F 2 VAL B 632 VAL B 634 0
SHEET 2 F 2 MET B 640 ILE B 642 -1 O LYS B 641 N LEU B 633
LINK ND2 ASN A 631 MG MG A 803 1555 1555 2.28
LINK OD2 ASP A 644 MG MG A 803 1555 1555 2.25
LINK OD1 ASP A 644 MG MG A 804 1555 1555 2.43
LINK OD2 ASP A 644 MG MG A 804 1555 1555 2.42
LINK MG MG A 803 O1G ACP A 805 1555 1555 4.66
LINK MG MG A 803 O2A ACP A 805 1555 1555 4.40
LINK MG MG A 803 O1A ACP A 805 1555 1555 2.25
LINK MG MG A 803 O3G ACP A 805 1555 1555 2.38
LINK MG MG A 803 O HOH A 934 1555 1555 2.24
LINK MG MG A 803 O HOH A 946 1555 1555 2.45
LINK MG MG A 804 O2G ACP A 805 1555 1555 2.30
LINK MG MG A 804 O2B ACP A 805 1555 1555 4.49
LINK MG MG A 804 O1B ACP A 805 1555 1555 2.23
LINK MG MG A 804 O HOH A 922 1555 1555 2.26
LINK MG MG A 804 O HOH A 932 1555 1555 2.22
LINK ND2 ASN B 631 MG MG B 803 1555 1555 2.37
LINK OD2 ASP B 644 MG MG B 803 1555 1555 2.28
LINK OD1 ASP B 644 MG MG B 804 1555 1555 2.41
LINK OD2 ASP B 644 MG MG B 804 1555 1555 2.50
LINK MG MG B 803 O1G ACP B 805 1555 1555 3.53
LINK MG MG B 803 O2A ACP B 805 1555 1555 2.32
LINK MG MG B 803 O2G ACP B 805 1555 1555 2.26
LINK MG MG B 803 O HOH B 979 1555 1555 2.31
LINK MG MG B 803 O HOH B 988 1555 1555 2.37
LINK MG MG B 804 O2B ACP B 805 1555 1555 4.60
LINK MG MG B 804 O2G ACP B 805 1555 1555 3.95
LINK MG MG B 804 O1B ACP B 805 1555 1555 2.26
LINK MG MG B 804 O1G ACP B 805 1555 1555 2.29
LINK MG MG B 804 O HOH B 961 1555 1555 2.22
LINK MG MG B 804 O HOH B 980 1555 1555 2.32
SITE 1 AC1 6 LYS A 526 ARG A 625 ARG A 649 ARG A 664
SITE 2 AC1 6 HOH A 942 HOH A 974
SITE 1 AC2 3 ARG A 737 PRO B 744 SER B 745
SITE 1 AC3 5 ASN A 631 ASP A 644 ACP A 805 HOH A 934
SITE 2 AC3 5 HOH A 946
SITE 1 AC4 4 ASP A 644 ACP A 805 HOH A 922 HOH A 932
SITE 1 AC5 17 LEU A 487 VAL A 495 ALA A 515 LYS A 517
SITE 2 AC5 17 VAL A 564 GLY A 565 ALA A 567 ASN A 571
SITE 3 AC5 17 ARG A 630 ASN A 631 LEU A 633 ASP A 644
SITE 4 AC5 17 MG A 803 MG A 804 HOH A 911 HOH A 934
SITE 5 AC5 17 HOH A 943
SITE 1 AC6 6 ARG B 625 ARG B 649 ARG B 664 HOH B 906
SITE 2 AC6 6 HOH B 910 HOH B 927
SITE 1 AC7 2 THR B 729 ASN B 730
SITE 1 AC8 5 ASN B 631 ASP B 644 ACP B 805 HOH B 979
SITE 2 AC8 5 HOH B 988
SITE 1 AC9 4 ASP B 644 ACP B 805 HOH B 961 HOH B 980
SITE 1 BC1 18 GLY B 488 GLY B 493 ALA B 515 LYS B 517
SITE 2 BC1 18 VAL B 564 GLY B 565 TYR B 566 ALA B 567
SITE 3 BC1 18 ASN B 571 ARG B 630 ASN B 631 LEU B 633
SITE 4 BC1 18 ASP B 644 MG B 803 MG B 804 HOH B 978
SITE 5 BC1 18 HOH B 979 HOH B 988
CRYST1 104.897 114.748 64.440 90.00 90.00 90.00 P 21 21 2 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 0.009533 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008715 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015518 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
