HEADER TRANSFERASE 09-JAN-17 5UGL
TITLE CRYSTAL STRUCTURE OF FGF RECEPTOR 2 TYROSINE KINASE DOMAIN HARBORING
TITLE 2 THE D650V ACTIVATING MUTATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBROBLAST GROWTH FACTOR RECEPTOR 2;
COMPND 3 CHAIN: B, A;
COMPND 4 FRAGMENT: UNP RESIDUES 341-651;
COMPND 5 SYNONYM: FGFR-2,K-SAM,KGFR,KERATINOCYTE GROWTH FACTOR RECEPTOR;
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: FGFR2, BEK, KGFR, KSAM;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TYROSINE KINASE DOMAIN, ATP ANALOGE, GAIN-OF-FUNCTION MUTATION,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MOHAMMADI,H.CHEN
REVDAT 4 04-OCT-23 5UGL 1 REMARK
REVDAT 3 11-DEC-19 5UGL 1 REMARK
REVDAT 2 27-SEP-17 5UGL 1 REMARK
REVDAT 1 22-FEB-17 5UGL 0
JRNL AUTH H.CHEN,W.M.MARSIGLIA,M.K.CHO,Z.HUANG,J.DENG,S.P.BLAIS,W.GAI,
JRNL AUTH 2 S.BHATTACHARYA,T.A.NEUBERT,N.J.TRAASETH,M.MOHAMMADI
JRNL TITL ELUCIDATION OF A FOUR-SITE ALLOSTERIC NETWORK IN FIBROBLAST
JRNL TITL 2 GROWTH FACTOR RECEPTOR TYROSINE KINASES.
JRNL REF ELIFE V. 6 2017
JRNL REFN ESSN 2050-084X
JRNL PMID 28166054
JRNL DOI 10.7554/ELIFE.21137
REMARK 2
REMARK 2 RESOLUTION. 1.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.84
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.9
REMARK 3 NUMBER OF REFLECTIONS : 46258
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.320
REMARK 3 FREE R VALUE TEST SET COUNT : 1998
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 34.8487 - 4.4820 0.97 3699 167 0.2038 0.2329
REMARK 3 2 4.4820 - 3.5586 0.66 2422 110 0.1803 0.2232
REMARK 3 3 3.5586 - 3.1091 0.99 3586 161 0.2165 0.2489
REMARK 3 4 3.1091 - 2.8250 1.00 3594 162 0.2256 0.2406
REMARK 3 5 2.8250 - 2.6226 1.00 3610 163 0.2276 0.2804
REMARK 3 6 2.6226 - 2.4680 1.00 3574 161 0.2216 0.2607
REMARK 3 7 2.4680 - 2.3444 1.00 3583 162 0.2160 0.2692
REMARK 3 8 2.3444 - 2.2424 0.93 2273 103 0.2265 0.2688
REMARK 3 9 2.2424 - 2.1561 0.94 2574 114 0.2206 0.2903
REMARK 3 10 2.1561 - 2.0817 1.00 3544 161 0.2212 0.2571
REMARK 3 11 2.0817 - 2.0166 1.00 3563 161 0.2141 0.2658
REMARK 3 12 2.0166 - 1.9590 1.00 3541 159 0.2229 0.2381
REMARK 3 13 1.9590 - 1.9074 0.62 2043 95 0.3565 0.4508
REMARK 3 14 1.9074 - 1.8609 0.86 2654 119 0.3288 0.3704
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.240
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) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 4622
REMARK 3 ANGLE : 0.882 6268
REMARK 3 CHIRALITY : 0.055 690
REMARK 3 PLANARITY : 0.006 789
REMARK 3 DIHEDRAL : 15.724 2816
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN 'B' AND RESID 468 THROUGH 764)
REMARK 3 ORIGIN FOR THE GROUP (A): 49.3638 36.1728 10.3898
REMARK 3 T TENSOR
REMARK 3 T11: 0.0601 T22: 0.1880
REMARK 3 T33: 0.0882 T12: 0.0556
REMARK 3 T13: 0.0239 T23: 0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 0.6559 L22: 0.3591
REMARK 3 L33: 0.1499 L12: -0.0958
REMARK 3 L13: 0.0391 L23: 0.0225
REMARK 3 S TENSOR
REMARK 3 S11: 0.1036 S12: 0.6634 S13: 0.0535
REMARK 3 S21: 0.0485 S22: -0.1364 S23: -0.0406
REMARK 3 S31: 0.0663 S32: 0.0745 S33: -0.0518
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN 'A' AND RESID 468 THROUGH 764)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2907 35.1856 24.7515
REMARK 3 T TENSOR
REMARK 3 T11: 0.1018 T22: 0.0792
REMARK 3 T33: 0.1042 T12: 0.0058
REMARK 3 T13: 0.0050 T23: -0.0159
REMARK 3 L TENSOR
REMARK 3 L11: 0.3867 L22: 0.1849
REMARK 3 L33: 0.1986 L12: 0.0702
REMARK 3 L13: 0.1294 L23: -0.0040
REMARK 3 S TENSOR
REMARK 3 S11: 0.0032 S12: -0.0107 S13: 0.0333
REMARK 3 S21: -0.0053 S22: -0.0528 S23: 0.0120
REMARK 3 S31: -0.0323 S32: -0.1120 S33: -0.0127
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5UGL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1000225807.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUL-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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) : 0.97912
REMARK 200 MONOCHROMATOR : NULL
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 : 46452
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860
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 (%) : 87.9
REMARK 200 DATA REDUNDANCY : 14.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 75.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 57.6
REMARK 200 DATA REDUNDANCY IN SHELL : 11.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.18200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 17.30
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 2PSQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25 MM HEPES PH7.5, 15%-25% W/V
REMARK 280 PEG4000, 0.2-0.3 M NH4SO3, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 33.60750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.27200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.39300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.27200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.60750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.39300
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 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 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 PRO B 582
REMARK 465 GLY B 583
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 595
REMARK 465 GLU B 596
REMARK 465 GLN B 597
REMARK 465 ASN B 652
REMARK 465 ASN B 653
REMARK 465 ILE B 654
REMARK 465 ASP B 655
REMARK 465 TYR B 656
REMARK 465 TYR B 657
REMARK 465 LYS B 658
REMARK 465 LYS B 659
REMARK 465 THR B 660
REMARK 465 THR B 661
REMARK 465 ASN B 662
REMARK 465 THR B 765
REMARK 465 ASN B 766
REMARK 465 GLU B 767
REMARK 465 GLU B 768
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 PRO A 581
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 THR A 765
REMARK 465 ASN A 766
REMARK 465 GLU A 767
REMARK 465 GLU A 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 B 507 CG CD CE NZ
REMARK 470 LYS B 621 CG CD CE NZ
REMARK 470 ARG B 678 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 509 CG CD CE NZ
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 O HOH A 954 O HOH A 989 1.96
REMARK 500 OD2 ASP A 644 O1G ANP A 802 2.07
REMARK 500 OD1 ASP A 644 O HOH A 901 2.13
REMARK 500 O HOH A 943 O HOH A 989 2.17
REMARK 500 O PRO B 508 O HOH B 901 2.17
REMARK 500 OH TYR B 561 O HOH B 902 2.17
REMARK 500 O HOH A 970 O HOH A 989 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD1 ASP B 506 NH1 ARG A 612 1655 2.05
REMARK 500 O HOH B 918 O HOH A 978 1655 2.07
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 ARG B 625 -7.57 75.49
REMARK 500 ARG A 625 -6.81 75.23
REMARK 500 ASP A 644 66.42 60.75
REMARK 500 ASP A 644 65.40 61.82
REMARK 500 ASN A 652 -120.17 -95.93
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 B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP A 802
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5UI0 RELATED DB: PDB
REMARK 900 RELATED ID: 5UGX RELATED DB: PDB
REMARK 900 RELATED ID: 5UHN RELATED DB: PDB
DBREF 5UGL B 458 768 UNP P21802 FGFR2_HUMAN 341 651
DBREF 5UGL A 458 768 UNP P21802 FGFR2_HUMAN 341 651
SEQADV 5UGL MET B 445 UNP P21802 INITIATING METHIONINE
SEQADV 5UGL GLY B 446 UNP P21802 EXPRESSION TAG
SEQADV 5UGL SER B 447 UNP P21802 EXPRESSION TAG
SEQADV 5UGL SER B 448 UNP P21802 EXPRESSION TAG
SEQADV 5UGL HIS B 449 UNP P21802 EXPRESSION TAG
SEQADV 5UGL HIS B 450 UNP P21802 EXPRESSION TAG
SEQADV 5UGL HIS B 451 UNP P21802 EXPRESSION TAG
SEQADV 5UGL HIS B 452 UNP P21802 EXPRESSION TAG
SEQADV 5UGL HIS B 453 UNP P21802 EXPRESSION TAG
SEQADV 5UGL HIS B 454 UNP P21802 EXPRESSION TAG
SEQADV 5UGL SER B 455 UNP P21802 EXPRESSION TAG
SEQADV 5UGL GLN B 456 UNP P21802 EXPRESSION TAG
SEQADV 5UGL ASP B 457 UNP P21802 EXPRESSION TAG
SEQADV 5UGL ALA B 491 UNP P21802 CYS 374 CONFLICT
SEQADV 5UGL VAL B 650 UNP P21802 ASP 533 ENGINEERED MUTATION
SEQADV 5UGL MET A 445 UNP P21802 INITIATING METHIONINE
SEQADV 5UGL GLY A 446 UNP P21802 EXPRESSION TAG
SEQADV 5UGL SER A 447 UNP P21802 EXPRESSION TAG
SEQADV 5UGL SER A 448 UNP P21802 EXPRESSION TAG
SEQADV 5UGL HIS A 449 UNP P21802 EXPRESSION TAG
SEQADV 5UGL HIS A 450 UNP P21802 EXPRESSION TAG
SEQADV 5UGL HIS A 451 UNP P21802 EXPRESSION TAG
SEQADV 5UGL HIS A 452 UNP P21802 EXPRESSION TAG
SEQADV 5UGL HIS A 453 UNP P21802 EXPRESSION TAG
SEQADV 5UGL HIS A 454 UNP P21802 EXPRESSION TAG
SEQADV 5UGL SER A 455 UNP P21802 EXPRESSION TAG
SEQADV 5UGL GLN A 456 UNP P21802 EXPRESSION TAG
SEQADV 5UGL ASP A 457 UNP P21802 EXPRESSION TAG
SEQADV 5UGL ALA A 491 UNP P21802 CYS 374 CONFLICT
SEQADV 5UGL VAL A 650 UNP P21802 ASP 533 ENGINEERED MUTATION
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 GLU 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 VAL 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
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 GLU 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 VAL 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
HET SO4 B 801 5
HET ANP B 802 31
HET SO4 A 801 5
HET ANP A 802 31
HETNAM SO4 SULFATE ION
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 ANP 2(C10 H17 N6 O12 P3)
FORMUL 7 HOH *182(H2 O)
HELIX 1 AA1 PRO B 477 ASP B 479 5 3
HELIX 2 AA2 THR B 524 ILE B 541 1 18
HELIX 3 AA3 ASN B 571 ALA B 578 1 8
HELIX 4 AA4 THR B 599 GLN B 620 1 22
HELIX 5 AA5 ALA B 628 ARG B 630 5 3
HELIX 6 AA6 ASP B 644 ALA B 648 5 5
HELIX 7 AA7 PRO B 666 MET B 670 5 5
HELIX 8 AA8 ALA B 671 ARG B 678 1 8
HELIX 9 AA9 THR B 681 THR B 698 1 18
HELIX 10 AB1 PRO B 708 GLU B 718 1 11
HELIX 11 AB2 THR B 729 TRP B 740 1 12
HELIX 12 AB3 VAL B 743 ARG B 747 5 5
HELIX 13 AB4 THR B 749 LEU B 763 1 15
HELIX 14 AB5 PRO A 477 ASP A 479 5 3
HELIX 15 AB6 THR A 524 ILE A 541 1 18
HELIX 16 AB7 ASN A 571 ALA A 578 1 8
HELIX 17 AB8 THR A 599 GLN A 620 1 22
HELIX 18 AB9 ALA A 628 ARG A 630 5 3
HELIX 19 AC1 ASP A 644 ALA A 648 5 5
HELIX 20 AC2 PRO A 666 MET A 670 5 5
HELIX 21 AC3 ALA A 671 ARG A 678 1 8
HELIX 22 AC4 THR A 681 THR A 698 1 18
HELIX 23 AC5 PRO A 708 GLU A 718 1 11
HELIX 24 AC6 THR A 729 TRP A 740 1 12
HELIX 25 AC7 VAL A 743 ARG A 747 5 5
HELIX 26 AC8 THR A 749 LEU A 763 1 15
SHEET 1 AA1 5 LEU B 481 GLU B 489 0
SHEET 2 AA1 5 GLN B 494 VAL B 501 -1 O MET B 497 N GLY B 484
SHEET 3 AA1 5 ALA B 511 MET B 518 -1 O VAL B 514 N ALA B 498
SHEET 4 AA1 5 TYR B 561 GLU B 565 -1 O VAL B 562 N LYS B 517
SHEET 5 AA1 5 LEU B 550 CYS B 554 -1 N LEU B 551 O ILE B 563
SHEET 1 AA2 2 CYS B 622 ILE B 623 0
SHEET 2 AA2 2 ARG B 649 VAL B 650 -1 O ARG B 649 N ILE B 623
SHEET 1 AA3 2 VAL B 632 VAL B 634 0
SHEET 2 AA3 2 MET B 640 ILE B 642 -1 O LYS B 641 N LEU B 633
SHEET 1 AA4 5 LEU A 481 GLU A 489 0
SHEET 2 AA4 5 GLN A 494 VAL A 501 -1 O MET A 497 N GLY A 484
SHEET 3 AA4 5 ALA A 511 MET A 518 -1 O VAL A 514 N ALA A 498
SHEET 4 AA4 5 TYR A 561 GLU A 565 -1 O VAL A 564 N ALA A 515
SHEET 5 AA4 5 LEU A 550 CYS A 554 -1 N LEU A 551 O ILE A 563
SHEET 1 AA5 2 CYS A 622 ILE A 623 0
SHEET 2 AA5 2 ARG A 649 VAL A 650 -1 O ARG A 649 N ILE A 623
SHEET 1 AA6 2 VAL A 632 VAL A 634 0
SHEET 2 AA6 2 MET A 640 ILE A 642 -1 O LYS A 641 N LEU A 633
SHEET 1 AA7 2 TYR A 656 TYR A 657 0
SHEET 2 AA7 2 VAL A 679 TYR A 680 -1 O TYR A 680 N TYR A 656
SITE 1 AC1 4 ARG B 625 ARG B 649 ARG B 664 TYR B 680
SITE 1 AC2 14 LEU B 487 GLY B 488 VAL B 495 ALA B 515
SITE 2 AC2 14 VAL B 564 GLU B 565 ALA B 567 ASN B 571
SITE 3 AC2 14 ARG B 630 ASN B 631 LEU B 633 ASP B 644
SITE 4 AC2 14 HOH B 955 HOH B 978
SITE 1 AC3 5 ARG A 625 ARG A 649 TYR A 656 THR A 660
SITE 2 AC3 5 ARG A 664
SITE 1 AC4 15 LEU A 487 GLY A 488 VAL A 495 ALA A 515
SITE 2 AC4 15 LYS A 517 VAL A 564 GLU A 565 ALA A 567
SITE 3 AC4 15 ARG A 630 ASN A 631 LEU A 633 ASP A 644
SITE 4 AC4 15 HOH A 903 HOH A 954 HOH A 970
CRYST1 67.215 78.786 116.544 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014878 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012693 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008580 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
