HEADER TRANSFERASE 07-MAR-07 2P2I
TITLE CRYSTAL STRUCTURE OF THE VEGFR2 KINASE DOMAIN IN COMPLEX WITH A
TITLE 2 NICOTINAMIDE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: KINASE DOMAIN;
COMPND 5 SYNONYM: VEGFR-2, KINASE INSERT DOMAIN RECEPTOR, PROTEIN-TYROSINE
COMPND 6 KINASE RECEPTOR FLK-1, CD309 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: KDR, FLK1;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS RECEPTOR TYROSINE KINASE, KDR, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.WHITTINGTON,J.L.KIM,A.M.LONG,P.ROSE,Y.GU,H.ZHAO
REVDAT 5 21-FEB-24 2P2I 1 REMARK
REVDAT 4 20-OCT-21 2P2I 1 REMARK SEQADV
REVDAT 3 16-AUG-17 2P2I 1 SOURCE REMARK
REVDAT 2 24-FEB-09 2P2I 1 VERSN
REVDAT 1 20-MAR-07 2P2I 0
JRNL AUTH B.L.HODOUS,S.D.GEUNS-MEYER,P.E.HUGHES,B.K.ALBRECHT,S.BELLON,
JRNL AUTH 2 J.BREADY,S.CAENEPEEL,V.J.CEE,S.C.CHAFFEE,A.COXON,M.EMERY,
JRNL AUTH 3 J.FRETLAND,P.GALLANT,Y.GU,D.HOFFMAN,R.E.JOHNSON,R.KENDALL,
JRNL AUTH 4 J.L.KIM,A.M.LONG,M.MORRISON,P.R.OLIVIERI,V.F.PATEL,
JRNL AUTH 5 A.POLVERINO,P.ROSE,P.TEMPEST,L.WANG,D.A.WHITTINGTON,H.ZHAO
JRNL TITL EVOLUTION OF A HIGHLY SELECTIVE AND POTENT
JRNL TITL 2 2-(PYRIDIN-2-YL)-1,3,5-TRIAZINE TIE-2 KINASE INHIBITOR
JRNL REF J.MED.CHEM. V. 50 611 2007
JRNL REFN ISSN 0022-2623
JRNL PMID 17253678
JRNL DOI 10.1021/JM061107L
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.86
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1700177.875
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.8
REMARK 3 NUMBER OF REFLECTIONS : 23375
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) : 0.222
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1128
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3247
REMARK 3 BIN R VALUE (WORKING SET) : 0.3350
REMARK 3 BIN FREE R VALUE : 0.3230
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 149
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.026
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4337
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 122
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.69000
REMARK 3 B22 (A**2) : -3.25000
REMARK 3 B33 (A**2) : 11.94000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.11000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.56
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.38
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.46
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.390
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.821
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 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 : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 30.46
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 2P2I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000041884.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23837
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.41500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR 2.4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 33.53000
REMARK 290 SMTRY3 2 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 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 GLU A 815
REMARK 465 HIS A 816
REMARK 465 LYS A 858
REMARK 465 THR A 859
REMARK 465 ALA A 860
REMARK 465 LYS A 871
REMARK 465 GLU A 872
REMARK 465 GLY A 873
REMARK 465 ALA A 874
REMARK 465 ARG A 1051
REMARK 465 ASP A 1052
REMARK 465 ILE A 1053
REMARK 465 PTR A 1054
REMARK 465 LYS A 1055
REMARK 465 ASP A 1056
REMARK 465 PRO A 1057
REMARK 465 ASP A 1058
REMARK 465 PTR A 1059
REMARK 465 VAL A 1060
REMARK 465 ARG A 1061
REMARK 465 LYS A 1062
REMARK 465 GLY A 1063
REMARK 465 ASP A 1064
REMARK 465 ALA A 1065
REMARK 465 ARG A 1066
REMARK 465 GLU B 815
REMARK 465 HIS B 816
REMARK 465 ALA B 817
REMARK 465 GLU B 818
REMARK 465 ARG B 819
REMARK 465 ALA B 844
REMARK 465 PHE B 845
REMARK 465 GLY B 846
REMARK 465 LYS B 871
REMARK 465 GLU B 872
REMARK 465 GLY B 873
REMARK 465 ALA B 874
REMARK 465 VAL B 990
REMARK 465 ALA B 991
REMARK 465 PRO B 992
REMARK 465 GLU B 993
REMARK 465 ASP B 994
REMARK 465 LEU B 995
REMARK 465 TYR B 996
REMARK 465 LYS B 997
REMARK 465 ASP B 998
REMARK 465 GLY B 1048
REMARK 465 LEU B 1049
REMARK 465 ALA B 1050
REMARK 465 ARG B 1051
REMARK 465 ASP B 1052
REMARK 465 ILE B 1053
REMARK 465 PTR B 1054
REMARK 465 LYS B 1055
REMARK 465 ASP B 1056
REMARK 465 PRO B 1057
REMARK 465 ASP B 1058
REMARK 465 PTR B 1059
REMARK 465 VAL B 1060
REMARK 465 ARG B 1061
REMARK 465 LYS B 1062
REMARK 465 GLY B 1063
REMARK 465 ASP B 1064
REMARK 465 ALA B 1065
REMARK 465 ARG B 1066
REMARK 465 LEU B 1067
REMARK 465 GLN B 1169
REMARK 465 GLN B 1170
REMARK 465 ASP B 1171
REMARK 465 ARG B 1172
REMARK 465 HIS B 1173
REMARK 465 HIS B 1174
REMARK 465 HIS B 1175
REMARK 465 HIS B 1176
REMARK 465 HIS B 1177
REMARK 465 HIS B 1178
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 A1110 CG CD CE NZ
REMARK 470 ARG A1126 CG CD NE CZ NH1 NH2
REMARK 470 ARG A1172 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 835 CG CD CE NZ
REMARK 470 LYS B 838 CG CD CE NZ
REMARK 470 ARG B 842 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 858 CG CD CE NZ
REMARK 470 LYS B 920 CG CD CE NZ
REMARK 470 GLU B 934 CG CD OE1 OE2
REMARK 470 TYR B 938 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 939 CG CD CE NZ
REMARK 470 LYS B1023 CG CD CE NZ
REMARK 470 ARG B1032 CG CD NE CZ NH1 NH2
REMARK 470 LYS B1039 CG CD CE NZ
REMARK 470 LYS B1070 CG CD CE NZ
REMARK 470 PHE B1078 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B1080 CG CD NE CZ NH1 NH2
REMARK 470 LYS B1110 CG CD CE NZ
REMARK 470 GLU B1113 CG CD OE1 OE2
REMARK 470 GLU B1114 CG CD OE1 OE2
REMARK 470 ARG B1117 CG CD NE CZ NH1 NH2
REMARK 470 LYS B1120 CG CD CE NZ
REMARK 470 GLU B1121 CG CD OE1 OE2
REMARK 470 GLU B1158 CG CD OE1 OE2
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 934 50.58 -114.89
REMARK 500 GLU A 993 -8.62 -48.01
REMARK 500 ARG A1027 -15.16 77.98
REMARK 500 ASP A1028 40.25 -142.03
REMARK 500 SER A1037 -155.34 -104.37
REMARK 500 ASP A1046 112.99 -165.76
REMARK 500 ALA B 860 19.33 59.05
REMARK 500 HIS B 891 -72.73 -62.46
REMARK 500 ILE B 892 -38.00 -38.72
REMARK 500 GLU B 934 38.58 -146.02
REMARK 500 ARG B1027 -7.38 71.89
REMARK 500 ASP B1028 45.14 -145.00
REMARK 500 LYS B1039 34.43 70.63
REMARK 500 VAL B1081 -82.66 -62.04
REMARK 500 TYR B1082 82.24 92.46
REMARK 500 ASP B1112 -161.67 166.47
REMARK 500 GLU B1113 -69.99 -18.74
REMARK 500 ALA B1127 129.87 -33.54
REMARK 500 TRP B1143 34.99 -98.68
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 608 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 608 B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2P2H RELATED DB: PDB
DBREF 2P2I A 815 939 UNP P35968 VGFR2_HUMAN 815 939
DBREF 2P2I B 815 939 UNP P35968 VGFR2_HUMAN 815 939
DBREF 2P2I A 990 1171 UNP P35968 VGFR2_HUMAN 990 1171
DBREF 2P2I B 990 1171 UNP P35968 VGFR2_HUMAN 990 1171
SEQADV 2P2I ALA A 817 UNP P35968 CYS 817 ENGINEERED MUTATION
SEQADV 2P2I VAL A 990 UNP P35968 GLU 990 ENGINEERED MUTATION
SEQADV 2P2I ARG A 1172 UNP P35968 CLONING ARTIFACT
SEQADV 2P2I HIS A 1173 UNP P35968 EXPRESSION TAG
SEQADV 2P2I HIS A 1174 UNP P35968 EXPRESSION TAG
SEQADV 2P2I HIS A 1175 UNP P35968 EXPRESSION TAG
SEQADV 2P2I HIS A 1176 UNP P35968 EXPRESSION TAG
SEQADV 2P2I HIS A 1177 UNP P35968 EXPRESSION TAG
SEQADV 2P2I HIS A 1178 UNP P35968 EXPRESSION TAG
SEQADV 2P2I ALA B 817 UNP P35968 CYS 817 ENGINEERED MUTATION
SEQADV 2P2I VAL B 990 UNP P35968 GLU 990 ENGINEERED MUTATION
SEQADV 2P2I ARG B 1172 UNP P35968 CLONING ARTIFACT
SEQADV 2P2I HIS B 1173 UNP P35968 EXPRESSION TAG
SEQADV 2P2I HIS B 1174 UNP P35968 EXPRESSION TAG
SEQADV 2P2I HIS B 1175 UNP P35968 EXPRESSION TAG
SEQADV 2P2I HIS B 1176 UNP P35968 EXPRESSION TAG
SEQADV 2P2I HIS B 1177 UNP P35968 EXPRESSION TAG
SEQADV 2P2I HIS B 1178 UNP P35968 EXPRESSION TAG
SEQRES 1 A 314 GLU HIS ALA GLU ARG LEU PRO TYR ASP ALA SER LYS TRP
SEQRES 2 A 314 GLU PHE PRO ARG ASP ARG LEU LYS LEU GLY LYS PRO LEU
SEQRES 3 A 314 GLY ARG GLY ALA PHE GLY GLN VAL ILE GLU ALA ASP ALA
SEQRES 4 A 314 PHE GLY ILE ASP LYS THR ALA THR CYS ARG THR VAL ALA
SEQRES 5 A 314 VAL LYS MET LEU LYS GLU GLY ALA THR HIS SER GLU HIS
SEQRES 6 A 314 ARG ALA LEU MET SER GLU LEU LYS ILE LEU ILE HIS ILE
SEQRES 7 A 314 GLY HIS HIS LEU ASN VAL VAL ASN LEU LEU GLY ALA CYS
SEQRES 8 A 314 THR LYS PRO GLY GLY PRO LEU MET VAL ILE VAL GLU PHE
SEQRES 9 A 314 CYS LYS PHE GLY ASN LEU SER THR TYR LEU ARG SER LYS
SEQRES 10 A 314 ARG ASN GLU PHE VAL PRO TYR LYS VAL ALA PRO GLU ASP
SEQRES 11 A 314 LEU TYR LYS ASP PHE LEU THR LEU GLU HIS LEU ILE CYS
SEQRES 12 A 314 TYR SER PHE GLN VAL ALA LYS GLY MET GLU PHE LEU ALA
SEQRES 13 A 314 SER ARG LYS CYS ILE HIS ARG ASP LEU ALA ALA ARG ASN
SEQRES 14 A 314 ILE LEU LEU SER GLU LYS ASN VAL VAL LYS ILE CYS ASP
SEQRES 15 A 314 PHE GLY LEU ALA ARG ASP ILE PTR LYS ASP PRO ASP PTR
SEQRES 16 A 314 VAL ARG LYS GLY ASP ALA ARG LEU PRO LEU LYS TRP MET
SEQRES 17 A 314 ALA PRO GLU THR ILE PHE ASP ARG VAL TYR THR ILE GLN
SEQRES 18 A 314 SER ASP VAL TRP SER PHE GLY VAL LEU LEU TRP GLU ILE
SEQRES 19 A 314 PHE SER LEU GLY ALA SER PRO TYR PRO GLY VAL LYS ILE
SEQRES 20 A 314 ASP GLU GLU PHE CYS ARG ARG LEU LYS GLU GLY THR ARG
SEQRES 21 A 314 MET ARG ALA PRO ASP TYR THR THR PRO GLU MET TYR GLN
SEQRES 22 A 314 THR MET LEU ASP CYS TRP HIS GLY GLU PRO SER GLN ARG
SEQRES 23 A 314 PRO THR PHE SER GLU LEU VAL GLU HIS LEU GLY ASN LEU
SEQRES 24 A 314 LEU GLN ALA ASN ALA GLN GLN ASP ARG HIS HIS HIS HIS
SEQRES 25 A 314 HIS HIS
SEQRES 1 B 314 GLU HIS ALA GLU ARG LEU PRO TYR ASP ALA SER LYS TRP
SEQRES 2 B 314 GLU PHE PRO ARG ASP ARG LEU LYS LEU GLY LYS PRO LEU
SEQRES 3 B 314 GLY ARG GLY ALA PHE GLY GLN VAL ILE GLU ALA ASP ALA
SEQRES 4 B 314 PHE GLY ILE ASP LYS THR ALA THR CYS ARG THR VAL ALA
SEQRES 5 B 314 VAL LYS MET LEU LYS GLU GLY ALA THR HIS SER GLU HIS
SEQRES 6 B 314 ARG ALA LEU MET SER GLU LEU LYS ILE LEU ILE HIS ILE
SEQRES 7 B 314 GLY HIS HIS LEU ASN VAL VAL ASN LEU LEU GLY ALA CYS
SEQRES 8 B 314 THR LYS PRO GLY GLY PRO LEU MET VAL ILE VAL GLU PHE
SEQRES 9 B 314 CYS LYS PHE GLY ASN LEU SER THR TYR LEU ARG SER LYS
SEQRES 10 B 314 ARG ASN GLU PHE VAL PRO TYR LYS VAL ALA PRO GLU ASP
SEQRES 11 B 314 LEU TYR LYS ASP PHE LEU THR LEU GLU HIS LEU ILE CYS
SEQRES 12 B 314 TYR SER PHE GLN VAL ALA LYS GLY MET GLU PHE LEU ALA
SEQRES 13 B 314 SER ARG LYS CYS ILE HIS ARG ASP LEU ALA ALA ARG ASN
SEQRES 14 B 314 ILE LEU LEU SER GLU LYS ASN VAL VAL LYS ILE CYS ASP
SEQRES 15 B 314 PHE GLY LEU ALA ARG ASP ILE PTR LYS ASP PRO ASP PTR
SEQRES 16 B 314 VAL ARG LYS GLY ASP ALA ARG LEU PRO LEU LYS TRP MET
SEQRES 17 B 314 ALA PRO GLU THR ILE PHE ASP ARG VAL TYR THR ILE GLN
SEQRES 18 B 314 SER ASP VAL TRP SER PHE GLY VAL LEU LEU TRP GLU ILE
SEQRES 19 B 314 PHE SER LEU GLY ALA SER PRO TYR PRO GLY VAL LYS ILE
SEQRES 20 B 314 ASP GLU GLU PHE CYS ARG ARG LEU LYS GLU GLY THR ARG
SEQRES 21 B 314 MET ARG ALA PRO ASP TYR THR THR PRO GLU MET TYR GLN
SEQRES 22 B 314 THR MET LEU ASP CYS TRP HIS GLY GLU PRO SER GLN ARG
SEQRES 23 B 314 PRO THR PHE SER GLU LEU VAL GLU HIS LEU GLY ASN LEU
SEQRES 24 B 314 LEU GLN ALA ASN ALA GLN GLN ASP ARG HIS HIS HIS HIS
SEQRES 25 B 314 HIS HIS
HET 608 A 501 30
HET 608 B 502 30
HETNAM 608 N-(4-PHENOXYPHENYL)-2-[(PYRIDIN-4-YLMETHYL)
HETNAM 2 608 AMINO]NICOTINAMIDE
FORMUL 3 608 2(C24 H20 N4 O2)
FORMUL 5 HOH *122(H2 O)
HELIX 1 1 ASP A 823 GLU A 828 1 6
HELIX 2 2 PRO A 830 ASP A 832 5 3
HELIX 3 3 THR A 875 GLY A 893 1 19
HELIX 4 4 ASN A 923 LYS A 931 1 9
HELIX 5 5 PRO A 992 LYS A 997 5 6
HELIX 6 6 THR A 1001 ARG A 1022 1 22
HELIX 7 7 ALA A 1030 ARG A 1032 5 3
HELIX 8 8 ALA A 1073 ASP A 1079 1 7
HELIX 9 9 THR A 1083 PHE A 1099 1 17
HELIX 10 10 ASP A 1112 GLY A 1122 1 11
HELIX 11 11 THR A 1132 TRP A 1143 1 12
HELIX 12 12 GLU A 1146 ARG A 1150 5 5
HELIX 13 13 THR A 1152 HIS A 1178 1 27
HELIX 14 14 ASP B 823 GLU B 828 1 6
HELIX 15 15 PRO B 830 ASP B 832 5 3
HELIX 16 16 THR B 875 ILE B 892 1 18
HELIX 17 17 ASN B 923 SER B 930 1 8
HELIX 18 18 LYS B 931 PHE B 935 5 5
HELIX 19 19 THR B 1001 SER B 1021 1 21
HELIX 20 20 ALA B 1030 ARG B 1032 5 3
HELIX 21 21 PRO B 1068 MET B 1072 5 5
HELIX 22 22 ALA B 1073 ASP B 1079 1 7
HELIX 23 23 THR B 1083 PHE B 1099 1 17
HELIX 24 24 ASP B 1112 GLY B 1122 1 11
HELIX 25 25 THR B 1132 TRP B 1143 1 12
HELIX 26 26 GLU B 1146 ARG B 1150 5 5
HELIX 27 27 THR B 1152 ALA B 1168 1 17
SHEET 1 A 5 LEU A 834 ARG A 842 0
SHEET 2 A 5 GLN A 847 PHE A 854 -1 O VAL A 848 N LEU A 840
SHEET 3 A 5 CYS A 862 MET A 869 -1 O VAL A 867 N ILE A 849
SHEET 4 A 5 MET A 913 GLU A 917 -1 O VAL A 914 N LYS A 868
SHEET 5 A 5 LEU A 901 CYS A 905 -1 N LEU A 902 O ILE A 915
SHEET 1 B 2 ILE A1034 LEU A1036 0
SHEET 2 B 2 VAL A1042 ILE A1044 -1 O LYS A1043 N LEU A1035
SHEET 1 C 5 LEU B 834 GLY B 841 0
SHEET 2 C 5 VAL B 848 PHE B 854 -1 O VAL B 848 N LEU B 840
SHEET 3 C 5 CYS B 862 LYS B 868 -1 O VAL B 865 N ALA B 851
SHEET 4 C 5 MET B 913 GLU B 917 -1 O VAL B 916 N ALA B 866
SHEET 5 C 5 LEU B 901 CYS B 905 -1 N LEU B 902 O ILE B 915
SHEET 1 D 2 ILE B1034 SER B1037 0
SHEET 2 D 2 VAL B1041 ILE B1044 -1 O LYS B1043 N LEU B1035
CISPEP 1 ALA A 991 PRO A 992 0 -0.26
SITE 1 AC1 16 LEU A 840 VAL A 848 ALA A 866 LYS A 868
SITE 2 AC1 16 GLU A 885 ILE A 888 ILE A 892 VAL A 914
SITE 3 AC1 16 GLU A 917 CYS A 919 CYS A1024 ILE A1025
SITE 4 AC1 16 LEU A1035 CYS A1045 ASP A1046 PHE A1047
SITE 1 AC2 16 LEU B 840 VAL B 848 ALA B 866 LYS B 868
SITE 2 AC2 16 GLU B 885 ILE B 888 VAL B 899 VAL B 916
SITE 3 AC2 16 GLU B 917 CYS B 919 CYS B1024 ILE B1025
SITE 4 AC2 16 HIS B1026 LEU B1035 CYS B1045 ASP B1046
CRYST1 55.420 67.060 88.510 90.00 94.51 90.00 P 1 21 1 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 0.018000 0.000000 0.001400 0.00000
SCALE2 0.000000 0.014900 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011300 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
