HEADER TRANSFERASE 26-FEB-08 3CCN
TITLE X-RAY STRUCTURE OF C-MET WITH TRIAZOLOPYRIDAZINE INHIBITOR.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEPATOCYTE GROWTH FACTOR RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PROTEIN KINASE DOMAIN,C-MET KINASE DOMAIN;
COMPND 5 SYNONYM: HGF RECEPTOR, SCATTER FACTOR RECEPTOR, SF RECEPTOR, HGF/SF
COMPND 6 RECEPTOR, MET PROTO-ONCOGENE TYROSINE KINASE, C-MET;
COMPND 7 EC: 2.7.10.1;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MET;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS C-MET KINASE TRIAZOLOPYRIDAZINE, ATP-BINDING, GLYCOPROTEIN, MEMBRANE,
KEYWDS 2 NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, PROTO-ONCOGENE, RECEPTOR,
KEYWDS 3 TRANSFERASE, TRANSMEMBRANE, TYROSINE-PROTEIN KINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.K.ABRECHT,J.-C.HARMANGE,D.BAUER,I.DUSSAULT,A.LONG,S.F.BELLON
REVDAT 4 30-AUG-23 3CCN 1 REMARK SEQADV
REVDAT 3 24-FEB-09 3CCN 1 VERSN
REVDAT 2 27-MAY-08 3CCN 1 JRNL
REVDAT 1 29-APR-08 3CCN 0
JRNL AUTH B.K.ALBRECHT,J.C.HARMANGE,D.BAUER,L.BERRY,C.BODE,A.A.BOEZIO,
JRNL AUTH 2 A.CHEN,D.CHOQUETTE,I.DUSSAULT,C.FRIDRICH,S.HIRAI,D.HOFFMAN,
JRNL AUTH 3 J.F.LARROW,P.KAPLAN-LEFKO,J.LIN,J.LOHMAN,A.M.LONG,
JRNL AUTH 4 J.MORIGUCHI,A.O'CONNOR,M.H.POTASHMAN,M.REESE,K.REX,
JRNL AUTH 5 A.SIEGMUND,K.SHAH,R.SHIMANOVICH,S.K.SPRINGER,Y.TEFFERA,
JRNL AUTH 6 Y.YANG,Y.ZHANG,S.F.BELLON
JRNL TITL DISCOVERY AND OPTIMIZATION OF TRIAZOLOPYRIDAZINES AS POTENT
JRNL TITL 2 AND SELECTIVE INHIBITORS OF THE C-MET KINASE.
JRNL REF J.MED.CHEM. V. 51 2879 2008
JRNL REFN ISSN 0022-2623
JRNL PMID 18426196
JRNL DOI 10.1021/JM800043G
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 3 NUMBER OF REFLECTIONS : 20714
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) : 0.238
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1089
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1291
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.31
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE SET COUNT : 71
REMARK 3 BIN FREE R VALUE : 0.3680
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2148
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 177
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.42000
REMARK 3 B22 (A**2) : 0.76000
REMARK 3 B33 (A**2) : -1.19000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.213
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.184
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.114
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.740
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.919
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.896
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2229 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3023 ; 1.057 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 270 ; 4.878 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 87 ;31.456 ;23.333
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 364 ;12.841 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;14.232 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 340 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1654 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1013 ; 0.172 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1498 ; 0.302 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 144 ; 0.116 ; 0.200
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): 36 ; 0.160 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.102 ; 0.200
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): 1417 ; 0.601 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2204 ; 0.999 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 952 ; 1.144 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 819 ; 1.676 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3CCN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-FEB-08.
REMARK 100 THE DEPOSITION ID IS D_1000046615.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 130
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NONE
REMARK 200 OPTICS : VARIMAX OPTICS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21891
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.17000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.500
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: 2RFN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.8, 15% PEG 4K, 6% 2
REMARK 280 -PROPANOL, 40MM BME, AND 3% ETHANOL., VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 298K
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 21.02900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.91350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.72000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.91350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.02900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 21.72000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1047
REMARK 465 GLN A 1048
REMARK 465 ASN A 1049
REMARK 465 THR A 1050
REMARK 465 VAL A 1051
REMARK 465 HIS A 1052
REMARK 465 ILE A 1053
REMARK 465 ASP A 1054
REMARK 465 LEU A 1098
REMARK 465 ASP A 1099
REMARK 465 ASN A 1100
REMARK 465 ASP A 1101
REMARK 465 GLY A 1102
REMARK 465 LYS A 1103
REMARK 465 ILE A 1115
REMARK 465 THR A 1116
REMARK 465 ASP A 1117
REMARK 465 ILE A 1118
REMARK 465 GLY A 1119
REMARK 465 ARG A 1148
REMARK 465 SER A 1149
REMARK 465 GLU A 1150
REMARK 465 GLY A 1151
REMARK 465 SER A 1152
REMARK 465 ASN A 1239
REMARK 465 GLU A 1347
REMARK 465 HIS A 1348
REMARK 465 TYR A 1349
REMARK 465 VAL A 1350
REMARK 465 HIS A 1351
REMARK 465 HIS A 1352
REMARK 465 HIS A 1353
REMARK 465 HIS A 1354
REMARK 465 HIS A 1355
REMARK 465 HIS A 1356
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 LEU A1058 CG CD1 CD2
REMARK 470 GLU A1061 CG CD OE1 OE2
REMARK 470 GLN A1064 CG CD OE1 NE2
REMARK 470 ARG A1086 CG CD NE CZ NH1 NH2
REMARK 470 ASN A1113 CG OD1 ND2
REMARK 470 ARG A1114 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1120 CG CD OE1 OE2
REMARK 470 ARG A1227 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1232 CG CD CE NZ
REMARK 470 LYS A1240 CG CD CE NZ
REMARK 470 THR A1241 OG1 CG2
REMARK 470 LYS A1259 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 PRO A1060 -114.46 -68.62
REMARK 500 ASN A1113 -63.74 -151.78
REMARK 500 ARG A1203 -21.52 80.65
REMARK 500 ASP A1204 42.31 -143.69
REMARK 500 ALA A1221 -153.22 -129.45
REMARK 500 THR A1289 -120.11 45.52
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 LKG A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3CD8 RELATED DB: PDB
DBREF 3CCN A 1048 1350 UNP P08581 MET_HUMAN 1048 1350
SEQADV 3CCN MET A 1047 UNP P08581 INITIATING METHIONINE
SEQADV 3CCN LEU A 1272 UNP P08581 VAL 1272 VARIANT
SEQADV 3CCN HIS A 1351 UNP P08581 EXPRESSION TAG
SEQADV 3CCN HIS A 1352 UNP P08581 EXPRESSION TAG
SEQADV 3CCN HIS A 1353 UNP P08581 EXPRESSION TAG
SEQADV 3CCN HIS A 1354 UNP P08581 EXPRESSION TAG
SEQADV 3CCN HIS A 1355 UNP P08581 EXPRESSION TAG
SEQADV 3CCN HIS A 1356 UNP P08581 EXPRESSION TAG
SEQRES 1 A 310 MET GLN ASN THR VAL HIS ILE ASP LEU SER ALA LEU ASN
SEQRES 2 A 310 PRO GLU LEU VAL GLN ALA VAL GLN HIS VAL VAL ILE GLY
SEQRES 3 A 310 PRO SER SER LEU ILE VAL HIS PHE ASN GLU VAL ILE GLY
SEQRES 4 A 310 ARG GLY HIS PHE GLY CYS VAL TYR HIS GLY THR LEU LEU
SEQRES 5 A 310 ASP ASN ASP GLY LYS LYS ILE HIS CYS ALA VAL LYS SER
SEQRES 6 A 310 LEU ASN ARG ILE THR ASP ILE GLY GLU VAL SER GLN PHE
SEQRES 7 A 310 LEU THR GLU GLY ILE ILE MET LYS ASP PHE SER HIS PRO
SEQRES 8 A 310 ASN VAL LEU SER LEU LEU GLY ILE CYS LEU ARG SER GLU
SEQRES 9 A 310 GLY SER PRO LEU VAL VAL LEU PRO TYR MET LYS HIS GLY
SEQRES 10 A 310 ASP LEU ARG ASN PHE ILE ARG ASN GLU THR HIS ASN PRO
SEQRES 11 A 310 THR VAL LYS ASP LEU ILE GLY PHE GLY LEU GLN VAL ALA
SEQRES 12 A 310 LYS GLY MET LYS TYR LEU ALA SER LYS LYS PHE VAL HIS
SEQRES 13 A 310 ARG ASP LEU ALA ALA ARG ASN CYS MET LEU ASP GLU LYS
SEQRES 14 A 310 PHE THR VAL LYS VAL ALA ASP PHE GLY LEU ALA ARG ASP
SEQRES 15 A 310 MET TYR ASP LYS GLU TYR TYR SER VAL HIS ASN LYS THR
SEQRES 16 A 310 GLY ALA LYS LEU PRO VAL LYS TRP MET ALA LEU GLU SER
SEQRES 17 A 310 LEU GLN THR GLN LYS PHE THR THR LYS SER ASP VAL TRP
SEQRES 18 A 310 SER PHE GLY VAL LEU LEU TRP GLU LEU MET THR ARG GLY
SEQRES 19 A 310 ALA PRO PRO TYR PRO ASP VAL ASN THR PHE ASP ILE THR
SEQRES 20 A 310 VAL TYR LEU LEU GLN GLY ARG ARG LEU LEU GLN PRO GLU
SEQRES 21 A 310 TYR CYS PRO ASP PRO LEU TYR GLU VAL MET LEU LYS CYS
SEQRES 22 A 310 TRP HIS PRO LYS ALA GLU MET ARG PRO SER PHE SER GLU
SEQRES 23 A 310 LEU VAL SER ARG ILE SER ALA ILE PHE SER THR PHE ILE
SEQRES 24 A 310 GLY GLU HIS TYR VAL HIS HIS HIS HIS HIS HIS
HET LKG A 1 23
HETNAM LKG 4-[(6-PHENYL[1,2,4]TRIAZOLO[4,3-B]PYRIDAZIN-3-YL)
HETNAM 2 LKG METHYL]PHENOL
FORMUL 2 LKG C18 H14 N4 O
FORMUL 3 HOH *177(H2 O)
HELIX 1 1 LEU A 1062 GLN A 1064 5 3
HELIX 2 2 ALA A 1065 VAL A 1069 1 5
HELIX 3 3 GLU A 1120 ASP A 1133 1 14
HELIX 4 4 ASP A 1164 ASN A 1171 1 8
HELIX 5 5 THR A 1177 LYS A 1198 1 22
HELIX 6 6 ALA A 1206 ARG A 1208 5 3
HELIX 7 7 PHE A 1223 ARG A 1227 5 5
HELIX 8 8 ASP A 1231 TYR A 1235 5 5
HELIX 9 9 PRO A 1246 MET A 1250 5 5
HELIX 10 10 ALA A 1251 GLN A 1258 1 8
HELIX 11 11 THR A 1261 THR A 1278 1 18
HELIX 12 12 ASN A 1288 PHE A 1290 5 3
HELIX 13 13 ASP A 1291 GLN A 1298 1 8
HELIX 14 14 PRO A 1309 TRP A 1320 1 12
HELIX 15 15 LYS A 1323 ARG A 1327 5 5
HELIX 16 16 SER A 1329 THR A 1343 1 15
SHEET 1 A 6 VAL A1070 ILE A1071 0
SHEET 2 A 6 GLY A1144 CYS A1146 1 O ILE A1145 N ILE A1071
SHEET 3 A 6 LEU A1154 PRO A1158 -1 O LEU A1154 N CYS A1146
SHEET 4 A 6 HIS A1106 LYS A1110 -1 N ALA A1108 O LEU A1157
SHEET 5 A 6 CYS A1091 THR A1096 -1 N TYR A1093 O VAL A1109
SHEET 6 A 6 ILE A1077 ARG A1086 -1 N ILE A1077 O THR A1096
SHEET 1 B 2 CYS A1210 LEU A1212 0
SHEET 2 B 2 VAL A1218 VAL A1220 -1 O LYS A1219 N MET A1211
SHEET 1 C 2 SER A1236 VAL A1237 0
SHEET 2 C 2 LYS A1244 LEU A1245 -1 O LEU A1245 N SER A1236
SITE 1 AC1 14 ILE A1084 ALA A1108 LEU A1157 PRO A1158
SITE 2 AC1 14 TYR A1159 MET A1160 ASP A1164 ARG A1208
SITE 3 AC1 14 MET A1211 ALA A1221 ASP A1222 ALA A1226
SITE 4 AC1 14 TYR A1230 HOH A1480
CRYST1 42.058 43.440 157.827 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.023777 0.000000 0.000000 0.00000
SCALE2 0.000000 0.023020 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006336 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
