HEADER TRANSFERASE 20-MAR-12 4ANL
TITLE STRUCTURE OF G1269A MUTANT ANAPLASTIC LYMPHOMA KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALK TYROSINE KINASE RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE, RESIDUES 1093-1411;
COMPND 5 SYNONYM: ANAPLASTIC LYMPHOMA KINASE, CD246;
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 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1
KEYWDS TRANSFERASE, CRIZOTINIB
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MCTIGUE,Y.DENG,W.LIU,A.BROOUN
REVDAT 4 20-DEC-23 4ANL 1 REMARK
REVDAT 3 08-MAY-19 4ANL 1 REMARK
REVDAT 2 19-MAR-14 4ANL 1 JRNL
REVDAT 1 27-MAR-13 4ANL 0
JRNL AUTH Q.HUANG,T.W.JOHNSON,S.BAILEY,A.BROOUN,K.D.BUNKER,B.J.BURKE,
JRNL AUTH 2 M.R.COLLINS,A.S.COOK,J.J.CUI,K.N.DACK,J.G.DEAL,Y.DENG,
JRNL AUTH 3 D.DINH,L.D.ENGSTROM,M.HE,J.HOFFMAN,R.L.HOFFMAN,P.S.JOHNSON,
JRNL AUTH 4 R.S.KANIA,H.LAM,J.L.LAM,P.T.LE,Q.LI,L.LINGARDO,W.LIU,M.W.LU,
JRNL AUTH 5 M.MCTIGUE,C.L.PALMER,P.F.RICHARDSON,N.W.SACH,H.SHEN,T.SMEAL,
JRNL AUTH 6 G.L.SMITH,A.E.STEWART,S.TIMOFEEVSKI,K.TSAPARIKOS,H.WANG,
JRNL AUTH 7 H.ZHU,J.ZHU,H.Y.ZOU,M.P.EDWARDS
JRNL TITL DESIGN OF POTENT AND SELECTIVE INHIBITORS TO OVERCOME
JRNL TITL 2 CLINICAL ANAPLASTIC LYMPHOMA KINASE MUTATIONS RESISTANT TO
JRNL TITL 3 CRIZOTINIB.
JRNL REF J.MED.CHEM. V. 57 1170 2014
JRNL REFN ISSN 0022-2623
JRNL PMID 24432909
JRNL DOI 10.1021/JM401805H
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2005
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 52.58
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1141278.310
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 35145
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1054
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.81
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5525
REMARK 3 BIN R VALUE (WORKING SET) : 0.2550
REMARK 3 BIN FREE R VALUE : 0.2710
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 164
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2305
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 274
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.69000
REMARK 3 B22 (A**2) : -0.72000
REMARK 3 B33 (A**2) : 4.41000
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) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.12
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) : 0.23
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.16
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.004
REMARK 3 BOND ANGLES (DEGREES) : 0.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.650
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) : 1.320 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.090 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.240 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.380 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 50.35
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4ANL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1290051601.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 87
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35264
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 105.150
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNX
REMARK 200 STARTING MODEL: PDB ENTRY 2XP2
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN BY THE HANGING
REMARK 280 DROP VAPOR DIFFUSION METHOD AT 13 DEGRESS CELCIUS BY MIXING 2
REMARK 280 MICROLITERS OF PROTEIN SOLUTION WITH A RESERVOIR SOLUTION
REMARK 280 CONTAINING: 19% (W/V) PEG 3350, 0.1 M TRIS PH 8.5, 0.2 M LITHIUM
REMARK 280 SULFATE, AND 0.1 (W/V) BETA-OCTYLGLCOSIDE, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 286K
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 25.91800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.57550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.79600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.57550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.91800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.79600
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLY 1269 TO ALA
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 1070
REMARK 465 ALA A 1071
REMARK 465 HIS A 1072
REMARK 465 HIS A 1073
REMARK 465 HIS A 1074
REMARK 465 HIS A 1075
REMARK 465 HIS A 1076
REMARK 465 HIS A 1077
REMARK 465 ASP A 1078
REMARK 465 TYR A 1079
REMARK 465 GLY A 1080
REMARK 465 ILE A 1081
REMARK 465 PRO A 1082
REMARK 465 THR A 1083
REMARK 465 THR A 1084
REMARK 465 GLU A 1085
REMARK 465 ASN A 1086
REMARK 465 LEU A 1087
REMARK 465 TYR A 1088
REMARK 465 PHE A 1089
REMARK 465 GLN A 1090
REMARK 465 GLY A 1091
REMARK 465 SER A 1092
REMARK 465 ASN A 1093
REMARK 465 HIS A 1124
REMARK 465 GLY A 1125
REMARK 465 SER A 1136
REMARK 465 GLY A 1137
REMARK 465 MET A 1138
REMARK 465 PRO A 1139
REMARK 465 ASN A 1140
REMARK 465 ASP A 1141
REMARK 465 PRO A 1142
REMARK 465 SER A 1143
REMARK 465 ALA A 1280
REMARK 465 SER A 1281
REMARK 465 TYR A 1282
REMARK 465 TYR A 1283
REMARK 465 ARG A 1284
REMARK 465 LYS A 1285
REMARK 465 PRO A 1403
REMARK 465 LEU A 1404
REMARK 465 VAL A 1405
REMARK 465 GLU A 1406
REMARK 465 GLU A 1407
REMARK 465 GLU A 1408
REMARK 465 GLU A 1409
REMARK 465 LYS A 1410
REMARK 465 VAL A 1411
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 GLY A1402 CA C O
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 A1248 -10.50 79.26
REMARK 500 ASP A1249 47.07 -148.76
REMARK 500 SER A1332 -3.08 77.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2034 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH A2039 DISTANCE = 6.14 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ANQ RELATED DB: PDB
REMARK 900 STRUCTURE OF G1269A MUTANT ANAPLASTIC LYMPHOMA KINASE IN COMPLEX
REMARK 900 WITH CRIZOTINIB
REMARK 900 RELATED ID: 4ANS RELATED DB: PDB
REMARK 900 STRUCTURE OF L1196M,G1269A DOUBLE MUTANT ANAPLASTIC LYMPHOMA KINASE
REMARK 900 IN COMPLEX WITH CRIZOTINIB
REMARK 900 RELATED ID: 4AOI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF C-MET KINASE DOMAIN IN COMPLEX WITH 4-(3-((1H-
REMARK 900 PYRROLO(2,3-B)PYRIDIN-3-YL)METHYL )-(1,2,4)TRIAZOLO(4,3-B)(1,2,4)
REMARK 900 TRIAZIN-6-YL) BENZONITRILE
DBREF 4ANL A 1093 1411 UNP Q9UM73 ALK_HUMAN 1093 1411
SEQADV 4ANL MET A 1070 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL ALA A 1071 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL HIS A 1072 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL HIS A 1073 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL HIS A 1074 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL HIS A 1075 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL HIS A 1076 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL HIS A 1077 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL ASP A 1078 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL TYR A 1079 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL GLY A 1080 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL ILE A 1081 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL PRO A 1082 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL THR A 1083 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL THR A 1084 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL GLU A 1085 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL ASN A 1086 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL LEU A 1087 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL TYR A 1088 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL PHE A 1089 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL GLN A 1090 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL GLY A 1091 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL SER A 1092 UNP Q9UM73 EXPRESSION TAG
SEQADV 4ANL ALA A 1269 UNP Q9UM73 GLY 1269 ENGINEERED MUTATION
SEQRES 1 A 342 MET ALA HIS HIS HIS HIS HIS HIS ASP TYR GLY ILE PRO
SEQRES 2 A 342 THR THR GLU ASN LEU TYR PHE GLN GLY SER ASN PRO ASN
SEQRES 3 A 342 TYR CYS PHE ALA GLY LYS THR SER SER ILE SER ASP LEU
SEQRES 4 A 342 LYS GLU VAL PRO ARG LYS ASN ILE THR LEU ILE ARG GLY
SEQRES 5 A 342 LEU GLY HIS GLY ALA PHE GLY GLU VAL TYR GLU GLY GLN
SEQRES 6 A 342 VAL SER GLY MET PRO ASN ASP PRO SER PRO LEU GLN VAL
SEQRES 7 A 342 ALA VAL LYS THR LEU PRO GLU VAL CYS SER GLU GLN ASP
SEQRES 8 A 342 GLU LEU ASP PHE LEU MET GLU ALA LEU ILE ILE SER LYS
SEQRES 9 A 342 PHE ASN HIS GLN ASN ILE VAL ARG CYS ILE GLY VAL SER
SEQRES 10 A 342 LEU GLN SER LEU PRO ARG PHE ILE LEU LEU GLU LEU MET
SEQRES 11 A 342 ALA GLY GLY ASP LEU LYS SER PHE LEU ARG GLU THR ARG
SEQRES 12 A 342 PRO ARG PRO SER GLN PRO SER SER LEU ALA MET LEU ASP
SEQRES 13 A 342 LEU LEU HIS VAL ALA ARG ASP ILE ALA CYS GLY CYS GLN
SEQRES 14 A 342 TYR LEU GLU GLU ASN HIS PHE ILE HIS ARG ASP ILE ALA
SEQRES 15 A 342 ALA ARG ASN CYS LEU LEU THR CYS PRO GLY PRO GLY ARG
SEQRES 16 A 342 VAL ALA LYS ILE ALA ASP PHE GLY MET ALA ARG ASP ILE
SEQRES 17 A 342 TYR ARG ALA SER TYR TYR ARG LYS GLY GLY CYS ALA MET
SEQRES 18 A 342 LEU PRO VAL LYS TRP MET PRO PRO GLU ALA PHE MET GLU
SEQRES 19 A 342 GLY ILE PHE THR SER LYS THR ASP THR TRP SER PHE GLY
SEQRES 20 A 342 VAL LEU LEU TRP GLU ILE PHE SER LEU GLY TYR MET PRO
SEQRES 21 A 342 TYR PRO SER LYS SER ASN GLN GLU VAL LEU GLU PHE VAL
SEQRES 22 A 342 THR SER GLY GLY ARG MET ASP PRO PRO LYS ASN CYS PRO
SEQRES 23 A 342 GLY PRO VAL TYR ARG ILE MET THR GLN CYS TRP GLN HIS
SEQRES 24 A 342 GLN PRO GLU ASP ARG PRO ASN PHE ALA ILE ILE LEU GLU
SEQRES 25 A 342 ARG ILE GLU TYR CYS THR GLN ASP PRO ASP VAL ILE ASN
SEQRES 26 A 342 THR ALA LEU PRO ILE GLU TYR GLY PRO LEU VAL GLU GLU
SEQRES 27 A 342 GLU GLU LYS VAL
FORMUL 2 HOH *274(H2 O)
HELIX 1 1 SER A 1104 LEU A 1108 5 5
HELIX 2 2 PRO A 1112 ILE A 1116 5 5
HELIX 3 3 SER A 1157 PHE A 1174 1 18
HELIX 4 4 LEU A 1204 THR A 1211 1 8
HELIX 5 5 ALA A 1222 ASN A 1243 1 22
HELIX 6 6 ALA A 1251 ARG A 1253 5 3
HELIX 7 7 PHE A 1271 ARG A 1279 1 9
HELIX 8 8 GLY A 1287 LEU A 1291 5 5
HELIX 9 9 PRO A 1292 MET A 1296 5 5
HELIX 10 10 PRO A 1297 GLY A 1304 1 8
HELIX 11 11 THR A 1307 SER A 1324 1 18
HELIX 12 12 SER A 1334 SER A 1344 1 11
HELIX 13 13 PRO A 1355 TRP A 1366 1 12
HELIX 14 14 GLN A 1369 ARG A 1373 5 5
HELIX 15 15 ASN A 1375 ASP A 1389 1 15
HELIX 16 16 ASP A 1389 ASN A 1394 1 6
SHEET 1 AA 2 TYR A1096 PHE A1098 0
SHEET 2 AA 2 LYS A1101 SER A1103 -1 O LYS A1101 N PHE A1098
SHEET 1 AB 5 THR A1117 GLY A1121 0
SHEET 2 AB 5 VAL A1130 GLN A1134 -1 O GLU A1132 N ILE A1119
SHEET 3 AB 5 GLN A1146 THR A1151 -1 O VAL A1147 N GLY A1133
SHEET 4 AB 5 PHE A1193 GLU A1197 -1 O ILE A1194 N LYS A1150
SHEET 5 AB 5 CYS A1182 SER A1186 -1 N ILE A1183 O LEU A1195
SHEET 1 AC 3 GLY A1202 ASP A1203 0
SHEET 2 AC 3 CYS A1255 LEU A1257 -1 N LEU A1257 O GLY A1202
SHEET 3 AC 3 ALA A1266 ILE A1268 -1 O LYS A1267 N LEU A1256
CISPEP 1 LEU A 1190 PRO A 1191 0 -2.56
CRYST1 51.836 57.592 105.151 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 0.019292 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017364 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009510 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
