HEADER TRANSFERASE 01-AUG-17 5WO4
TITLE JAK1 COMPLEXED WITH COMPOUND 28
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE JAK1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 854-1154;
COMPND 5 SYNONYM: JANUS KINASE 1,JAK-1;
COMPND 6 EC: 2.7.10.2;
COMPND 7 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: JAK1, JAK1A, JAK1B;
SOURCE 6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10469
KEYWDS PROTEIN TYROSINE KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.A.LESBURG,S.B.PATEL
REVDAT 4 06-MAR-24 5WO4 1 REMARK
REVDAT 3 27-DEC-17 5WO4 1 JRNL
REVDAT 2 13-DEC-17 5WO4 1 JRNL
REVDAT 1 06-DEC-17 5WO4 0
JRNL AUTH T.SIU,J.BRUBAKER,P.FULLER,L.TORRES,H.ZENG,J.CLOSE,
JRNL AUTH 2 D.M.MAMPREIAN,F.SHI,D.LIU,X.FRADERA,K.JOHNSON,N.BAYS,
JRNL AUTH 3 E.KADIC,F.HE,P.GOLDENBLATT,L.SHAFFER,S.B.PATEL,C.A.LESBURG,
JRNL AUTH 4 C.ALPERT,L.DOROSH,S.V.DESHMUKH,H.YU,J.KLAPPENBACH,F.ELWOOD,
JRNL AUTH 5 C.J.DINSMORE,R.FERNANDEZ,L.MOY,J.R.YOUNG
JRNL TITL THE DISCOVERY OF
JRNL TITL 2 3-((4-CHLORO-3-METHOXYPHENYL)AMINO)-1-((3R,4S)
JRNL TITL 3 -4-CYANOTETRAHYDRO-2H-PYRAN-3-YL)-1H-PYRAZOLE-4-CARBOXAMIDE,
JRNL TITL 4 A HIGHLY LIGAND EFFICIENT AND EFFICACIOUS JANUS KINASE 1
JRNL TITL 5 SELECTIVE INHIBITOR WITH FAVORABLE PHARMACOKINETIC
JRNL TITL 6 PROPERTIES.
JRNL REF J. MED. CHEM. V. 60 9676 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 29156136
JRNL DOI 10.1021/ACS.JMEDCHEM.7B01135
REMARK 2
REMARK 2 RESOLUTION. 1.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.4
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 55350
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.530
REMARK 3 FREE R VALUE TEST SET COUNT : 2505
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.89
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.43
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4031
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2066
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3860
REMARK 3 BIN R VALUE (WORKING SET) : 0.2052
REMARK 3 BIN FREE R VALUE : 0.2371
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.24
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 171
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 : 4689
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 471
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.37
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.74410
REMARK 3 B22 (A**2) : 0.07030
REMARK 3 B33 (A**2) : -0.81440
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.78500
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.211
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.136
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.120
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.133
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.119
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4859 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 6556 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1740 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 126 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 711 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4859 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 597 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 6021 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.01
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.33
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.87
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5WO4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1000229335.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-SEP-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55407
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840
REMARK 200 RESOLUTION RANGE LOW (A) : 173.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.54500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: AUTOBUSTER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 6.0, 30% (W/V) PEG 6000,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, 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 86.68000
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 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 GLY A 853
REMARK 465 GLU A 913
REMARK 465 SER A 914
REMARK 465 GLY A 915
REMARK 465 GLY A 916
REMARK 465 ASP A 947
REMARK 465 GLY A 948
REMARK 465 GLY A 949
REMARK 465 GLY B 853
REMARK 465 ASP B 854
REMARK 465 ILE B 855
REMARK 465 VAL B 856
REMARK 465 SER B 857
REMARK 465 GLU B 858
REMARK 465 LYS B 859
REMARK 465 LYS B 860
REMARK 465 PRO B 861
REMARK 465 ALA B 862
REMARK 465 THR B 863
REMARK 465 GLU B 864
REMARK 465 GLU B 913
REMARK 465 SER B 914
REMARK 465 GLY B 915
REMARK 465 GLY B 916
REMARK 465 GLU B 946
REMARK 465 ASP B 947
REMARK 465 GLY B 948
REMARK 465 GLY B 949
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 A 861 -151.82 -92.79
REMARK 500 ILE A 878 -61.56 -103.31
REMARK 500 HIS A 885 73.46 46.61
REMARK 500 ARG A1002 -2.92 67.85
REMARK 500 ASP A1003 35.29 -141.21
REMARK 500 ILE B 878 -62.44 -103.22
REMARK 500 HIS B 885 73.49 46.22
REMARK 500 ASP B1003 36.01 -143.90
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 B7V A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue B7V B 2001
DBREF 5WO4 A 854 1154 UNP P23458 JAK1_HUMAN 854 1154
DBREF 5WO4 B 854 1154 UNP P23458 JAK1_HUMAN 854 1154
SEQADV 5WO4 GLY A 853 UNP P23458 EXPRESSION TAG
SEQADV 5WO4 GLY B 853 UNP P23458 EXPRESSION TAG
SEQRES 1 A 302 GLY ASP ILE VAL SER GLU LYS LYS PRO ALA THR GLU VAL
SEQRES 2 A 302 ASP PRO THR HIS PHE GLU LYS ARG PHE LEU LYS ARG ILE
SEQRES 3 A 302 ARG ASP LEU GLY GLU GLY HIS PHE GLY LYS VAL GLU LEU
SEQRES 4 A 302 CYS ARG TYR ASP PRO GLU GLY ASP ASN THR GLY GLU GLN
SEQRES 5 A 302 VAL ALA VAL LYS SER LEU LYS PRO GLU SER GLY GLY ASN
SEQRES 6 A 302 HIS ILE ALA ASP LEU LYS LYS GLU ILE GLU ILE LEU ARG
SEQRES 7 A 302 ASN LEU TYR HIS GLU ASN ILE VAL LYS TYR LYS GLY ILE
SEQRES 8 A 302 CYS THR GLU ASP GLY GLY ASN GLY ILE LYS LEU ILE MET
SEQRES 9 A 302 GLU PHE LEU PRO SER GLY SER LEU LYS GLU TYR LEU PRO
SEQRES 10 A 302 LYS ASN LYS ASN LYS ILE ASN LEU LYS GLN GLN LEU LYS
SEQRES 11 A 302 TYR ALA VAL GLN ILE CYS LYS GLY MET ASP TYR LEU GLY
SEQRES 12 A 302 SER ARG GLN TYR VAL HIS ARG ASP LEU ALA ALA ARG ASN
SEQRES 13 A 302 VAL LEU VAL GLU SER GLU HIS GLN VAL LYS ILE GLY ASP
SEQRES 14 A 302 PHE GLY LEU THR LYS ALA ILE GLU THR ASP LYS GLU PTR
SEQRES 15 A 302 PTR THR VAL LYS ASP ASP ARG ASP SER PRO VAL PHE TRP
SEQRES 16 A 302 TYR ALA PRO GLU CYS LEU MET GLN SER LYS PHE TYR ILE
SEQRES 17 A 302 ALA SER ASP VAL TRP SER PHE GLY VAL THR LEU HIS GLU
SEQRES 18 A 302 LEU LEU THR TYR CYS ASP SER ASP SER SER PRO MET ALA
SEQRES 19 A 302 LEU PHE LEU LYS MET ILE GLY PRO THR HIS GLY GLN MET
SEQRES 20 A 302 THR VAL THR ARG LEU VAL ASN THR LEU LYS GLU GLY LYS
SEQRES 21 A 302 ARG LEU PRO CYS PRO PRO ASN CYS PRO ASP GLU VAL TYR
SEQRES 22 A 302 GLN LEU MET ARG LYS CYS TRP GLU PHE GLN PRO SER ASN
SEQRES 23 A 302 ARG THR SER PHE GLN ASN LEU ILE GLU GLY PHE GLU ALA
SEQRES 24 A 302 LEU LEU LYS
SEQRES 1 B 302 GLY ASP ILE VAL SER GLU LYS LYS PRO ALA THR GLU VAL
SEQRES 2 B 302 ASP PRO THR HIS PHE GLU LYS ARG PHE LEU LYS ARG ILE
SEQRES 3 B 302 ARG ASP LEU GLY GLU GLY HIS PHE GLY LYS VAL GLU LEU
SEQRES 4 B 302 CYS ARG TYR ASP PRO GLU GLY ASP ASN THR GLY GLU GLN
SEQRES 5 B 302 VAL ALA VAL LYS SER LEU LYS PRO GLU SER GLY GLY ASN
SEQRES 6 B 302 HIS ILE ALA ASP LEU LYS LYS GLU ILE GLU ILE LEU ARG
SEQRES 7 B 302 ASN LEU TYR HIS GLU ASN ILE VAL LYS TYR LYS GLY ILE
SEQRES 8 B 302 CYS THR GLU ASP GLY GLY ASN GLY ILE LYS LEU ILE MET
SEQRES 9 B 302 GLU PHE LEU PRO SER GLY SER LEU LYS GLU TYR LEU PRO
SEQRES 10 B 302 LYS ASN LYS ASN LYS ILE ASN LEU LYS GLN GLN LEU LYS
SEQRES 11 B 302 TYR ALA VAL GLN ILE CYS LYS GLY MET ASP TYR LEU GLY
SEQRES 12 B 302 SER ARG GLN TYR VAL HIS ARG ASP LEU ALA ALA ARG ASN
SEQRES 13 B 302 VAL LEU VAL GLU SER GLU HIS GLN VAL LYS ILE GLY ASP
SEQRES 14 B 302 PHE GLY LEU THR LYS ALA ILE GLU THR ASP LYS GLU PTR
SEQRES 15 B 302 PTR THR VAL LYS ASP ASP ARG ASP SER PRO VAL PHE TRP
SEQRES 16 B 302 TYR ALA PRO GLU CYS LEU MET GLN SER LYS PHE TYR ILE
SEQRES 17 B 302 ALA SER ASP VAL TRP SER PHE GLY VAL THR LEU HIS GLU
SEQRES 18 B 302 LEU LEU THR TYR CYS ASP SER ASP SER SER PRO MET ALA
SEQRES 19 B 302 LEU PHE LEU LYS MET ILE GLY PRO THR HIS GLY GLN MET
SEQRES 20 B 302 THR VAL THR ARG LEU VAL ASN THR LEU LYS GLU GLY LYS
SEQRES 21 B 302 ARG LEU PRO CYS PRO PRO ASN CYS PRO ASP GLU VAL TYR
SEQRES 22 B 302 GLN LEU MET ARG LYS CYS TRP GLU PHE GLN PRO SER ASN
SEQRES 23 B 302 ARG THR SER PHE GLN ASN LEU ILE GLU GLY PHE GLU ALA
SEQRES 24 B 302 LEU LEU LYS
MODRES 5WO4 PTR A 1034 TYR MODIFIED RESIDUE
MODRES 5WO4 PTR A 1035 TYR MODIFIED RESIDUE
MODRES 5WO4 PTR B 1034 TYR MODIFIED RESIDUE
MODRES 5WO4 PTR B 1035 TYR MODIFIED RESIDUE
HET PTR A1034 16
HET PTR A1035 16
HET PTR B1034 16
HET PTR B1035 16
HET B7V A2001 26
HET B7V B2001 26
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM B7V 3-[(4-CHLORO-3-METHOXYPHENYL)AMINO]-1-[(3R,4S)-4-
HETNAM 2 B7V CYANOOXAN-3-YL]-1H-PYRAZOLE-4-CARBOXAMIDE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 PTR 4(C9 H12 N O6 P)
FORMUL 3 B7V 2(C17 H18 CL N5 O3)
FORMUL 5 HOH *471(H2 O)
HELIX 1 AA1 GLU A 871 ARG A 873 5 3
HELIX 2 AA2 HIS A 918 ASN A 931 1 14
HELIX 3 AA3 SER A 963 ASN A 971 1 9
HELIX 4 AA4 ASN A 976 ARG A 997 1 22
HELIX 5 AA5 ALA A 1005 ARG A 1007 5 3
HELIX 6 AA6 PRO A 1044 TYR A 1048 5 5
HELIX 7 AA7 ALA A 1049 SER A 1056 1 8
HELIX 8 AA8 ILE A 1060 THR A 1076 1 17
HELIX 9 AA9 ASP A 1079 SER A 1082 5 4
HELIX 10 AB1 SER A 1083 GLY A 1093 1 11
HELIX 11 AB2 HIS A 1096 GLN A 1098 5 3
HELIX 12 AB3 MET A 1099 GLU A 1110 1 12
HELIX 13 AB4 PRO A 1121 LYS A 1130 1 10
HELIX 14 AB5 CYS A 1131 GLU A 1133 5 3
HELIX 15 AB6 GLN A 1135 ARG A 1139 5 5
HELIX 16 AB7 SER A 1141 LYS A 1154 1 14
HELIX 17 AB8 GLU B 871 ARG B 873 5 3
HELIX 18 AB9 HIS B 918 ASN B 931 1 14
HELIX 19 AC1 SER B 963 LYS B 972 1 10
HELIX 20 AC2 ASN B 976 ARG B 997 1 22
HELIX 21 AC3 ALA B 1005 ARG B 1007 5 3
HELIX 22 AC4 PRO B 1044 TYR B 1048 5 5
HELIX 23 AC5 ALA B 1049 SER B 1056 1 8
HELIX 24 AC6 ILE B 1060 THR B 1076 1 17
HELIX 25 AC7 ASP B 1079 SER B 1082 5 4
HELIX 26 AC8 SER B 1083 GLY B 1093 1 11
HELIX 27 AC9 HIS B 1096 GLN B 1098 5 3
HELIX 28 AD1 MET B 1099 GLU B 1110 1 12
HELIX 29 AD2 PRO B 1121 LYS B 1130 1 10
HELIX 30 AD3 GLN B 1135 ARG B 1139 5 5
HELIX 31 AD4 SER B 1141 LYS B 1154 1 14
SHEET 1 AA1 5 LEU A 875 GLY A 884 0
SHEET 2 AA1 5 GLY A 887 TYR A 894 -1 O VAL A 889 N GLY A 882
SHEET 3 AA1 5 GLU A 903 LEU A 910 -1 O VAL A 907 N GLU A 890
SHEET 4 AA1 5 ILE A 952 GLU A 957 -1 O MET A 956 N ALA A 906
SHEET 5 AA1 5 TYR A 940 THR A 945 -1 N LYS A 941 O ILE A 955
SHEET 1 AA2 2 TYR A 999 VAL A1000 0
SHEET 2 AA2 2 LYS A1026 ALA A1027 -1 O LYS A1026 N VAL A1000
SHEET 1 AA3 2 VAL A1009 SER A1013 0
SHEET 2 AA3 2 GLN A1016 ILE A1019 -1 O LYS A1018 N LEU A1010
SHEET 1 AA4 2 PTR A1034 THR A1036 0
SHEET 2 AA4 2 LYS A1057 TYR A1059 -1 O PHE A1058 N PTR A1035
SHEET 1 AA5 5 LEU B 875 GLY B 884 0
SHEET 2 AA5 5 GLY B 887 TYR B 894 -1 O VAL B 889 N LEU B 881
SHEET 3 AA5 5 GLU B 903 LEU B 910 -1 O GLU B 903 N TYR B 894
SHEET 4 AA5 5 LYS B 953 GLU B 957 -1 O MET B 956 N ALA B 906
SHEET 5 AA5 5 TYR B 940 CYS B 944 -1 N LYS B 941 O ILE B 955
SHEET 1 AA6 2 TYR B 999 VAL B1000 0
SHEET 2 AA6 2 LYS B1026 ALA B1027 -1 O LYS B1026 N VAL B1000
SHEET 1 AA7 2 VAL B1009 SER B1013 0
SHEET 2 AA7 2 GLN B1016 ILE B1019 -1 O LYS B1018 N LEU B1010
SHEET 1 AA8 2 PTR B1034 THR B1036 0
SHEET 2 AA8 2 LYS B1057 TYR B1059 -1 O PHE B1058 N PTR B1035
LINK C GLU A1033 N PTR A1034 1555 1555 1.34
LINK C PTR A1034 N PTR A1035 1555 1555 1.34
LINK C PTR A1035 N THR A1036 1555 1555 1.34
LINK C GLU B1033 N PTR B1034 1555 1555 1.34
LINK C PTR B1034 N PTR B1035 1555 1555 1.34
LINK C PTR B1035 N THR B1036 1555 1555 1.35
SITE 1 AC1 16 LEU A 881 GLY A 882 ALA A 906 GLU A 957
SITE 2 AC1 16 PHE A 958 LEU A 959 PRO A 960 GLY A 962
SITE 3 AC1 16 GLU A 966 ARG A1007 ASN A1008 LEU A1010
SITE 4 AC1 16 GLY A1020 ASP A1021 HOH A2109 HOH A2195
SITE 1 AC2 15 LEU B 881 GLY B 882 ALA B 906 GLU B 957
SITE 2 AC2 15 PHE B 958 LEU B 959 PRO B 960 GLY B 962
SITE 3 AC2 15 GLU B 966 ARG B1007 ASN B1008 LEU B1010
SITE 4 AC2 15 GLY B1020 HOH B2163 HOH B2229
CRYST1 42.570 173.360 44.650 90.00 93.94 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 0.023491 0.000000 0.001618 0.00000
SCALE2 0.000000 0.005768 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022449 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
