HEADER IMMUNE SYSTEM 27-NOV-18 6N7A
TITLE STRUCTURE OF THE HUMAN JAK1 KINASE DOMAIN WITH COMPOUND 39
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE JAK1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: JANUS KINASE 1,JAK-1;
COMPND 5 EC: 2.7.10.2;
COMPND 6 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: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS JAK1, IL13, IL-13, JAK2, JAK3, TYK2, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.LUPARDUS,D.BROWN
REVDAT 2 15-MAY-19 6N7A 1 JRNL
REVDAT 1 24-APR-19 6N7A 0
JRNL AUTH M.ZAK,E.J.HANAN,P.LUPARDUS,D.G.BROWN,C.ROBINSON,M.SIU,
JRNL AUTH 2 J.P.LYSSIKATOS,F.A.ROMERO,G.ZHAO,T.KELLAR,R.MENDONCA,
JRNL AUTH 3 N.C.RAY,S.C.GOODACRE,P.H.CRACKETT,N.MCLEAN,C.A.HURLEY,
JRNL AUTH 4 P.W.YUEN,Y.X.CHENG,X.LIU,M.LIIMATTA,P.B.KOHLI,J.NONOMIYA,
JRNL AUTH 5 G.SALMON,G.BUCKLEY,J.LLOYD,P.GIBBONS,N.GHILARDI,J.R.KENNY,
JRNL AUTH 6 A.JOHNSON
JRNL TITL DISCOVERY OF A CLASS OF HIGHLY POTENT JANUS KINASE 1/2
JRNL TITL 2 (JAK1/2) INHIBITORS DEMONSTRATING EFFECTIVE CELL-BASED
JRNL TITL 3 BLOCKADE OF IL-13 SIGNALING.
JRNL REF BIOORG.MED.CHEM.LETT. V. 29 1522 2019
JRNL REFN ESSN 1464-3405
JRNL PMID 30981576
JRNL DOI 10.1016/J.BMCL.2019.04.008
REMARK 2
REMARK 2 RESOLUTION. 1.33 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.7
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) : 1.33
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 86.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 146153
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 7315
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) : 1.33
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.36
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.96
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 10330
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2767
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 9827
REMARK 3 BIN R VALUE (WORKING SET) : 0.2767
REMARK 3 BIN FREE R VALUE : 0.2758
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.87
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 503
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 : 4613
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 74
REMARK 3 SOLVENT ATOMS : 588
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.66
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.27140
REMARK 3 B22 (A**2) : -0.60160
REMARK 3 B33 (A**2) : 0.33020
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.19940
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.190
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.054
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.054
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.053
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.053
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 : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4839 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 6539 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1712 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 862 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4839 ; 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 : 598 ; 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 : 6157 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.03
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.89
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.47
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 6N7A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1000238011.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAY-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92
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 : XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 146507
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.330
REMARK 200 RESOLUTION RANGE LOW (A) : 173.230
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.33
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.66600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 5-6 AND 25-35% PEG 6000,
REMARK 280 PH 5.5, 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 86.61500
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 851
REMARK 465 SER A 852
REMARK 465 GLY A 853
REMARK 465 ASP A 854
REMARK 465 ILE A 855
REMARK 465 VAL A 856
REMARK 465 SER A 857
REMARK 465 GLU A 858
REMARK 465 LYS A 859
REMARK 465 LYS A 860
REMARK 465 PRO A 861
REMARK 465 ALA A 862
REMARK 465 THR A 863
REMARK 465 GLU A 864
REMARK 465 GLU A 913
REMARK 465 SER A 914
REMARK 465 GLY A 915
REMARK 465 GLY A 916
REMARK 465 ASN A 917
REMARK 465 GLU A 946
REMARK 465 ASP A 947
REMARK 465 GLY A 948
REMARK 465 GLY A 949
REMARK 465 ASN A 950
REMARK 465 PRO A 1094
REMARK 465 THR A 1095
REMARK 465 GLU B 913
REMARK 465 SER B 914
REMARK 465 GLY B 915
REMARK 465 GLY B 916
REMARK 465 ASN B 917
REMARK 465 GLU B 946
REMARK 465 ASP B 947
REMARK 465 GLY B 948
REMARK 465 GLY B 949
REMARK 465 ASN B 950
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 A1038 CG CD CE NZ
REMARK 470 ARG A1041 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 859 CG CD CE NZ
REMARK 470 LYS B 860 CG CD CE NZ
REMARK 470 GLU B 864 CG CD OE1 OE2
REMARK 470 LYS B1038 CG CD CE NZ
REMARK 470 ARG B1041 CG CD NE CZ NH1 NH2
REMARK 470 ASP B1042 CG OD1 OD2
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 A1002 -4.01 72.80
REMARK 500 ASP A1003 35.87 -142.17
REMARK 500 ASP B1003 35.97 -146.43
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 GOL A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KEV A 1203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KEV B 1202
DBREF 6N7A A 854 1154 UNP P23458 JAK1_HUMAN 854 1154
DBREF 6N7A B 854 1154 UNP P23458 JAK1_HUMAN 854 1154
SEQADV 6N7A GLY A 851 UNP P23458 EXPRESSION TAG
SEQADV 6N7A SER A 852 UNP P23458 EXPRESSION TAG
SEQADV 6N7A GLY A 853 UNP P23458 EXPRESSION TAG
SEQADV 6N7A GLY B 851 UNP P23458 EXPRESSION TAG
SEQADV 6N7A SER B 852 UNP P23458 EXPRESSION TAG
SEQADV 6N7A GLY B 853 UNP P23458 EXPRESSION TAG
SEQRES 1 A 304 GLY SER GLY ASP ILE VAL SER GLU LYS LYS PRO ALA THR
SEQRES 2 A 304 GLU VAL ASP PRO THR HIS PHE GLU LYS ARG PHE LEU LYS
SEQRES 3 A 304 ARG ILE ARG ASP LEU GLY GLU GLY HIS PHE GLY LYS VAL
SEQRES 4 A 304 GLU LEU CYS ARG TYR ASP PRO GLU GLY ASP ASN THR GLY
SEQRES 5 A 304 GLU GLN VAL ALA VAL LYS SER LEU LYS PRO GLU SER GLY
SEQRES 6 A 304 GLY ASN HIS ILE ALA ASP LEU LYS LYS GLU ILE GLU ILE
SEQRES 7 A 304 LEU ARG ASN LEU TYR HIS GLU ASN ILE VAL LYS TYR LYS
SEQRES 8 A 304 GLY ILE CYS THR GLU ASP GLY GLY ASN GLY ILE LYS LEU
SEQRES 9 A 304 ILE MET GLU PHE LEU PRO SER GLY SER LEU LYS GLU TYR
SEQRES 10 A 304 LEU PRO LYS ASN LYS ASN LYS ILE ASN LEU LYS GLN GLN
SEQRES 11 A 304 LEU LYS TYR ALA VAL GLN ILE CYS LYS GLY MET ASP TYR
SEQRES 12 A 304 LEU GLY SER ARG GLN TYR VAL HIS ARG ASP LEU ALA ALA
SEQRES 13 A 304 ARG ASN VAL LEU VAL GLU SER GLU HIS GLN VAL LYS ILE
SEQRES 14 A 304 GLY ASP PHE GLY LEU THR LYS ALA ILE GLU THR ASP LYS
SEQRES 15 A 304 GLU PTR PTR THR VAL LYS ASP ASP ARG ASP SER PRO VAL
SEQRES 16 A 304 PHE TRP TYR ALA PRO GLU CYS LEU MET GLN SER LYS PHE
SEQRES 17 A 304 TYR ILE ALA SER ASP VAL TRP SER PHE GLY VAL THR LEU
SEQRES 18 A 304 HIS GLU LEU LEU THR TYR CYS ASP SER ASP SER SER PRO
SEQRES 19 A 304 MET ALA LEU PHE LEU LYS MET ILE GLY PRO THR HIS GLY
SEQRES 20 A 304 GLN MET THR VAL THR ARG LEU VAL ASN THR LEU LYS GLU
SEQRES 21 A 304 GLY LYS ARG LEU PRO CYS PRO PRO ASN CYS PRO ASP GLU
SEQRES 22 A 304 VAL TYR GLN LEU MET ARG LYS CYS TRP GLU PHE GLN PRO
SEQRES 23 A 304 SER ASN ARG THR SER PHE GLN ASN LEU ILE GLU GLY PHE
SEQRES 24 A 304 GLU ALA LEU LEU LYS
SEQRES 1 B 304 GLY SER GLY ASP ILE VAL SER GLU LYS LYS PRO ALA THR
SEQRES 2 B 304 GLU VAL ASP PRO THR HIS PHE GLU LYS ARG PHE LEU LYS
SEQRES 3 B 304 ARG ILE ARG ASP LEU GLY GLU GLY HIS PHE GLY LYS VAL
SEQRES 4 B 304 GLU LEU CYS ARG TYR ASP PRO GLU GLY ASP ASN THR GLY
SEQRES 5 B 304 GLU GLN VAL ALA VAL LYS SER LEU LYS PRO GLU SER GLY
SEQRES 6 B 304 GLY ASN HIS ILE ALA ASP LEU LYS LYS GLU ILE GLU ILE
SEQRES 7 B 304 LEU ARG ASN LEU TYR HIS GLU ASN ILE VAL LYS TYR LYS
SEQRES 8 B 304 GLY ILE CYS THR GLU ASP GLY GLY ASN GLY ILE LYS LEU
SEQRES 9 B 304 ILE MET GLU PHE LEU PRO SER GLY SER LEU LYS GLU TYR
SEQRES 10 B 304 LEU PRO LYS ASN LYS ASN LYS ILE ASN LEU LYS GLN GLN
SEQRES 11 B 304 LEU LYS TYR ALA VAL GLN ILE CYS LYS GLY MET ASP TYR
SEQRES 12 B 304 LEU GLY SER ARG GLN TYR VAL HIS ARG ASP LEU ALA ALA
SEQRES 13 B 304 ARG ASN VAL LEU VAL GLU SER GLU HIS GLN VAL LYS ILE
SEQRES 14 B 304 GLY ASP PHE GLY LEU THR LYS ALA ILE GLU THR ASP LYS
SEQRES 15 B 304 GLU PTR PTR THR VAL LYS ASP ASP ARG ASP SER PRO VAL
SEQRES 16 B 304 PHE TRP TYR ALA PRO GLU CYS LEU MET GLN SER LYS PHE
SEQRES 17 B 304 TYR ILE ALA SER ASP VAL TRP SER PHE GLY VAL THR LEU
SEQRES 18 B 304 HIS GLU LEU LEU THR TYR CYS ASP SER ASP SER SER PRO
SEQRES 19 B 304 MET ALA LEU PHE LEU LYS MET ILE GLY PRO THR HIS GLY
SEQRES 20 B 304 GLN MET THR VAL THR ARG LEU VAL ASN THR LEU LYS GLU
SEQRES 21 B 304 GLY LYS ARG LEU PRO CYS PRO PRO ASN CYS PRO ASP GLU
SEQRES 22 B 304 VAL TYR GLN LEU MET ARG LYS CYS TRP GLU PHE GLN PRO
SEQRES 23 B 304 SER ASN ARG THR SER PHE GLN ASN LEU ILE GLU GLY PHE
SEQRES 24 B 304 GLU ALA LEU LEU LYS
MODRES 6N7A PTR A 1034 TYR MODIFIED RESIDUE
MODRES 6N7A PTR A 1035 TYR MODIFIED RESIDUE
MODRES 6N7A PTR B 1034 TYR MODIFIED RESIDUE
MODRES 6N7A PTR B 1035 TYR MODIFIED RESIDUE
HET PTR A1034 16
HET PTR A1035 16
HET PTR B1034 16
HET PTR B1035 16
HET GOL A1201 6
HET GOL A1202 6
HET KEV A1203 28
HET GOL B1201 6
HET KEV B1202 28
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM GOL GLYCEROL
HETNAM KEV N-[3-(5-CHLORO-2-METHOXYPHENYL)-1-METHYL-1H-PYRAZOL-4-
HETNAM 2 KEV YL]-2-METHYL-2H-PYRAZOLO[4,3-C]PYRIDINE-7-CARBOXAMIDE
HETSYN PTR PHOSPHONOTYROSINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 PTR 4(C9 H12 N O6 P)
FORMUL 3 GOL 3(C3 H8 O3)
FORMUL 5 KEV 2(C19 H17 CL N6 O2)
FORMUL 8 HOH *588(H2 O)
HELIX 1 AA1 GLU A 871 ARG A 873 5 3
HELIX 2 AA2 ILE A 919 ASN A 931 1 13
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 MET A 1099 GLU A 1110 1 12
HELIX 12 AB3 PRO A 1121 LYS A 1130 1 10
HELIX 13 AB4 CYS A 1131 GLU A 1133 5 3
HELIX 14 AB5 GLN A 1135 ARG A 1139 5 5
HELIX 15 AB6 SER A 1141 LYS A 1154 1 14
HELIX 16 AB7 GLU B 871 ARG B 873 5 3
HELIX 17 AB8 ILE B 919 ASN B 931 1 13
HELIX 18 AB9 SER B 963 ASN B 971 1 9
HELIX 19 AC1 ASN B 976 ARG B 997 1 22
HELIX 20 AC2 ALA B 1005 ARG B 1007 5 3
HELIX 21 AC3 PRO B 1044 TYR B 1048 5 5
HELIX 22 AC4 ALA B 1049 SER B 1056 1 8
HELIX 23 AC5 ILE B 1060 THR B 1076 1 17
HELIX 24 AC6 ASP B 1079 SER B 1082 5 4
HELIX 25 AC7 SER B 1083 GLY B 1093 1 11
HELIX 26 AC8 MET B 1099 GLU B 1110 1 12
HELIX 27 AC9 PRO B 1121 CYS B 1131 1 11
HELIX 28 AD1 GLN B 1135 ARG B 1139 5 5
HELIX 29 AD2 SER B 1141 LYS B 1154 1 14
SHEET 1 AA1 5 LEU A 875 GLU A 883 0
SHEET 2 AA1 5 GLY A 887 TYR A 894 -1 O LEU A 891 N ILE A 878
SHEET 3 AA1 5 GLU A 903 LEU A 910 -1 O GLU A 903 N TYR A 894
SHEET 4 AA1 5 LYS A 953 GLU A 957 -1 O MET A 956 N ALA A 906
SHEET 5 AA1 5 TYR A 940 CYS A 944 -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 GLU B 883 0
SHEET 2 AA5 5 GLY B 887 TYR B 894 -1 O LEU B 891 N ARG B 879
SHEET 3 AA5 5 GLU B 903 LEU B 910 -1 O VAL B 905 N CYS B 892
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 GLY B 942 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 1.32
LINK C PTR A1034 N PTR A1035 1555 1555 1.35
LINK C PTR A1035 N THR A1036 1555 1555 1.34
LINK C GLU B1033 N PTR B1034 1555 1555 1.33
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 6 LYS A 872 LEU A 875 GLU A 890 CYS A 892
SITE 2 AC1 6 VAL A 907 LYS A 953
SITE 1 AC2 9 ASP A 921 LYS A 924 GLY A1023 LEU A1024
SITE 2 AC2 9 THR A1025 LYS A1026 HOH A1428 HOH A1439
SITE 3 AC2 9 HOH A1514
SITE 1 AC3 17 LEU A 881 GLY A 882 GLY A 887 VAL A 889
SITE 2 AC3 17 ALA A 906 MET A 956 GLU A 957 LEU A 959
SITE 3 AC3 17 GLY A 962 GLU A 966 ARG A1007 LEU A1010
SITE 4 AC3 17 GLY A1020 ASP A1021 HOH A1362 HOH A1395
SITE 5 AC3 17 HOH A1425
SITE 1 AC4 9 ASP B 921 LYS B 924 GLY B1023 LEU B1024
SITE 2 AC4 9 THR B1025 LYS B1026 HOH B1374 HOH B1486
SITE 3 AC4 9 HOH B1511
SITE 1 AC5 16 LEU B 881 GLY B 882 GLY B 884 GLY B 887
SITE 2 AC5 16 VAL B 889 ALA B 906 MET B 956 GLU B 957
SITE 3 AC5 16 LEU B 959 GLU B 966 ARG B1007 LEU B1010
SITE 4 AC5 16 GLY B1020 ASP B1021 HOH B1324 HOH B1406
CRYST1 42.720 173.230 45.060 90.00 94.17 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 0.023408 0.000000 0.001707 0.00000
SCALE2 0.000000 0.005773 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022252 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
