HEADER TRANSFERASE/TRANSFERASE INHIBITOR 17-JUL-13 3WF7
TITLE CRYSTAL STRUCTURE OF S6K1 KINASE DOMAIN IN COMPLEX WITH A PURINE
TITLE 2 DERIVATIVE 1-(9H-PURIN-6-YL)-N-[3-(TRIFLUOROMETHYL)PHENYL]PIPERIDINE-
TITLE 3 4-CARBOXAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBOSOMAL PROTEIN S6 KINASE BETA-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 78-399;
COMPND 5 SYNONYM: S6K-BETA-1, S6K1, 70 KDA RIBOSOMAL PROTEIN S6 KINASE 1,
COMPND 6 RIBOSOMAL PROTEIN S6 KINASE I, SERINE/THREONINE-PROTEIN KINASE 14A,
COMPND 7 P70 RIBOSOMAL S6 KINASE ALPHA;
COMPND 8 EC: 2.7.11.1;
COMPND 9 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: RPS6KB1;
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 SERINE/THREONINE PROTEIN KINASE DOMAIN, TRANSFERASE, PHOSPHORYLATION,
KEYWDS 2 ATP-BINDING, ZINC-BINDING, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.NIWA,M.SHIROUZU,S.YOKOYAMA
REVDAT 3 29-OCT-14 3WF7 1 JRNL
REVDAT 2 13-AUG-14 3WF7 1 JRNL
REVDAT 1 06-AUG-14 3WF7 0
JRNL AUTH H.NIWA,J.MIKUNI,S.SASAKI,Y.TOMABECHI,K.HONDA,M.IKEDA,
JRNL AUTH 2 N.OHSAWA,M.WAKIYAMA,N.HANDA,M.SHIROUZU,T.HONMA,A.TANAKA,
JRNL AUTH 3 S.YOKOYAMA
JRNL TITL CRYSTAL STRUCTURES OF THE S6K1 KINASE DOMAIN IN COMPLEXES
JRNL TITL 2 WITH INHIBITORS
JRNL REF J.STRUCT.FUNCT.GENOM. V. 15 153 2014
JRNL REFN ISSN 1345-711X
JRNL PMID 25078151
JRNL DOI 10.1007/S10969-014-9188-8
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1690)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.10
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.170
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 31266
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 2919
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.1174 - 5.1014 1.00 2666 113 0.1823 0.2458
REMARK 3 2 5.1014 - 4.0497 1.00 2614 139 0.1388 0.1775
REMARK 3 3 4.0497 - 3.5380 1.00 2652 125 0.1339 0.2002
REMARK 3 4 3.5380 - 3.2146 1.00 2631 129 0.1686 0.2266
REMARK 3 5 3.2146 - 2.9842 1.00 2629 127 0.1873 0.2834
REMARK 3 6 2.9842 - 2.8083 1.00 2617 163 0.1836 0.2318
REMARK 3 7 2.8083 - 2.6676 1.00 2618 141 0.1740 0.1936
REMARK 3 8 2.6676 - 2.5515 1.00 2635 148 0.1770 0.2468
REMARK 3 9 2.5515 - 2.4533 1.00 2614 142 0.1776 0.2294
REMARK 3 10 2.4533 - 2.3686 1.00 2608 167 0.1685 0.2038
REMARK 3 11 2.3686 - 2.2946 1.00 2639 129 0.1710 0.2146
REMARK 3 12 2.2946 - 2.2290 1.00 2585 164 0.1766 0.2275
REMARK 3 13 2.2290 - 2.1703 1.00 2622 122 0.1817 0.2235
REMARK 3 14 2.1703 - 2.1174 1.00 2662 131 0.1812 0.2247
REMARK 3 15 2.1174 - 2.0692 1.00 2594 165 0.1964 0.2207
REMARK 3 16 2.0692 - 2.0252 1.00 2685 104 0.2057 0.2504
REMARK 3 17 2.0252 - 1.9847 1.00 2600 138 0.2193 0.2322
REMARK 3 18 1.9847 - 1.9472 1.00 2662 148 0.2347 0.3101
REMARK 3 19 1.9472 - 1.9124 1.00 2590 147 0.2450 0.2796
REMARK 3 20 1.9124 - 1.8800 1.00 2615 148 0.2727 0.2731
REMARK 3 21 1.8800 - 1.8497 1.00 2637 129 0.3004 0.3287
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.120
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 2399
REMARK 3 ANGLE : 0.967 3235
REMARK 3 CHIRALITY : 0.041 346
REMARK 3 PLANARITY : 0.005 408
REMARK 3 DIHEDRAL : 16.948 919
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 83:179 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3748 -5.9565 9.7449
REMARK 3 T TENSOR
REMARK 3 T11: 0.3285 T22: 0.3394
REMARK 3 T33: 0.2431 T12: 0.0214
REMARK 3 T13: 0.0078 T23: 0.0306
REMARK 3 L TENSOR
REMARK 3 L11: 2.1770 L22: 3.9794
REMARK 3 L33: 3.8326 L12: -0.3909
REMARK 3 L13: 0.6427 L23: 1.0694
REMARK 3 S TENSOR
REMARK 3 S11: 0.0649 S12: 0.5751 S13: 0.2762
REMARK 3 S21: -0.6938 S22: -0.1207 S23: 0.0304
REMARK 3 S31: -0.6867 S32: 0.0443 S33: 0.0508
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 180:374 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0202 -27.8692 3.2354
REMARK 3 T TENSOR
REMARK 3 T11: 0.2150 T22: 0.1529
REMARK 3 T33: 0.2012 T12: -0.0199
REMARK 3 T13: -0.0327 T23: -0.0498
REMARK 3 L TENSOR
REMARK 3 L11: 2.6341 L22: 2.1900
REMARK 3 L33: 5.1860 L12: -1.0057
REMARK 3 L13: -1.1170 L23: 0.9753
REMARK 3 S TENSOR
REMARK 3 S11: 0.0051 S12: -0.0685 S13: 0.1817
REMARK 3 S21: -0.0314 S22: -0.0215 S23: -0.0173
REMARK 3 S31: -0.0145 S32: 0.1515 S33: 0.0462
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3WF7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-JUL-13.
REMARK 100 THE RCSB ID CODE IS RCSB096259.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95369
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31350
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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 (%): 47.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, 3.7-3.9M SODIUM
REMARK 280 FORMATE, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.82450
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 34.71900
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.71900
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 36.41225
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.71900
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 34.71900
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 109.23675
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.71900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.71900
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 36.41225
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 34.71900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.71900
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 109.23675
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 72.82450
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 GLY A 71
REMARK 465 SER A 72
REMARK 465 PHE A 73
REMARK 465 THR A 74
REMARK 465 SER A 75
REMARK 465 SER A 76
REMARK 465 GLY A 77
REMARK 465 SER A 78
REMARK 465 VAL A 79
REMARK 465 ASN A 80
REMARK 465 ARG A 81
REMARK 465 GLY A 82
REMARK 465 GLY A 247
REMARK 465 THR A 248
REMARK 465 VAL A 249
REMARK 465 SER A 375
REMARK 465 GLU A 376
REMARK 465 GLU A 377
REMARK 465 ASP A 378
REMARK 465 VAL A 379
REMARK 465 SER A 380
REMARK 465 GLN A 381
REMARK 465 PHE A 382
REMARK 465 ASP A 383
REMARK 465 SER A 384
REMARK 465 LYS A 385
REMARK 465 PHE A 386
REMARK 465 THR A 387
REMARK 465 ARG A 388
REMARK 465 GLN A 389
REMARK 465 THR A 390
REMARK 465 PRO A 391
REMARK 465 VAL A 392
REMARK 465 ASP A 393
REMARK 465 SER A 394
REMARK 465 PRO A 395
REMARK 465 ASP A 396
REMARK 465 ASP A 397
REMARK 465 SER A 398
REMARK 465 THR A 399
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 ARG A 132 NE CZ NH1 NH2
REMARK 470 LYS A 135 CG CD CE NZ
REMARK 470 ILE A 244 CG1 CG2 CD1
REMARK 470 LYS A 364 CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 724 O HOH A 726 2.02
REMARK 500 O HOH A 659 O HOH A 667 2.10
REMARK 500 O2 GOL A 403 O HOH A 539 2.14
REMARK 500 OG1 THR A 250 O3P TPO A 252 2.15
REMARK 500 O HOH A 636 O HOH A 685 2.16
REMARK 500
REMARK 500 REMARK: NULL
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 ASN A 115 38.03 -92.68
REMARK 500 ARG A 132 -74.98 -63.45
REMARK 500 LYS A 135 -50.26 -123.08
REMARK 500 ASP A 136 97.85 -163.41
REMARK 500 ARG A 217 -48.65 77.10
REMARK 500 LEU A 219 30.71 -98.25
REMARK 500 HIS A 245 -149.73 -81.36
REMARK 500 ASN A 331 98.81 -69.92
REMARK 500 ASP A 342 -120.28 46.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 251 ND1
REMARK 620 2 HIS A 245 ND1 112.2
REMARK 620 3 CYS A 240 SG 108.0 118.8
REMARK 620 4 CYS A 254 SG 107.8 97.4 111.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FS9 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WE4 RELATED DB: PDB
REMARK 900 RELATED ID: 3WF5 RELATED DB: PDB
REMARK 900 RELATED ID: 3WF6 RELATED DB: PDB
REMARK 900 RELATED ID: 3WF8 RELATED DB: PDB
REMARK 900 RELATED ID: 3WF9 RELATED DB: PDB
DBREF 3WF7 A 78 399 UNP P23443 KS6B1_HUMAN 78 399
SEQADV 3WF7 GLY A 71 UNP P23443 EXPRESSION TAG
SEQADV 3WF7 SER A 72 UNP P23443 EXPRESSION TAG
SEQADV 3WF7 PHE A 73 UNP P23443 EXPRESSION TAG
SEQADV 3WF7 THR A 74 UNP P23443 EXPRESSION TAG
SEQADV 3WF7 SER A 75 UNP P23443 EXPRESSION TAG
SEQADV 3WF7 SER A 76 UNP P23443 EXPRESSION TAG
SEQADV 3WF7 GLY A 77 UNP P23443 EXPRESSION TAG
SEQRES 1 A 329 GLY SER PHE THR SER SER GLY SER VAL ASN ARG GLY PRO
SEQRES 2 A 329 GLU LYS ILE ARG PRO GLU CYS PHE GLU LEU LEU ARG VAL
SEQRES 3 A 329 LEU GLY LYS GLY GLY TYR GLY LYS VAL PHE GLN VAL ARG
SEQRES 4 A 329 LYS VAL THR GLY ALA ASN THR GLY LYS ILE PHE ALA MET
SEQRES 5 A 329 LYS VAL LEU LYS LYS ALA MET ILE VAL ARG ASN ALA LYS
SEQRES 6 A 329 ASP THR ALA HIS THR LYS ALA GLU ARG ASN ILE LEU GLU
SEQRES 7 A 329 GLU VAL LYS HIS PRO PHE ILE VAL ASP LEU ILE TYR ALA
SEQRES 8 A 329 PHE GLN THR GLY GLY LYS LEU TYR LEU ILE LEU GLU TYR
SEQRES 9 A 329 LEU SER GLY GLY GLU LEU PHE MET GLN LEU GLU ARG GLU
SEQRES 10 A 329 GLY ILE PHE MET GLU ASP THR ALA CYS PHE TYR LEU ALA
SEQRES 11 A 329 GLU ILE SER MET ALA LEU GLY HIS LEU HIS GLN LYS GLY
SEQRES 12 A 329 ILE ILE TYR ARG ASP LEU LYS PRO GLU ASN ILE MET LEU
SEQRES 13 A 329 ASN HIS GLN GLY HIS VAL LYS LEU THR ASP PHE GLY LEU
SEQRES 14 A 329 CYS LYS GLU SER ILE HIS ASP GLY THR VAL THR HIS TPO
SEQRES 15 A 329 PHE CYS GLY THR ILE GLU TYR MET ALA PRO GLU ILE LEU
SEQRES 16 A 329 MET ARG SER GLY HIS ASN ARG ALA VAL ASP TRP TRP SER
SEQRES 17 A 329 LEU GLY ALA LEU MET TYR ASP MET LEU THR GLY ALA PRO
SEQRES 18 A 329 PRO PHE THR GLY GLU ASN ARG LYS LYS THR ILE ASP LYS
SEQRES 19 A 329 ILE LEU LYS CYS LYS LEU ASN LEU PRO PRO TYR LEU THR
SEQRES 20 A 329 GLN GLU ALA ARG ASP LEU LEU LYS LYS LEU LEU LYS ARG
SEQRES 21 A 329 ASN ALA ALA SER ARG LEU GLY ALA GLY PRO GLY ASP ALA
SEQRES 22 A 329 GLY GLU VAL GLN ALA HIS PRO PHE PHE ARG HIS ILE ASN
SEQRES 23 A 329 TRP GLU GLU LEU LEU ALA ARG LYS VAL GLU PRO PRO PHE
SEQRES 24 A 329 LYS PRO LEU LEU GLN SER GLU GLU ASP VAL SER GLN PHE
SEQRES 25 A 329 ASP SER LYS PHE THR ARG GLN THR PRO VAL ASP SER PRO
SEQRES 26 A 329 ASP ASP SER THR
MODRES 3WF7 TPO A 252 THR PHOSPHOTHREONINE
HET TPO A 252 11
HET ZN A 401 1
HET FS9 A 402 28
HET GOL A 403 6
HETNAM TPO PHOSPHOTHREONINE
HETNAM ZN ZINC ION
HETNAM FS9 1-(9H-PURIN-6-YL)-N-[3-(TRIFLUOROMETHYL)
HETNAM 2 FS9 PHENYL]PIPERIDINE-4-CARBOXAMIDE
HETNAM GOL GLYCEROL
HETSYN TPO PHOSPHONOTHREONINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 2 ZN ZN 2+
FORMUL 3 FS9 C18 H17 F3 N6 O
FORMUL 4 GOL C3 H8 O3
FORMUL 5 HOH *226(H2 O)
HELIX 1 1 ARG A 87 GLU A 89 5 3
HELIX 2 2 LYS A 127 ASN A 133 1 7
HELIX 3 3 ASP A 136 VAL A 150 1 15
HELIX 4 4 GLU A 179 GLY A 188 1 10
HELIX 5 5 MET A 191 GLY A 213 1 23
HELIX 6 6 LYS A 220 GLU A 222 5 3
HELIX 7 7 ALA A 261 MET A 266 1 6
HELIX 8 8 ARG A 272 GLY A 289 1 18
HELIX 9 9 ASN A 297 CYS A 308 1 12
HELIX 10 10 THR A 317 LEU A 328 1 12
HELIX 11 11 ASN A 331 ARG A 335 5 5
HELIX 12 12 ASP A 342 ALA A 348 1 7
HELIX 13 13 HIS A 349 ARG A 353 5 5
HELIX 14 14 ASN A 356 ALA A 362 1 7
SHEET 1 A 5 PHE A 91 LYS A 99 0
SHEET 2 A 5 GLY A 103 LYS A 110 -1 O VAL A 105 N LEU A 97
SHEET 3 A 5 ILE A 119 LYS A 126 -1 O MET A 122 N PHE A 106
SHEET 4 A 5 LYS A 167 GLU A 173 -1 O LEU A 172 N ALA A 121
SHEET 5 A 5 LEU A 158 THR A 164 -1 N PHE A 162 O TYR A 169
SHEET 1 B 2 ILE A 224 LEU A 226 0
SHEET 2 B 2 VAL A 232 LEU A 234 -1 O LYS A 233 N MET A 225
LINK C HIS A 251 N TPO A 252 1555 1555 1.33
LINK C TPO A 252 N PHE A 253 1555 1555 1.33
LINK ND1 HIS A 251 ZN ZN A 401 1555 1555 2.23
LINK ND1 HIS A 245 ZN ZN A 401 1555 1555 2.32
LINK SG CYS A 240 ZN ZN A 401 1555 1555 2.49
LINK SG CYS A 254 ZN ZN A 401 1555 1555 2.52
SITE 1 AC1 4 CYS A 240 HIS A 245 HIS A 251 CYS A 254
SITE 1 AC2 18 LYS A 99 GLY A 100 TYR A 102 GLY A 103
SITE 2 AC2 18 LYS A 104 VAL A 105 ALA A 121 LYS A 123
SITE 3 AC2 18 LEU A 125 VAL A 156 GLU A 173 TYR A 174
SITE 4 AC2 18 LEU A 175 MET A 225 LYS A 241 HOH A 560
SITE 5 AC2 18 HOH A 563 HOH A 696
SITE 1 AC3 8 TYR A 174 SER A 176 LYS A 329 ASN A 331
SITE 2 AC3 8 SER A 334 HOH A 539 HOH A 595 HOH A 600
CRYST1 69.438 69.438 145.649 90.00 90.00 90.00 P 41 21 2 8
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 0.014401 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014401 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006866 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
