HEADER CHAPERONE 11-APR-16 5J9X
TITLE HSP90 IN COMPLEX WITH N-BUTYL-5-[4-(2-FLUORO-PHENYL)-5-OXO-4,5-
TITLE 2 DIHYDRO-1H-[1,2,4]TRIAZOL-3-YL]-2,4-DIHYDROXY-N-METHYL-BENZAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HEAT SHOCK 86 KDA,HSP86,LIPOPOLYSACCHARIDE-ASSOCIATED
COMPND 5 PROTEIN 2,LPS-ASSOCIATED PROTEIN 2,RENAL CARCINOMA ANTIGEN NY-REN-38;
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: HSP90AA1, HSP90A, HSPC1, HSPCA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS INHIBITOR, CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.AMARAL,P.MATIAS
REVDAT 3 10-JAN-24 5J9X 1 REMARK
REVDAT 2 24-JAN-18 5J9X 1 JRNL
REVDAT 1 06-DEC-17 5J9X 0
JRNL AUTH M.AMARAL,D.B.KOKH,J.BOMKE,A.WEGENER,H.P.BUCHSTALLER,
JRNL AUTH 2 H.M.EGGENWEILER,P.MATIAS,C.SIRRENBERG,R.C.WADE,M.FRECH
JRNL TITL PROTEIN CONFORMATIONAL FLEXIBILITY MODULATES KINETICS AND
JRNL TITL 2 THERMODYNAMICS OF DRUG BINDING.
JRNL REF NAT COMMUN V. 8 2276 2017
JRNL REFN ESSN 2041-1723
JRNL PMID 29273709
JRNL DOI 10.1038/S41467-017-02258-W
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.63
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.9
REMARK 3 NUMBER OF REFLECTIONS : 25976
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1301
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 36.6390 - 3.7431 0.99 3168 167 0.1366 0.1671
REMARK 3 2 3.7431 - 2.9714 0.99 3046 161 0.1547 0.2172
REMARK 3 3 2.9714 - 2.5959 0.98 2960 156 0.1816 0.2480
REMARK 3 4 2.5959 - 2.3586 1.00 3049 160 0.1815 0.2303
REMARK 3 5 2.3586 - 2.1896 0.94 2851 151 0.2283 0.2804
REMARK 3 6 2.1896 - 2.0605 0.86 2598 138 0.2939 0.3152
REMARK 3 7 2.0605 - 1.9573 0.92 2785 147 0.3545 0.4459
REMARK 3 8 1.9573 - 1.8721 0.51 1424 74 0.5610 0.5797
REMARK 3 9 1.8721 - 1.8000 0.99 2794 147 0.4701 0.5395
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.670
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.012 1696
REMARK 3 ANGLE : 1.416 2289
REMARK 3 CHIRALITY : 0.057 258
REMARK 3 PLANARITY : 0.007 292
REMARK 3 DIHEDRAL : 13.302 1010
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 16 THROUGH 40 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.1793 27.6160 -18.0479
REMARK 3 T TENSOR
REMARK 3 T11: 0.2597 T22: 0.3764
REMARK 3 T33: 0.2947 T12: 0.0506
REMARK 3 T13: -0.0287 T23: -0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 1.4294 L22: 0.8687
REMARK 3 L33: 0.4790 L12: -0.1724
REMARK 3 L13: -0.0049 L23: 0.2290
REMARK 3 S TENSOR
REMARK 3 S11: 0.0754 S12: -0.1226 S13: 0.0154
REMARK 3 S21: 0.0421 S22: 0.1949 S23: -0.0822
REMARK 3 S31: 0.0149 S32: 0.3123 S33: -0.0002
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 41 THROUGH 105 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5700 33.7076 -24.7801
REMARK 3 T TENSOR
REMARK 3 T11: 0.2250 T22: 0.2698
REMARK 3 T33: 0.2530 T12: 0.0123
REMARK 3 T13: -0.0475 T23: -0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 1.4622 L22: 1.8485
REMARK 3 L33: 1.7640 L12: -0.2416
REMARK 3 L13: -0.4671 L23: 0.7451
REMARK 3 S TENSOR
REMARK 3 S11: 0.0387 S12: 0.2651 S13: 0.0641
REMARK 3 S21: -0.2950 S22: -0.1092 S23: 0.1776
REMARK 3 S31: -0.0229 S32: -0.1805 S33: -0.0005
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 106 THROUGH 136 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6775 39.4751 -15.0543
REMARK 3 T TENSOR
REMARK 3 T11: 0.2480 T22: 0.4643
REMARK 3 T33: 0.4851 T12: -0.0544
REMARK 3 T13: -0.0105 T23: -0.0959
REMARK 3 L TENSOR
REMARK 3 L11: 1.1732 L22: 0.8643
REMARK 3 L33: 1.1586 L12: -0.7625
REMARK 3 L13: 0.3252 L23: -0.5432
REMARK 3 S TENSOR
REMARK 3 S11: -0.0240 S12: -0.0030 S13: 1.2099
REMARK 3 S21: 0.0425 S22: -0.0755 S23: -0.3078
REMARK 3 S31: -0.0926 S32: 0.9463 S33: -0.1222
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 137 THROUGH 190 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6523 25.5733 -26.9420
REMARK 3 T TENSOR
REMARK 3 T11: 0.2301 T22: 0.3009
REMARK 3 T33: 0.2829 T12: 0.0156
REMARK 3 T13: -0.0127 T23: -0.0613
REMARK 3 L TENSOR
REMARK 3 L11: 1.4921 L22: 1.3228
REMARK 3 L33: 1.2679 L12: -0.1450
REMARK 3 L13: -1.3201 L23: 0.5113
REMARK 3 S TENSOR
REMARK 3 S11: -0.0615 S12: 0.3947 S13: -0.2114
REMARK 3 S21: -0.1565 S22: -0.0216 S23: 0.0194
REMARK 3 S31: 0.1846 S32: -0.0528 S33: -0.0004
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 191 THROUGH 210 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.0259 25.7917 -6.9084
REMARK 3 T TENSOR
REMARK 3 T11: 0.3396 T22: 0.3334
REMARK 3 T33: 0.2762 T12: -0.0006
REMARK 3 T13: 0.0099 T23: 0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 0.4064 L22: 0.4164
REMARK 3 L33: 0.7992 L12: 0.0210
REMARK 3 L13: 0.0654 L23: 0.1065
REMARK 3 S TENSOR
REMARK 3 S11: -0.1348 S12: -0.4850 S13: -0.0876
REMARK 3 S21: 0.1035 S22: -0.0082 S23: 0.0611
REMARK 3 S31: 0.2282 S32: -0.3352 S33: -0.0047
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 211 THROUGH 223 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.0440 33.1990 -15.5185
REMARK 3 T TENSOR
REMARK 3 T11: 0.2492 T22: 0.4483
REMARK 3 T33: 0.3644 T12: 0.0057
REMARK 3 T13: 0.0025 T23: 0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 0.1853 L22: 1.0570
REMARK 3 L33: 2.2836 L12: -0.1730
REMARK 3 L13: -0.0159 L23: -1.3220
REMARK 3 S TENSOR
REMARK 3 S11: -0.1269 S12: -0.5806 S13: -0.0118
REMARK 3 S21: 0.8143 S22: 0.1728 S23: 0.1704
REMARK 3 S31: -0.6892 S32: -0.4803 S33: 0.0014
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 5J9X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220219.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-MAR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
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 PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28122
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 45.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 5.980
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.63
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1YES
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM FLUORIDE 0.1 M BIS TRIS
REMARK 280 PROPANE PH 8.5 20 % W/V PEG 3350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 33.94700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 45.66700
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 49.48200
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 33.94700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 45.66700
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 49.48200
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 33.94700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 45.66700
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 49.48200
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 33.94700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 45.66700
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 49.48200
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: DIMERIC
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 91.33400
REMARK 350 BIOMT3 2 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 ASP A 9
REMARK 465 GLN A 10
REMARK 465 PRO A 11
REMARK 465 MET A 12
REMARK 465 GLU A 13
REMARK 465 GLU A 14
REMARK 465 GLU A 15
REMARK 465 LYS A 224
REMARK 465 GLU A 225
REMARK 465 ARG A 226
REMARK 465 ASP A 227
REMARK 465 LYS A 228
REMARK 465 GLU A 229
REMARK 465 VAL A 230
REMARK 465 SER A 231
REMARK 465 ASP A 232
REMARK 465 ASP A 233
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 16 CD
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 HG1 THR A 152 HG1 THR A 184 1.30
REMARK 500 O HOH A 469 O HOH A 544 1.98
REMARK 500 O HOH A 485 O HOH A 556 2.06
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 ASP A 66 79.36 -166.12
REMARK 500 ALA A 124 22.92 -71.30
REMARK 500 ARG A 182 132.46 -171.31
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 6GC A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 302
DBREF 5J9X A 9 233 UNP P07900 HS90A_HUMAN 131 355
SEQRES 1 A 225 ASP GLN PRO MET GLU GLU GLU GLU VAL GLU THR PHE ALA
SEQRES 2 A 225 PHE GLN ALA GLU ILE ALA GLN LEU MET SER LEU ILE ILE
SEQRES 3 A 225 ASN THR PHE TYR SER ASN LYS GLU ILE PHE LEU ARG GLU
SEQRES 4 A 225 LEU ILE SER ASN SER SER ASP ALA LEU ASP LYS ILE ARG
SEQRES 5 A 225 TYR GLU SER LEU THR ASP PRO SER LYS LEU ASP SER GLY
SEQRES 6 A 225 LYS GLU LEU HIS ILE ASN LEU ILE PRO ASN LYS GLN ASP
SEQRES 7 A 225 ARG THR LEU THR ILE VAL ASP THR GLY ILE GLY MET THR
SEQRES 8 A 225 LYS ALA ASP LEU ILE ASN ASN LEU GLY THR ILE ALA LYS
SEQRES 9 A 225 SER GLY THR LYS ALA PHE MET GLU ALA LEU GLN ALA GLY
SEQRES 10 A 225 ALA ASP ILE SER MET ILE GLY GLN PHE GLY VAL GLY PHE
SEQRES 11 A 225 TYR SER ALA TYR LEU VAL ALA GLU LYS VAL THR VAL ILE
SEQRES 12 A 225 THR LYS HIS ASN ASP ASP GLU GLN TYR ALA TRP GLU SER
SEQRES 13 A 225 SER ALA GLY GLY SER PHE THR VAL ARG THR ASP THR GLY
SEQRES 14 A 225 GLU PRO MET GLY ARG GLY THR LYS VAL ILE LEU HIS LEU
SEQRES 15 A 225 LYS GLU ASP GLN THR GLU TYR LEU GLU GLU ARG ARG ILE
SEQRES 16 A 225 LYS GLU ILE VAL LYS LYS HIS SER GLN PHE ILE GLY TYR
SEQRES 17 A 225 PRO ILE THR LEU PHE VAL GLU LYS GLU ARG ASP LYS GLU
SEQRES 18 A 225 VAL SER ASP ASP
HET 6GC A 301 50
HET DMS A 302 10
HETNAM 6GC N-BUTYL-5-[4-(2-FLUOROPHENYL)-5-OXO-4,5-DIHYDRO-1H-1,2,
HETNAM 2 6GC 4-TRIAZOL-3-YL]-2,4-DIHYDROXY-N-METHYLBENZAMIDE
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 2 6GC C20 H21 F N4 O4
FORMUL 3 DMS C2 H6 O S
FORMUL 4 HOH *169(H2 O)
HELIX 1 AA1 GLN A 23 THR A 36 1 14
HELIX 2 AA2 GLU A 42 THR A 65 1 24
HELIX 3 AA3 ASP A 66 ASP A 71 5 6
HELIX 4 AA4 THR A 99 ASN A 105 1 7
HELIX 5 AA5 ASN A 105 ALA A 124 1 20
HELIX 6 AA6 ASP A 127 GLY A 135 5 9
HELIX 7 AA7 VAL A 136 LEU A 143 5 8
HELIX 8 AA8 GLU A 192 LEU A 198 5 7
HELIX 9 AA9 GLU A 199 SER A 211 1 13
SHEET 1 AA1 8 GLU A 18 ALA A 21 0
SHEET 2 AA1 8 SER A 169 THR A 174 -1 O PHE A 170 N PHE A 20
SHEET 3 AA1 8 TYR A 160 SER A 164 -1 N ALA A 161 O ARG A 173
SHEET 4 AA1 8 ALA A 145 LYS A 153 -1 N VAL A 150 O TRP A 162
SHEET 5 AA1 8 GLY A 183 LEU A 190 -1 O ILE A 187 N THR A 149
SHEET 6 AA1 8 THR A 88 ASP A 93 -1 N ASP A 93 O THR A 184
SHEET 7 AA1 8 ILE A 78 ASN A 83 -1 N ASN A 79 O VAL A 92
SHEET 8 AA1 8 ILE A 218 LEU A 220 1 O THR A 219 N LEU A 80
SITE 1 AC1 14 ASN A 51 ALA A 55 LYS A 58 ASP A 93
SITE 2 AC1 14 ILE A 96 GLY A 97 MET A 98 LEU A 107
SITE 3 AC1 14 PHE A 138 THR A 184 VAL A 186 HOH A 436
SITE 4 AC1 14 HOH A 460 HOH A 475
SITE 1 AC2 4 HIS A 77 ASN A 79 SER A 169 HOH A 413
CRYST1 67.894 91.334 98.964 90.00 90.00 90.00 I 2 2 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 0.014729 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010949 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010105 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
