HEADER CHAPERONE/CHAPERONE INHIBITOR 18-JUN-13 4L93
TITLE CRYSTAL STRUCTURE OF HUMAN HSP90 WITH S36
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 9-236;
COMPND 5 SYNONYM: HEAT SHOCK 86 KDA, HSP 86, HSP86, RENAL CARCINOMA ANTIGEN
COMPND 6 NY-REN-38;
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: HSP90AA1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ATP HYDROLYSIS, HSP90N-HSP90N INHIBITOR COMPLEX, CHAPERONE-CHAPERONE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LI,J.REN,M.YANG,B.XIONG,J.HE
REVDAT 2 08-NOV-23 4L93 1 REMARK
REVDAT 1 18-JUN-14 4L93 0
JRNL AUTH J.LI,J.REN,M.YANG,B.XIONG,J.HE
JRNL TITL CRYSTAL STRUCTURE OF HUMAN HSP90 WITH S36
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.2_432)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.56
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 3 NUMBER OF REFLECTIONS : 45118
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.110
REMARK 3 FREE R VALUE TEST SET COUNT : 1853
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 30.5659 - 3.9723 0.97 4827 207 0.1993 0.2086
REMARK 3 2 3.9723 - 3.1540 0.99 4704 203 0.2119 0.2555
REMARK 3 3 3.1540 - 2.7556 0.95 4481 191 0.2439 0.2575
REMARK 3 4 2.7556 - 2.5038 0.94 4406 189 0.2531 0.2838
REMARK 3 5 2.5038 - 2.3244 0.93 4362 186 0.2387 0.3126
REMARK 3 6 2.3244 - 2.1874 0.92 4300 182 0.2165 0.2687
REMARK 3 7 2.1874 - 2.0779 0.94 4371 187 0.2205 0.2800
REMARK 3 8 2.0779 - 1.9874 0.91 4225 188 0.2330 0.2967
REMARK 3 9 1.9874 - 1.9109 0.85 3977 168 0.2471 0.3228
REMARK 3 10 1.9109 - 1.8450 0.78 3612 152 0.2612 0.3379
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 40.77
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.39170
REMARK 3 B22 (A**2) : 6.05260
REMARK 3 B33 (A**2) : -0.66090
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 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 : 0.006 3354
REMARK 3 ANGLE : 1.022 4528
REMARK 3 CHIRALITY : 0.072 514
REMARK 3 PLANARITY : 0.006 574
REMARK 3 DIHEDRAL : 14.311 1244
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 1.2348 -14.1864 -24.3651
REMARK 3 T TENSOR
REMARK 3 T11: 0.1291 T22: 0.1411
REMARK 3 T33: 0.1237 T12: 0.0072
REMARK 3 T13: -0.0092 T23: -0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 0.1947 L22: 0.1582
REMARK 3 L33: 0.3920 L12: 0.0296
REMARK 3 L13: 0.0830 L23: 0.1511
REMARK 3 S TENSOR
REMARK 3 S11: 0.0638 S12: 0.0710 S13: -0.0308
REMARK 3 S21: -0.0398 S22: -0.0077 S23: -0.0157
REMARK 3 S31: -0.0211 S32: 0.0176 S33: -0.0440
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 4L93 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-JUN-13.
REMARK 100 THE DEPOSITION ID IS D_1000080335.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
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 : 49026
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.845
REMARK 200 RESOLUTION RANGE LOW (A) : 30.562
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
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: PHENIX
REMARK 200 STARTING MODEL: 3T0Z
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%-25%(W/V) PEG 2000 MONOMETHYL
REMARK 280 ETHER, 200MM MAGNESIUM CHLORIDE, 100MM SODIUM CACODYLATE, PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z
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 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 32.15950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.41500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.15950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.41500
REMARK 290 SMTRY3 4 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: 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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
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 GLU A 16
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 465 GLU A 234
REMARK 465 ALA A 235
REMARK 465 GLU A 236
REMARK 465 ASP B 9
REMARK 465 GLN B 10
REMARK 465 PRO B 11
REMARK 465 MET B 12
REMARK 465 GLU B 13
REMARK 465 GLU B 14
REMARK 465 GLU B 15
REMARK 465 GLU B 16
REMARK 465 LYS B 224
REMARK 465 GLU B 225
REMARK 465 ARG B 226
REMARK 465 ASP B 227
REMARK 465 LYS B 228
REMARK 465 GLU B 229
REMARK 465 VAL B 230
REMARK 465 SER B 231
REMARK 465 ASP B 232
REMARK 465 ASP B 233
REMARK 465 GLU B 234
REMARK 465 ALA B 235
REMARK 465 GLU B 236
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2 ARG B 60 CD1 ILE B 110 2555 1.54
REMARK 500 CZ ARG B 60 OG SER B 113 2555 2.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 196 CB GLU A 196 CG -0.141
REMARK 500 GLU B 196 CB GLU B 196 CG -0.168
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU B 103 CB - CG - CD2 ANGL. DEV. = -11.2 DEGREES
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 TYR A 38 109.56 -162.00
REMARK 500 ASP A 66 87.68 -152.21
REMARK 500 ALA A 111 -132.98 56.93
REMARK 500 ALA A 166 -145.82 64.38
REMARK 500 GLU A 178 102.70 1.10
REMARK 500 TYR B 38 109.03 -161.71
REMARK 500 ILE B 110 55.48 -91.83
REMARK 500 ALA B 166 -142.50 64.46
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 S36 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S36 B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4L8Z RELATED DB: PDB
REMARK 900 RELATED ID: 4L90 RELATED DB: PDB
REMARK 900 RELATED ID: 4L91 RELATED DB: PDB
REMARK 900 RELATED ID: 4L94 RELATED DB: PDB
DBREF 4L93 A 9 236 UNP P07900 HS90A_HUMAN 9 236
DBREF 4L93 B 9 236 UNP P07900 HS90A_HUMAN 9 236
SEQRES 1 A 228 ASP GLN PRO MET GLU GLU GLU GLU VAL GLU THR PHE ALA
SEQRES 2 A 228 PHE GLN ALA GLU ILE ALA GLN LEU MET SER LEU ILE ILE
SEQRES 3 A 228 ASN THR PHE TYR SER ASN LYS GLU ILE PHE LEU ARG GLU
SEQRES 4 A 228 LEU ILE SER ASN SER SER ASP ALA LEU ASP LYS ILE ARG
SEQRES 5 A 228 TYR GLU SER LEU THR ASP PRO SER LYS LEU ASP SER GLY
SEQRES 6 A 228 LYS GLU LEU HIS ILE ASN LEU ILE PRO ASN LYS GLN ASP
SEQRES 7 A 228 ARG THR LEU THR ILE VAL ASP THR GLY ILE GLY MET THR
SEQRES 8 A 228 LYS ALA ASP LEU ILE ASN ASN LEU GLY THR ILE ALA LYS
SEQRES 9 A 228 SER GLY THR LYS ALA PHE MET GLU ALA LEU GLN ALA GLY
SEQRES 10 A 228 ALA ASP ILE SER MET ILE GLY GLN PHE GLY VAL GLY PHE
SEQRES 11 A 228 TYR SER ALA TYR LEU VAL ALA GLU LYS VAL THR VAL ILE
SEQRES 12 A 228 THR LYS HIS ASN ASP ASP GLU GLN TYR ALA TRP GLU SER
SEQRES 13 A 228 SER ALA GLY GLY SER PHE THR VAL ARG THR ASP THR GLY
SEQRES 14 A 228 GLU PRO MET GLY ARG GLY THR LYS VAL ILE LEU HIS LEU
SEQRES 15 A 228 LYS GLU ASP GLN THR GLU TYR LEU GLU GLU ARG ARG ILE
SEQRES 16 A 228 LYS GLU ILE VAL LYS LYS HIS SER GLN PHE ILE GLY TYR
SEQRES 17 A 228 PRO ILE THR LEU PHE VAL GLU LYS GLU ARG ASP LYS GLU
SEQRES 18 A 228 VAL SER ASP ASP GLU ALA GLU
SEQRES 1 B 228 ASP GLN PRO MET GLU GLU GLU GLU VAL GLU THR PHE ALA
SEQRES 2 B 228 PHE GLN ALA GLU ILE ALA GLN LEU MET SER LEU ILE ILE
SEQRES 3 B 228 ASN THR PHE TYR SER ASN LYS GLU ILE PHE LEU ARG GLU
SEQRES 4 B 228 LEU ILE SER ASN SER SER ASP ALA LEU ASP LYS ILE ARG
SEQRES 5 B 228 TYR GLU SER LEU THR ASP PRO SER LYS LEU ASP SER GLY
SEQRES 6 B 228 LYS GLU LEU HIS ILE ASN LEU ILE PRO ASN LYS GLN ASP
SEQRES 7 B 228 ARG THR LEU THR ILE VAL ASP THR GLY ILE GLY MET THR
SEQRES 8 B 228 LYS ALA ASP LEU ILE ASN ASN LEU GLY THR ILE ALA LYS
SEQRES 9 B 228 SER GLY THR LYS ALA PHE MET GLU ALA LEU GLN ALA GLY
SEQRES 10 B 228 ALA ASP ILE SER MET ILE GLY GLN PHE GLY VAL GLY PHE
SEQRES 11 B 228 TYR SER ALA TYR LEU VAL ALA GLU LYS VAL THR VAL ILE
SEQRES 12 B 228 THR LYS HIS ASN ASP ASP GLU GLN TYR ALA TRP GLU SER
SEQRES 13 B 228 SER ALA GLY GLY SER PHE THR VAL ARG THR ASP THR GLY
SEQRES 14 B 228 GLU PRO MET GLY ARG GLY THR LYS VAL ILE LEU HIS LEU
SEQRES 15 B 228 LYS GLU ASP GLN THR GLU TYR LEU GLU GLU ARG ARG ILE
SEQRES 16 B 228 LYS GLU ILE VAL LYS LYS HIS SER GLN PHE ILE GLY TYR
SEQRES 17 B 228 PRO ILE THR LEU PHE VAL GLU LYS GLU ARG ASP LYS GLU
SEQRES 18 B 228 VAL SER ASP ASP GLU ALA GLU
HET S36 A 301 23
HET S36 B 301 23
HETNAM S36 3,4-DIHYDROISOQUINOLIN-2(1H)-YL[2,4-DIHYDROXY-5-
HETNAM 2 S36 (PROPAN-2-YL)PHENYL]METHANONE
FORMUL 3 S36 2(C19 H21 N O3)
FORMUL 5 HOH *183(H2 O)
HELIX 1 1 GLN A 23 THR A 36 1 14
HELIX 2 2 GLU A 42 ASP A 66 1 25
HELIX 3 3 PRO A 67 ASP A 71 5 5
HELIX 4 4 THR A 99 THR A 109 1 11
HELIX 5 5 GLY A 114 ALA A 124 1 11
HELIX 6 6 ASP A 127 GLY A 135 5 9
HELIX 7 7 VAL A 136 LEU A 143 5 8
HELIX 8 8 GLU A 192 LEU A 198 5 7
HELIX 9 9 GLU A 199 SER A 211 1 13
HELIX 10 10 GLN B 23 THR B 36 1 14
HELIX 11 11 GLU B 42 ASP B 66 1 25
HELIX 12 12 PRO B 67 ASP B 71 5 5
HELIX 13 13 THR B 99 ASN B 105 1 7
HELIX 14 14 ASN B 106 THR B 109 5 4
HELIX 15 15 ILE B 110 ALA B 124 1 15
HELIX 16 16 ASP B 127 GLY B 135 5 9
HELIX 17 17 VAL B 136 LEU B 143 5 8
HELIX 18 18 GLU B 192 LEU B 198 5 7
HELIX 19 19 GLU B 199 SER B 211 1 13
SHEET 1 A 8 GLU A 18 ALA A 21 0
SHEET 2 A 8 SER A 169 THR A 174 -1 O PHE A 170 N PHE A 20
SHEET 3 A 8 TYR A 160 SER A 164 -1 N ALA A 161 O ARG A 173
SHEET 4 A 8 ALA A 145 LYS A 153 -1 N VAL A 150 O TRP A 162
SHEET 5 A 8 GLY A 183 LEU A 190 -1 O ILE A 187 N THR A 149
SHEET 6 A 8 THR A 88 ASP A 93 -1 N LEU A 89 O LEU A 188
SHEET 7 A 8 ILE A 78 ASN A 83 -1 N ILE A 81 O THR A 90
SHEET 8 A 8 ILE A 218 LEU A 220 1 O THR A 219 N LEU A 80
SHEET 1 B 8 GLU B 18 ALA B 21 0
SHEET 2 B 8 SER B 169 THR B 174 -1 O PHE B 170 N PHE B 20
SHEET 3 B 8 TYR B 160 SER B 164 -1 N ALA B 161 O ARG B 173
SHEET 4 B 8 ALA B 145 LYS B 153 -1 N VAL B 150 O TRP B 162
SHEET 5 B 8 GLY B 183 LEU B 190 -1 O ILE B 187 N THR B 149
SHEET 6 B 8 THR B 88 ASP B 93 -1 N ILE B 91 O VAL B 186
SHEET 7 B 8 ILE B 78 ASN B 83 -1 N ILE B 81 O THR B 90
SHEET 8 B 8 ILE B 218 LEU B 220 1 O THR B 219 N LEU B 80
SITE 1 AC1 12 ASN A 51 ASP A 54 ALA A 55 ASP A 93
SITE 2 AC1 12 GLY A 97 MET A 98 LEU A 107 PHE A 138
SITE 3 AC1 12 THR A 184 VAL A 186 HOH A 401 HOH A 437
SITE 1 AC2 11 ASN B 51 ASP B 54 ALA B 55 ASP B 93
SITE 2 AC2 11 ILE B 96 GLY B 97 PHE B 138 THR B 184
SITE 3 AC2 11 VAL B 186 HOH B 401 HOH B 417
CRYST1 64.319 88.830 98.181 90.00 90.00 90.00 P 21 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 0.015548 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011257 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010185 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
