HEADER TRANSCRIPTION 20-DEC-16 5MQK
TITLE CRYSTAL STRUCTURE OF CREBBP BROMODOMAIN COMPLEXED WITH CBP019
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CREB-BINDING PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: BROMODOMAIN, UNP RESIDUES 1081-1197;
COMPND 5 EC: 2.3.1.48;
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: CREBBP, CBP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS CREBBP BROMODOMAIN, INHIBITOR, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ZHU,D.SPILIOTOPOULOS,A.CAFLISCH
REVDAT 5 16-OCT-19 5MQK 1 REMARK
REVDAT 4 17-MAY-17 5MQK 1 JRNL
REVDAT 3 10-MAY-17 5MQK 1 AUTHOR
REVDAT 2 26-APR-17 5MQK 1 JRNL
REVDAT 1 19-APR-17 5MQK 0
JRNL AUTH D.SPILIOTOPOULOS,J.ZHU,E.C.WAMHOFF,N.DEERAIN,J.R.MARCHAND,
JRNL AUTH 2 J.ARETZ,C.RADEMACHER,A.CAFLISCH
JRNL TITL VIRTUAL SCREEN TO NMR (VS2NMR): DISCOVERY OF FRAGMENT HITS
JRNL TITL 2 FOR THE CBP BROMODOMAIN.
JRNL REF BIOORG. MED. CHEM. LETT. V. 27 2472 2017
JRNL REFN ESSN 1464-3405
JRNL PMID 28410781
JRNL DOI 10.1016/J.BMCL.2017.04.001
REMARK 2
REMARK 2 RESOLUTION. 1.53 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 1.53
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 33854
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.930
REMARK 3 FREE R VALUE TEST SET COUNT : 2007
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 37.7347 - 3.6866 0.99 2256 143 0.1410 0.1640
REMARK 3 2 3.6866 - 2.9265 0.99 2268 143 0.1668 0.1804
REMARK 3 3 2.9265 - 2.5567 1.00 2281 147 0.1879 0.2082
REMARK 3 4 2.5567 - 2.3229 1.00 2269 142 0.1967 0.2317
REMARK 3 5 2.3229 - 2.1565 0.99 2259 142 0.2084 0.2075
REMARK 3 6 2.1565 - 2.0293 1.00 2285 144 0.2095 0.2502
REMARK 3 7 2.0293 - 1.9277 1.00 2275 145 0.2188 0.2922
REMARK 3 8 1.9277 - 1.8438 1.00 2260 141 0.2209 0.2466
REMARK 3 9 1.8438 - 1.7728 1.00 2315 145 0.2263 0.2496
REMARK 3 10 1.7728 - 1.7116 1.00 2275 143 0.2399 0.3164
REMARK 3 11 1.7116 - 1.6581 0.99 2295 143 0.2543 0.3087
REMARK 3 12 1.6581 - 1.6107 0.99 2221 143 0.2568 0.3128
REMARK 3 13 1.6107 - 1.5683 1.00 2330 145 0.2623 0.3145
REMARK 3 14 1.5683 - 1.5300 1.00 2258 141 0.2782 0.2749
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.680
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 : 0.007 2063
REMARK 3 ANGLE : 0.915 2816
REMARK 3 CHIRALITY : 0.053 290
REMARK 3 PLANARITY : 0.007 368
REMARK 3 DIHEDRAL : 8.908 1737
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): 5.4460 -20.0062 4.0986
REMARK 3 T TENSOR
REMARK 3 T11: 0.2083 T22: 0.3196
REMARK 3 T33: 0.2501 T12: -0.0572
REMARK 3 T13: 0.0088 T23: 0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 1.5055 L22: 0.6970
REMARK 3 L33: -0.4123 L12: 1.2696
REMARK 3 L13: 0.2429 L23: 0.2185
REMARK 3 S TENSOR
REMARK 3 S11: 0.0268 S12: -0.1005 S13: -0.1199
REMARK 3 S21: 0.0095 S22: -0.0179 S23: -0.0703
REMARK 3 S31: -0.0463 S32: 0.1162 S33: -0.0032
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 5MQK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1200002851.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-16
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 : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99998
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33860
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.530
REMARK 200 RESOLUTION RANGE LOW (A) : 37.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.04100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.5000
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15 M KSCN, 20% PEG3350, 10% EG,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 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 61.17800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.32113
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 13.45600
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 61.17800
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 35.32113
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 13.45600
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 61.17800
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 35.32113
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 13.45600
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 70.64227
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 26.91200
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 70.64227
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 26.91200
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 70.64227
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 26.91200
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 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 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 SER A 1079
REMARK 465 MET A 1080
REMARK 465 SER B 1079
REMARK 465 MET B 1080
REMARK 465 ARG B 1081
REMARK 465 LYS B 1082
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 A1081 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1082 CE NZ
REMARK 470 LYS A1083 CG CD CE NZ
REMARK 470 LYS A1086 CE NZ
REMARK 470 GLU A1089 CD OE1 OE2
REMARK 470 LYS B1086 CG CD CE NZ
REMARK 470 LYS B1176 CD CE NZ
REMARK 470 GLN B1194 CG CD OE1 NE2
REMARK 470 GLY B1197 C O
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 1402 O HOH A 1411 1.89
REMARK 500 OH TYR A 1102 O HOH A 1301 1.92
REMARK 500 O HOH A 1338 O HOH A 1356 2.00
REMARK 500 OH TYR A 1102 O HOH A 1302 2.01
REMARK 500 O HOH A 1414 O HOH B 1362 2.05
REMARK 500 OD2 ASP B 1116 O HOH B 1301 2.10
REMARK 500 NH1 ARG A 1169 O HOH A 1303 2.10
REMARK 500 O HOH A 1392 O HOH A 1417 2.14
REMARK 500 O HOH A 1402 O HOH B 1348 2.14
REMARK 500 O HOH B 1333 O HOH B 1367 2.19
REMARK 500 OD1 ASP A 1127 O HOH A 1304 2.19
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 ILE B1122 69.99 -119.87
REMARK 500 GLU B1188 -18.01 -144.52
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 QPR A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue QPR B 1201
DBREF 5MQK A 1081 1197 UNP Q92793 CBP_HUMAN 1081 1197
DBREF 5MQK B 1081 1197 UNP Q92793 CBP_HUMAN 1081 1197
SEQADV 5MQK SER A 1079 UNP Q92793 EXPRESSION TAG
SEQADV 5MQK MET A 1080 UNP Q92793 EXPRESSION TAG
SEQADV 5MQK SER B 1079 UNP Q92793 EXPRESSION TAG
SEQADV 5MQK MET B 1080 UNP Q92793 EXPRESSION TAG
SEQRES 1 A 119 SER MET ARG LYS LYS ILE PHE LYS PRO GLU GLU LEU ARG
SEQRES 2 A 119 GLN ALA LEU MET PRO THR LEU GLU ALA LEU TYR ARG GLN
SEQRES 3 A 119 ASP PRO GLU SER LEU PRO PHE ARG GLN PRO VAL ASP PRO
SEQRES 4 A 119 GLN LEU LEU GLY ILE PRO ASP TYR PHE ASP ILE VAL LYS
SEQRES 5 A 119 ASN PRO MET ASP LEU SER THR ILE LYS ARG LYS LEU ASP
SEQRES 6 A 119 THR GLY GLN TYR GLN GLU PRO TRP GLN TYR VAL ASP ASP
SEQRES 7 A 119 VAL TRP LEU MET PHE ASN ASN ALA TRP LEU TYR ASN ARG
SEQRES 8 A 119 LYS THR SER ARG VAL TYR LYS PHE CYS SER LYS LEU ALA
SEQRES 9 A 119 GLU VAL PHE GLU GLN GLU ILE ASP PRO VAL MET GLN SER
SEQRES 10 A 119 LEU GLY
SEQRES 1 B 119 SER MET ARG LYS LYS ILE PHE LYS PRO GLU GLU LEU ARG
SEQRES 2 B 119 GLN ALA LEU MET PRO THR LEU GLU ALA LEU TYR ARG GLN
SEQRES 3 B 119 ASP PRO GLU SER LEU PRO PHE ARG GLN PRO VAL ASP PRO
SEQRES 4 B 119 GLN LEU LEU GLY ILE PRO ASP TYR PHE ASP ILE VAL LYS
SEQRES 5 B 119 ASN PRO MET ASP LEU SER THR ILE LYS ARG LYS LEU ASP
SEQRES 6 B 119 THR GLY GLN TYR GLN GLU PRO TRP GLN TYR VAL ASP ASP
SEQRES 7 B 119 VAL TRP LEU MET PHE ASN ASN ALA TRP LEU TYR ASN ARG
SEQRES 8 B 119 LYS THR SER ARG VAL TYR LYS PHE CYS SER LYS LEU ALA
SEQRES 9 B 119 GLU VAL PHE GLU GLN GLU ILE ASP PRO VAL MET GLN SER
SEQRES 10 B 119 LEU GLY
HET QPR A1201 13
HET QPR B1201 13
HETNAM QPR 1-(1-METHYLINDOL-3-YL)ETHANONE
FORMUL 3 QPR 2(C11 H11 N O)
FORMUL 5 HOH *211(H2 O)
HELIX 1 AA1 LYS A 1086 ARG A 1103 1 18
HELIX 2 AA2 SER A 1108 ARG A 1112 5 5
HELIX 3 AA3 ASP A 1116 GLY A 1121 1 6
HELIX 4 AA4 ASP A 1124 VAL A 1129 1 6
HELIX 5 AA5 ASP A 1134 THR A 1144 1 11
HELIX 6 AA6 GLU A 1149 ASN A 1168 1 20
HELIX 7 AA7 SER A 1172 LEU A 1196 1 25
HELIX 8 AA8 LYS B 1086 ARG B 1103 1 18
HELIX 9 AA9 SER B 1108 ARG B 1112 5 5
HELIX 10 AB1 ASP B 1116 GLY B 1121 1 6
HELIX 11 AB2 ASP B 1124 VAL B 1129 1 6
HELIX 12 AB3 ASP B 1134 THR B 1144 1 11
HELIX 13 AB4 GLU B 1149 ASN B 1168 1 20
HELIX 14 AB5 SER B 1172 LEU B 1196 1 25
CISPEP 1 ASP A 1105 PRO A 1106 0 12.72
CISPEP 2 ASP B 1105 PRO B 1106 0 9.55
SITE 1 AC1 5 PRO A1110 VAL A1115 ASN A1168 VAL A1174
SITE 2 AC1 5 HOH A1318
SITE 1 AC2 4 PRO B1110 VAL B1115 ASN B1168 HOH B1325
CRYST1 122.356 122.356 40.368 90.00 90.00 120.00 H 3 18
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 0.008173 0.004719 0.000000 0.00000
SCALE2 0.000000 0.009437 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024772 0.00000
(ATOM LINES ARE NOT SHOWN.)
END