HEADER TRANSCRIPTION REGULATOR/INHIBITOR 30-NOV-16 5U2C
TITLE BRD4 SECOND BROMODOMAIN (BD2) IN COMPLEX WITH DUAL PI3 KINASE (PI3K)
TITLE 2 INHIBITOR SF2558HA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PROTEIN HUNK1;
COMPND 5 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: BRD4, HUNK1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BROMODOMAIN, TRANSCRIPTION, INHIBITOR, EPIGENETICS, TRANSCRIPTION
KEYWDS 2 REGULATOR-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR F.H.ANDREWS,T.G.KUTATELADZE
REVDAT 3 06-MAR-24 5U2C 1 REMARK
REVDAT 2 01-MAR-17 5U2C 1 JRNL
REVDAT 1 08-FEB-17 5U2C 0
JRNL AUTH F.H.ANDREWS,A.R.SINGH,S.JOSHI,C.A.SMITH,G.A.MORALES,
JRNL AUTH 2 J.R.GARLICH,D.L.DURDEN,T.G.KUTATELADZE
JRNL TITL DUAL-ACTIVITY PI3K-BRD4 INHIBITOR FOR THE ORTHOGONAL
JRNL TITL 2 INHIBITION OF MYC TO BLOCK TUMOR GROWTH AND METASTASIS.
JRNL REF PROC. NATL. ACAD. SCI. V. 114 E1072 2017
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 28137841
JRNL DOI 10.1073/PNAS.1613091114
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 60.37
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 6991
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.279
REMARK 3 R VALUE (WORKING SET) : 0.276
REMARK 3 FREE R VALUE : 0.296
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.250
REMARK 3 FREE R VALUE TEST SET COUNT : 367
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 17.5275 - 4.7412 0.94 2247 135 0.2585 0.2994
REMARK 3 2 4.7412 - 3.7756 0.95 2155 113 0.2779 0.2744
REMARK 3 3 3.7756 - 3.3019 0.95 2150 119 0.3046 0.3175
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 40.150
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 : 0.003 1977
REMARK 3 ANGLE : 0.878 2660
REMARK 3 CHIRALITY : 0.028 264
REMARK 3 PLANARITY : 0.003 341
REMARK 3 DIHEDRAL : 14.176 762
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): -8.6409 35.0881 -5.6359
REMARK 3 T TENSOR
REMARK 3 T11: 0.7398 T22: 0.8473
REMARK 3 T33: 0.3123 T12: -0.0748
REMARK 3 T13: 0.0131 T23: 0.1086
REMARK 3 L TENSOR
REMARK 3 L11: 1.7746 L22: 3.0289
REMARK 3 L33: 0.4480 L12: -0.1959
REMARK 3 L13: -0.8700 L23: 0.3822
REMARK 3 S TENSOR
REMARK 3 S11: -0.0092 S12: 0.2293 S13: -0.1543
REMARK 3 S21: -0.2149 S22: 0.0996 S23: 0.3180
REMARK 3 S31: 0.1183 S32: -0.0828 S33: -0.1425
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 5U2C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1000225197.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 4.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NOIR-1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6991
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 60.370
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.80
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : 0.07800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.0000
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: 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 (%): 68.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5 M AMMONIUM SULFATE IN 100 MM TRIS
REMARK 280 (PH 7.5), VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 32.88500
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 65.77000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 65.77000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 32.88500
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 337
REMARK 465 GLY A 338
REMARK 465 ASP A 459
REMARK 465 GLU A 460
REMARK 465 GLY B 337
REMARK 465 GLY B 338
REMARK 465 GLY B 339
REMARK 465 ILE B 340
REMARK 465 LEU B 341
REMARK 465 PRO B 342
REMARK 465 ALA B 343
REMARK 465 PRO B 344
REMARK 465 GLU B 345
REMARK 465 LYS B 346
REMARK 465 SER B 347
REMARK 465 SER B 348
REMARK 465 GLU B 460
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 SER A 348 N VAL A 350 2.09
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 LEU A 341 108.69 -40.18
REMARK 500 GLU A 345 142.92 -176.94
REMARK 500 SER A 347 -170.88 -63.52
REMARK 500 SER A 348 -94.85 -60.53
REMARK 500 LYS A 349 -43.09 47.59
REMARK 500 SER A 358 -70.38 -65.22
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 82Y A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 82Y B 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5U28 RELATED DB: PDB
REMARK 900 RELATED ID: 5U2F RELATED DB: PDB
REMARK 900 RELATED ID: 5U2E RELATED DB: PDB
DBREF 5U2C A 342 460 UNP O60885 BRD4_HUMAN 342 460
DBREF 5U2C B 342 460 UNP O60885 BRD4_HUMAN 342 460
SEQADV 5U2C GLY A 337 UNP O60885 EXPRESSION TAG
SEQADV 5U2C GLY A 338 UNP O60885 EXPRESSION TAG
SEQADV 5U2C GLY A 339 UNP O60885 EXPRESSION TAG
SEQADV 5U2C ILE A 340 UNP O60885 EXPRESSION TAG
SEQADV 5U2C LEU A 341 UNP O60885 EXPRESSION TAG
SEQADV 5U2C GLY B 337 UNP O60885 EXPRESSION TAG
SEQADV 5U2C GLY B 338 UNP O60885 EXPRESSION TAG
SEQADV 5U2C GLY B 339 UNP O60885 EXPRESSION TAG
SEQADV 5U2C ILE B 340 UNP O60885 EXPRESSION TAG
SEQADV 5U2C LEU B 341 UNP O60885 EXPRESSION TAG
SEQRES 1 A 124 GLY GLY GLY ILE LEU PRO ALA PRO GLU LYS SER SER LYS
SEQRES 2 A 124 VAL SER GLU GLN LEU LYS CYS CYS SER GLY ILE LEU LYS
SEQRES 3 A 124 GLU MET PHE ALA LYS LYS HIS ALA ALA TYR ALA TRP PRO
SEQRES 4 A 124 PHE TYR LYS PRO VAL ASP VAL GLU ALA LEU GLY LEU HIS
SEQRES 5 A 124 ASP TYR CYS ASP ILE ILE LYS HIS PRO MET ASP MET SER
SEQRES 6 A 124 THR ILE LYS SER LYS LEU GLU ALA ARG GLU TYR ARG ASP
SEQRES 7 A 124 ALA GLN GLU PHE GLY ALA ASP VAL ARG LEU MET PHE SER
SEQRES 8 A 124 ASN CYS TYR LYS TYR ASN PRO PRO ASP HIS GLU VAL VAL
SEQRES 9 A 124 ALA MET ALA ARG LYS LEU GLN ASP VAL PHE GLU MET ARG
SEQRES 10 A 124 PHE ALA LYS MET PRO ASP GLU
SEQRES 1 B 124 GLY GLY GLY ILE LEU PRO ALA PRO GLU LYS SER SER LYS
SEQRES 2 B 124 VAL SER GLU GLN LEU LYS CYS CYS SER GLY ILE LEU LYS
SEQRES 3 B 124 GLU MET PHE ALA LYS LYS HIS ALA ALA TYR ALA TRP PRO
SEQRES 4 B 124 PHE TYR LYS PRO VAL ASP VAL GLU ALA LEU GLY LEU HIS
SEQRES 5 B 124 ASP TYR CYS ASP ILE ILE LYS HIS PRO MET ASP MET SER
SEQRES 6 B 124 THR ILE LYS SER LYS LEU GLU ALA ARG GLU TYR ARG ASP
SEQRES 7 B 124 ALA GLN GLU PHE GLY ALA ASP VAL ARG LEU MET PHE SER
SEQRES 8 B 124 ASN CYS TYR LYS TYR ASN PRO PRO ASP HIS GLU VAL VAL
SEQRES 9 B 124 ALA MET ALA ARG LYS LEU GLN ASP VAL PHE GLU MET ARG
SEQRES 10 B 124 PHE ALA LYS MET PRO ASP GLU
HET 82Y A 501 26
HET 82Y B 501 26
HETNAM 82Y N-HYDROXY-4-[5-(MORPHOLIN-4-YL)-7-OXO-7H-THIENO[3,2-
HETNAM 2 82Y B]PYRAN-3-YL]BENZAMIDE
FORMUL 3 82Y 2(C18 H16 N2 O5 S)
HELIX 1 AA1 LYS A 349 PHE A 365 1 17
HELIX 2 AA2 ALA A 366 LYS A 368 5 3
HELIX 3 AA3 HIS A 369 TRP A 374 1 6
HELIX 4 AA4 PRO A 375 TYR A 377 5 3
HELIX 5 AA5 ASP A 389 ILE A 394 1 6
HELIX 6 AA6 ASP A 399 ALA A 409 1 11
HELIX 7 AA7 ASP A 414 ASN A 433 1 20
HELIX 8 AA8 HIS A 437 LYS A 456 1 20
HELIX 9 AA9 VAL B 350 PHE B 365 1 16
HELIX 10 AB1 HIS B 369 TRP B 374 1 6
HELIX 11 AB2 PRO B 375 TYR B 377 5 3
HELIX 12 AB3 ASP B 389 ILE B 394 1 6
HELIX 13 AB4 ASP B 399 ALA B 409 1 11
HELIX 14 AB5 ASP B 414 ASN B 433 1 20
HELIX 15 AB6 HIS B 437 LYS B 456 1 20
SITE 1 AC1 7 TRP A 374 PRO A 375 VAL A 380 LEU A 385
SITE 2 AC1 7 TYR A 390 ASN A 433 HIS A 437
SITE 1 AC2 6 PRO B 375 VAL B 380 LEU B 385 TYR B 390
SITE 2 AC2 6 ASN B 433 HIS B 437
CRYST1 88.139 88.139 98.655 90.00 90.00 120.00 P 31 2 1 12
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 0.011346 0.006550 0.000000 0.00000
SCALE2 0.000000 0.013101 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010136 0.00000
(ATOM LINES ARE NOT SHOWN.)
END