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HEADER HYDROLASE 16-MAY-16 5JZ9
TITLE CRYSTAL STRUCTURE OF HSAD BOUND TO 3,5-DICHLORO-4-
TITLE 2 HYDROXYBENZENESULPHONIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 4,5:9,10-DISECO-3-HYDROXY-5,9,17-TRIOXOANDROSTA-1(10),2-
COMPND 3 DIENE-4-OATE HYDROLASE;
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: HSAD;
COMPND 6 SYNONYM: 2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOATE HYDROLASE,HOPDA
COMPND 7 HYDROLASE,META-CLEAVAGE PRODUCT HYDROLASE,MCP HYDROLASE;
COMPND 8 EC: 3.7.1.17,3.7.1.8;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS (STRAIN CDC 1551 /
SOURCE 3 OSHKOSH);
SOURCE 4 ORGANISM_TAXID: 83331;
SOURCE 5 STRAIN: CDC 1551 / OSHKOSH;
SOURCE 6 GENE: HSAD, BPHD, MT3674;
SOURCE 7 EXPRESSION_SYSTEM: PSEUDOMONAS PUTIDA;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 303;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: KT2442;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PVLT31
KEYWDS HSAD, M. TUBERCULOSIS, CHOLESTEROL, INHIBITOR, MCP-HYDROLASE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.RYAN,E.POLYCARPOU,N.A.LACK,D.EVANGELOPOULOS,C.SIEG,A.HALMAN,
AUTHOR 2 S.BHAKTA,A.SINCLAIR,O.ELEFTHERIADOU,T.D.MCHUGH,S.KEANY,E.LOWE,
AUTHOR 3 R.BALLET,A.ABIHAMMAD,A.CIULLI,E.SIM
REVDAT 3 05-JUL-17 5JZ9 1 JRNL
REVDAT 2 12-APR-17 5JZ9 1 JRNL
REVDAT 1 05-APR-17 5JZ9 0
JRNL AUTH A.RYAN,E.POLYCARPOU,N.A.LACK,D.EVANGELOPOULOS,C.SIEG,
JRNL AUTH 2 A.HALMAN,S.BHAKTA,O.ELEFTHERIADOU,T.D.MCHUGH,S.KEANY,
JRNL AUTH 3 E.D.LOWE,R.BALLET,A.ABUHAMMAD,W.R.JACOBS,A.CIULLI,E.SIM
JRNL TITL INVESTIGATION OF THE MYCOBACTERIAL ENZYME HSAD AS A
JRNL TITL 2 POTENTIAL NOVEL TARGET FOR ANTI-TUBERCULAR AGENTS USING A
JRNL TITL 3 FRAGMENT-BASED DRUG DESIGN APPROACH.
JRNL REF BR. J. PHARMACOL. V. 174 2209 2017
JRNL REFN ISSN 1476-5381
JRNL PMID 28380256
JRNL DOI 10.1111/BPH.13810
REMARK 2
REMARK 2 RESOLUTION. 2.68 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.68
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 75.29
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 18683
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.140
REMARK 3 FREE R VALUE TEST SET COUNT : 960
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 75.3242 - 5.1266 0.99 2670 126 0.1949 0.2170
REMARK 3 2 5.1266 - 4.0692 1.00 2584 120 0.1755 0.2295
REMARK 3 3 4.0692 - 3.5549 1.00 2540 113 0.1920 0.1718
REMARK 3 4 3.5549 - 3.2298 1.00 2503 149 0.2263 0.2457
REMARK 3 5 3.2298 - 2.9983 1.00 2477 157 0.2513 0.2932
REMARK 3 6 2.9983 - 2.8215 0.99 2466 153 0.2774 0.2872
REMARK 3 7 2.8215 - 2.6802 0.99 2483 142 0.2977 0.3531
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) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.850
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.17
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 : 0.004 4481
REMARK 3 ANGLE : 0.892 6081
REMARK 3 CHIRALITY : 0.033 658
REMARK 3 PLANARITY : 0.004 796
REMARK 3 DIHEDRAL : 13.284 1603
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND SEGID
REMARK 3 SELECTION : CHAIN B AND SEGID
REMARK 3 ATOM PAIRS NUMBER : 3310
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5JZ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221463.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97630
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18699
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.680
REMARK 200 RESOLUTION RANGE LOW (A) : 75.750
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.68
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.89500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.500
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: 2VF2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% (W/V) PEG-3000, 0.1M CHES PH 9.5,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y,-Z
REMARK 290 8555 X,-Y,-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 40.86500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 96.79200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.15900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 96.79200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.86500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.15900
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 40.86500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.15900
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 96.79200
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.15900
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 40.86500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 96.79200
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 -41.15900
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
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 GLU A 10 CG CD OE1 OE2
REMARK 470 GLU A 17 CD OE1 OE2
REMARK 470 LYS A 25 CG CD CE NZ
REMARK 470 ASP A 36 CG OD1 OD2
REMARK 470 GLN A 37 CG CD OE1 NE2
REMARK 470 LYS A 210 CE NZ
REMARK 470 GLU B 10 CG CD OE1 OE2
REMARK 470 GLU B 17 CG CD OE1 OE2
REMARK 470 LYS B 25 CG CD CE NZ
REMARK 470 ASP B 36 CG OD1 OD2
REMARK 470 GLU B 168 CG CD OE1 OE2
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 VAL A 33 CG1 CG2
REMARK 480 ASP A 36 CB
REMARK 480 LYS A 160 CE NZ
REMARK 480 GLU A 168 CD OE1 OE2
REMARK 480 ARG A 230 CD NE CZ NH1 NH2
REMARK 480 ARG A 258 CZ NH1 NH2
REMARK 480 ILE B 59 O
REMARK 480 LYS B 160 CD CE NZ
REMARK 480 ARG B 175 NE CZ
REMARK 480 GLN B 191 CG CD OE1 NE2
REMARK 480 GLU B 200 CG CD OE1 OE2
REMARK 480 LYS B 210 CD CE NZ
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 LYS A 81 77.13 -116.68
REMARK 500 SER A 114 -123.56 61.51
REMARK 500 LYS B 81 77.50 -114.62
REMARK 500 SER B 114 -120.98 60.17
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 6OR A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6OR B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VF2 RELATED DB: PDB
REMARK 900 APO ENZYME
DBREF 5JZ9 A 7 290 UNP P9WNH4 HSAD_MYCTO 7 290
DBREF 5JZ9 B 7 290 UNP P9WNH4 HSAD_MYCTO 7 290
SEQRES 1 A 284 LEU THR PHE GLU SER THR SER ARG PHE ALA GLU VAL ASP
SEQRES 2 A 284 VAL ASP GLY PRO LEU LYS LEU HIS TYR HIS GLU ALA GLY
SEQRES 3 A 284 VAL GLY ASN ASP GLN THR VAL VAL LEU LEU HIS GLY GLY
SEQRES 4 A 284 GLY PRO GLY ALA ALA SER TRP THR ASN PHE SER ARG ASN
SEQRES 5 A 284 ILE ALA VAL LEU ALA ARG HIS PHE HIS VAL LEU ALA VAL
SEQRES 6 A 284 ASP GLN PRO GLY TYR GLY HIS SER ASP LYS ARG ALA GLU
SEQRES 7 A 284 HIS GLY GLN PHE ASN ARG TYR ALA ALA MET ALA LEU LYS
SEQRES 8 A 284 GLY LEU PHE ASP GLN LEU GLY LEU GLY ARG VAL PRO LEU
SEQRES 9 A 284 VAL GLY ASN SER LEU GLY GLY GLY THR ALA VAL ARG PHE
SEQRES 10 A 284 ALA LEU ASP TYR PRO ALA ARG ALA GLY ARG LEU VAL LEU
SEQRES 11 A 284 MET GLY PRO GLY GLY LEU SER ILE ASN LEU PHE ALA PRO
SEQRES 12 A 284 ASP PRO THR GLU GLY VAL LYS ARG LEU SER LYS PHE SER
SEQRES 13 A 284 VAL ALA PRO THR ARG GLU ASN LEU GLU ALA PHE LEU ARG
SEQRES 14 A 284 VAL MET VAL TYR ASP LYS ASN LEU ILE THR PRO GLU LEU
SEQRES 15 A 284 VAL ASP GLN ARG PHE ALA LEU ALA SER THR PRO GLU SER
SEQRES 16 A 284 LEU THR ALA THR ARG ALA MET GLY LYS SER PHE ALA GLY
SEQRES 17 A 284 ALA ASP PHE GLU ALA GLY MET MET TRP ARG GLU VAL TYR
SEQRES 18 A 284 ARG LEU ARG GLN PRO VAL LEU LEU ILE TRP GLY ARG GLU
SEQRES 19 A 284 ASP ARG VAL ASN PRO LEU ASP GLY ALA LEU VAL ALA LEU
SEQRES 20 A 284 LYS THR ILE PRO ARG ALA GLN LEU HIS VAL PHE GLY GLN
SEQRES 21 A 284 CYS GLY HIS TRP VAL GLN VAL GLU LYS PHE ASP GLU PHE
SEQRES 22 A 284 ASN LYS LEU THR ILE GLU PHE LEU GLY GLY GLY
SEQRES 1 B 284 LEU THR PHE GLU SER THR SER ARG PHE ALA GLU VAL ASP
SEQRES 2 B 284 VAL ASP GLY PRO LEU LYS LEU HIS TYR HIS GLU ALA GLY
SEQRES 3 B 284 VAL GLY ASN ASP GLN THR VAL VAL LEU LEU HIS GLY GLY
SEQRES 4 B 284 GLY PRO GLY ALA ALA SER TRP THR ASN PHE SER ARG ASN
SEQRES 5 B 284 ILE ALA VAL LEU ALA ARG HIS PHE HIS VAL LEU ALA VAL
SEQRES 6 B 284 ASP GLN PRO GLY TYR GLY HIS SER ASP LYS ARG ALA GLU
SEQRES 7 B 284 HIS GLY GLN PHE ASN ARG TYR ALA ALA MET ALA LEU LYS
SEQRES 8 B 284 GLY LEU PHE ASP GLN LEU GLY LEU GLY ARG VAL PRO LEU
SEQRES 9 B 284 VAL GLY ASN SER LEU GLY GLY GLY THR ALA VAL ARG PHE
SEQRES 10 B 284 ALA LEU ASP TYR PRO ALA ARG ALA GLY ARG LEU VAL LEU
SEQRES 11 B 284 MET GLY PRO GLY GLY LEU SER ILE ASN LEU PHE ALA PRO
SEQRES 12 B 284 ASP PRO THR GLU GLY VAL LYS ARG LEU SER LYS PHE SER
SEQRES 13 B 284 VAL ALA PRO THR ARG GLU ASN LEU GLU ALA PHE LEU ARG
SEQRES 14 B 284 VAL MET VAL TYR ASP LYS ASN LEU ILE THR PRO GLU LEU
SEQRES 15 B 284 VAL ASP GLN ARG PHE ALA LEU ALA SER THR PRO GLU SER
SEQRES 16 B 284 LEU THR ALA THR ARG ALA MET GLY LYS SER PHE ALA GLY
SEQRES 17 B 284 ALA ASP PHE GLU ALA GLY MET MET TRP ARG GLU VAL TYR
SEQRES 18 B 284 ARG LEU ARG GLN PRO VAL LEU LEU ILE TRP GLY ARG GLU
SEQRES 19 B 284 ASP ARG VAL ASN PRO LEU ASP GLY ALA LEU VAL ALA LEU
SEQRES 20 B 284 LYS THR ILE PRO ARG ALA GLN LEU HIS VAL PHE GLY GLN
SEQRES 21 B 284 CYS GLY HIS TRP VAL GLN VAL GLU LYS PHE ASP GLU PHE
SEQRES 22 B 284 ASN LYS LEU THR ILE GLU PHE LEU GLY GLY GLY
HET 6OR A 301 16
HET 6OR B 301 16
HETNAM 6OR 3,5-DICHLORO-4-HYDROXYBENZENE-1-SULFONIC ACID
FORMUL 3 6OR 2(C6 H4 CL2 O4 S)
FORMUL 5 HOH *29(H2 O)
HELIX 1 AA1 THR A 8 THR A 12 1 5
HELIX 2 AA2 ALA A 50 PHE A 55 1 6
HELIX 3 AA3 ASN A 58 ARG A 64 1 7
HELIX 4 AA4 GLN A 87 GLY A 104 1 18
HELIX 5 AA5 SER A 114 TYR A 127 1 14
HELIX 6 AA6 THR A 152 ALA A 164 1 13
HELIX 7 AA7 THR A 166 VAL A 176 1 11
HELIX 8 AA8 ASP A 180 ILE A 184 5 5
HELIX 9 AA9 THR A 185 SER A 197 1 13
HELIX 10 AB1 THR A 198 PHE A 212 1 15
HELIX 11 AB2 ASP A 216 LEU A 229 5 14
HELIX 12 AB3 PRO A 245 GLY A 248 5 4
HELIX 13 AB4 ALA A 249 ILE A 256 1 8
HELIX 14 AB5 TRP A 270 LYS A 275 1 6
HELIX 15 AB6 LYS A 275 LEU A 287 1 13
HELIX 16 AB7 THR B 8 THR B 12 1 5
HELIX 17 AB8 ALA B 50 PHE B 55 1 6
HELIX 18 AB9 ASN B 58 ARG B 64 1 7
HELIX 19 AC1 GLN B 87 GLY B 104 1 18
HELIX 20 AC2 SER B 114 TYR B 127 1 14
HELIX 21 AC3 THR B 152 ALA B 164 1 13
HELIX 22 AC4 THR B 166 VAL B 176 1 11
HELIX 23 AC5 ASP B 180 ILE B 184 5 5
HELIX 24 AC6 THR B 185 SER B 197 1 13
HELIX 25 AC7 THR B 198 PHE B 212 1 15
HELIX 26 AC8 ASP B 216 LEU B 229 5 14
HELIX 27 AC9 PRO B 245 GLY B 248 5 4
HELIX 28 AD1 ALA B 249 ILE B 256 1 8
HELIX 29 AD2 TRP B 270 LYS B 275 1 6
HELIX 30 AD3 LYS B 275 LEU B 287 1 13
SHEET 1 AA1 8 SER A 13 ASP A 19 0
SHEET 2 AA1 8 PRO A 23 ALA A 31 -1 O LEU A 26 N ALA A 16
SHEET 3 AA1 8 HIS A 67 VAL A 71 -1 O ALA A 70 N HIS A 29
SHEET 4 AA1 8 THR A 38 LEU A 42 1 N VAL A 39 O HIS A 67
SHEET 5 AA1 8 VAL A 108 ASN A 113 1 O VAL A 111 N LEU A 42
SHEET 6 AA1 8 ALA A 131 MET A 137 1 O VAL A 135 N LEU A 110
SHEET 7 AA1 8 VAL A 233 GLY A 238 1 O LEU A 234 N LEU A 134
SHEET 8 AA1 8 ALA A 259 PHE A 264 1 O GLN A 260 N LEU A 235
SHEET 1 AA2 8 SER B 13 ASP B 19 0
SHEET 2 AA2 8 PRO B 23 ALA B 31 -1 O LEU B 26 N ALA B 16
SHEET 3 AA2 8 PHE B 66 VAL B 71 -1 O ALA B 70 N HIS B 29
SHEET 4 AA2 8 GLN B 37 LEU B 42 1 N GLN B 37 O HIS B 67
SHEET 5 AA2 8 VAL B 108 ASN B 113 1 O VAL B 111 N VAL B 40
SHEET 6 AA2 8 ALA B 131 MET B 137 1 O GLY B 132 N VAL B 108
SHEET 7 AA2 8 VAL B 233 GLY B 238 1 O LEU B 234 N LEU B 134
SHEET 8 AA2 8 ALA B 259 PHE B 264 1 O GLN B 260 N LEU B 235
CISPEP 1 ASP A 150 PRO A 151 0 -0.57
CISPEP 2 ASP B 150 PRO B 151 0 -1.60
SITE 1 AC1 12 GLY A 44 GLY A 45 GLY A 46 SER A 114
SITE 2 AC1 12 LEU A 115 GLY A 154 LEU A 158 PHE A 173
SITE 3 AC1 12 MET A 177 VAL A 243 HIS A 269 TRP A 270
SITE 1 AC2 12 GLY B 44 GLY B 45 GLY B 46 SER B 114
SITE 2 AC2 12 LEU B 115 GLY B 154 LEU B 158 PHE B 173
SITE 3 AC2 12 MET B 177 VAL B 243 HIS B 269 TRP B 270
CRYST1 81.730 82.318 193.584 90.00 90.00 90.00 I 21 21 21 16
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 0.012235 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012148 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005166 0.00000
TER 4320 GLY A 290
TER 8648 GLY B 290
MASTER 293 0 2 30 16 0 6 6 4404 2 32 44
END |