HEADER TRANSFERASE/TRANSFERASE INHIBITOR 19-JAN-18 6C6O
TITLE CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS MALATE SYNTHASE IN
TITLE 2 COMPLEX WITH 2-BR-4-OH-PHENYLDIKETOACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MALATE SYNTHASE G;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.3.3.9;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: GLCB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ACETYLTRANSFERASE, STRUCTURAL GENOMICS, TB STRUCTURAL GENOMICS
KEYWDS 2 CONSORTIUM, TBSGC, TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS 3 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR I.V.KRIEGER,J.C.SACCHETTINI,TB STRUCTURAL GENOMICS CONSORTIUM (TBSGC)
REVDAT 5 04-OCT-23 6C6O 1 LINK
REVDAT 4 18-DEC-19 6C6O 1 REMARK
REVDAT 3 20-FEB-19 6C6O 1 REMARK
REVDAT 2 31-OCT-18 6C6O 1 JRNL
REVDAT 1 05-SEP-18 6C6O 0
JRNL AUTH J.F.ELLENBARGER,I.V.KRIEGER,H.L.HUANG,S.GOMEZ-COCA,
JRNL AUTH 2 T.R.IOERGER,J.C.SACCHETTINI,S.E.WHEELER,K.R.DUNBAR
JRNL TITL ANION-PI INTERACTIONS IN COMPUTER-AIDED DRUG DESIGN:
JRNL TITL 2 MODELING THE INHIBITION OF MALATE SYNTHASE BY PHENYL-DIKETO
JRNL TITL 3 ACIDS.
JRNL REF J CHEM INF MODEL V. 58 2085 2018
JRNL REFN ESSN 1549-960X
JRNL PMID 30137983
JRNL DOI 10.1021/ACS.JCIM.8B00417
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH I.V.KRIEGER,J.S.FREUNDLICH,V.B.GAWANDI,J.P.ROBERTS,Q.SUN,
REMARK 1 AUTH 2 J.L.OWEN,M.T.FRAILE,S.I.HUSS,J.L.LAVANDERA,T.R.IOERGER,
REMARK 1 AUTH 3 J.C.SACCHETTINI
REMARK 1 TITL STRUCTURE-GUIDED DISCOVERY OF PHENYL-DIKETO ACIDS AS POTENT
REMARK 1 TITL 2 INHIBITORS OF M. TUBERCULOSIS MALATE SYNTHASE.
REMARK 1 REF CHEM. BIOL. V. 19 1556 2012
REMARK 1 REFN ISSN 1879-1301
REMARK 1 PMID 23261599
REMARK 1 DOI 10.1016/J.CHEMBIOL.2012.09.018
REMARK 2
REMARK 2 RESOLUTION. 2.30 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.18
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 3 NUMBER OF REFLECTIONS : 31378
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.272
REMARK 3 R VALUE (WORKING SET) : 0.268
REMARK 3 FREE R VALUE : 0.349
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 1578
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 45.1852 - 5.1131 0.93 2909 155 0.2246 0.2843
REMARK 3 2 5.1131 - 4.0593 0.98 2894 148 0.2195 0.2807
REMARK 3 3 4.0593 - 3.5464 0.98 2855 156 0.2528 0.3407
REMARK 3 4 3.5464 - 3.2222 0.99 2853 145 0.2775 0.3977
REMARK 3 5 3.2222 - 2.9913 0.98 2831 134 0.2985 0.4070
REMARK 3 6 2.9913 - 2.8150 0.94 2666 152 0.3184 0.4198
REMARK 3 7 2.8150 - 2.6740 0.93 2658 136 0.3304 0.4975
REMARK 3 8 2.6740 - 2.5576 0.94 2648 143 0.3244 0.3987
REMARK 3 9 2.5576 - 2.4592 0.93 2646 135 0.3514 0.4319
REMARK 3 10 2.4592 - 2.3743 0.89 2492 147 0.3789 0.4503
REMARK 3 11 2.3743 - 2.3001 0.83 2348 127 0.4205 0.4920
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.520
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 45.160
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 : 0.008 5472
REMARK 3 ANGLE : 1.005 7433
REMARK 3 CHIRALITY : 0.054 849
REMARK 3 PLANARITY : 0.006 976
REMARK 3 DIHEDRAL : 12.484 3287
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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6C6O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JAN-18.
REMARK 100 THE DEPOSITION ID IS D_1000232148.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-FEB-12
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 7.5-8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36374
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.21200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.79400
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: MOLREP
REMARK 200 STARTING MODEL: 1N8I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS-HCL, MGCL2, PEG3350, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 113.70600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.78100
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.78100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 170.55900
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.78100
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.78100
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 56.85300
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.78100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.78100
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 170.55900
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.78100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.78100
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 56.85300
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 113.70600
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: 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 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 MET A 1
REMARK 465 VAL A 72
REMARK 465 ILE A 73
REMARK 465 GLU A 74
REMARK 465 PRO A 75
REMARK 465 ILE A 76
REMARK 465 ALA A 302
REMARK 465 VAL A 303
REMARK 465 ASP A 304
REMARK 465 LYS A 305
REMARK 465 ASP A 306
REMARK 465 GLY A 307
REMARK 465 THR A 308
REMARK 465 ALA A 309
REMARK 465 PHE A 310
REMARK 465 LEU A 311
REMARK 465 PRO A 323
REMARK 465 GLY A 324
REMARK 465 GLY A 325
REMARK 465 ASP A 380
REMARK 465 VAL A 381
REMARK 465 ASN A 382
REMARK 465 GLU A 586
REMARK 465 LEU A 587
REMARK 465 ALA A 588
REMARK 465 ALA A 674
REMARK 465 GLY A 675
REMARK 465 ASP A 676
REMARK 465 LYS A 728
REMARK 465 PRO A 729
REMARK 465 ALA A 730
REMARK 465 PRO A 731
REMARK 465 SER A 732
REMARK 465 ASP A 733
REMARK 465 ARG A 734
REMARK 465 ALA A 735
REMARK 465 GLY A 736
REMARK 465 ASP A 737
REMARK 465 ASP A 738
REMARK 465 ALA A 739
REMARK 465 ALA A 740
REMARK 465 ARG A 741
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 PRO A 48 -71.80 -44.86
REMARK 500 ARG A 70 -94.58 -141.96
REMARK 500 GLU A 150 36.39 -86.51
REMARK 500 THR A 151 -146.86 -73.22
REMARK 500 ASP A 152 -127.27 10.99
REMARK 500 ASP A 259 162.05 179.20
REMARK 500 SER A 264 -73.38 -116.19
REMARK 500 GLU A 273 -110.52 -111.26
REMARK 500 ASN A 387 -74.49 -102.12
REMARK 500 ARG A 508 -44.45 -140.37
REMARK 500 LEU A 521 75.88 -104.82
REMARK 500 LYS A 570 88.91 -57.27
REMARK 500 ARG A 572 32.43 -83.91
REMARK 500 PRO A 591 40.62 -75.82
REMARK 500 ASP A 592 -39.38 -134.03
REMARK 500 ASP A 624 -162.86 -70.28
REMARK 500 PRO A 681 175.46 -59.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 801 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 434 OE1
REMARK 620 2 ASP A 462 OD2 93.8
REMARK 620 3 ENG A 803 O03 109.7 94.9
REMARK 620 4 ENG A 803 O05 101.4 162.4 88.4
REMARK 620 5 HOH A 904 O 160.4 71.6 85.0 91.5
REMARK 620 6 HOH A 919 O 79.2 88.6 170.1 85.6 87.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 802 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 946 O
REMARK 620 2 HOH A 984 O 108.8
REMARK 620 3 HOH A 992 O 165.2 85.9
REMARK 620 4 HOH A 995 O 78.2 173.1 87.2
REMARK 620 5 HOH A1016 O 101.4 78.2 83.0 100.7
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ENG A 803
DBREF1 6C6O A 1 741 UNP A0A045ITM4_MYCTX
DBREF2 6C6O A A0A045ITM4 1 741
SEQADV 6C6O ALA A 619 UNP A0A045ITM CYS 619 ENGINEERED MUTATION
SEQRES 1 A 741 MET THR ASP ARG VAL SER VAL GLY ASN LEU ARG ILE ALA
SEQRES 2 A 741 ARG VAL LEU TYR ASP PHE VAL ASN ASN GLU ALA LEU PRO
SEQRES 3 A 741 GLY THR ASP ILE ASP PRO ASP SER PHE TRP ALA GLY VAL
SEQRES 4 A 741 ASP LYS VAL VAL ALA ASP LEU THR PRO GLN ASN GLN ALA
SEQRES 5 A 741 LEU LEU ASN ALA ARG ASP GLU LEU GLN ALA GLN ILE ASP
SEQRES 6 A 741 LYS TRP HIS ARG ARG ARG VAL ILE GLU PRO ILE ASP MET
SEQRES 7 A 741 ASP ALA TYR ARG GLN PHE LEU THR GLU ILE GLY TYR LEU
SEQRES 8 A 741 LEU PRO GLU PRO ASP ASP PHE THR ILE THR THR SER GLY
SEQRES 9 A 741 VAL ASP ALA GLU ILE THR THR THR ALA GLY PRO GLN LEU
SEQRES 10 A 741 VAL VAL PRO VAL LEU ASN ALA ARG PHE ALA LEU ASN ALA
SEQRES 11 A 741 ALA ASN ALA ARG TRP GLY SER LEU TYR ASP ALA LEU TYR
SEQRES 12 A 741 GLY THR ASP VAL ILE PRO GLU THR ASP GLY ALA GLU LYS
SEQRES 13 A 741 GLY PRO THR TYR ASN LYS VAL ARG GLY ASP LYS VAL ILE
SEQRES 14 A 741 ALA TYR ALA ARG LYS PHE LEU ASP ASP SER VAL PRO LEU
SEQRES 15 A 741 SER SER GLY SER PHE GLY ASP ALA THR GLY PHE THR VAL
SEQRES 16 A 741 GLN ASP GLY GLN LEU VAL VAL ALA LEU PRO ASP LYS SER
SEQRES 17 A 741 THR GLY LEU ALA ASN PRO GLY GLN PHE ALA GLY TYR THR
SEQRES 18 A 741 GLY ALA ALA GLU SER PRO THR SER VAL LEU LEU ILE ASN
SEQRES 19 A 741 HIS GLY LEU HIS ILE GLU ILE LEU ILE ASP PRO GLU SER
SEQRES 20 A 741 GLN VAL GLY THR THR ASP ARG ALA GLY VAL LYS ASP VAL
SEQRES 21 A 741 ILE LEU GLU SER ALA ILE THR THR ILE MET ASP PHE GLU
SEQRES 22 A 741 ASP SER VAL ALA ALA VAL ASP ALA ALA ASP LYS VAL LEU
SEQRES 23 A 741 GLY TYR ARG ASN TRP LEU GLY LEU ASN LYS GLY ASP LEU
SEQRES 24 A 741 ALA ALA ALA VAL ASP LYS ASP GLY THR ALA PHE LEU ARG
SEQRES 25 A 741 VAL LEU ASN ARG ASP ARG ASN TYR THR ALA PRO GLY GLY
SEQRES 26 A 741 GLY GLN PHE THR LEU PRO GLY ARG SER LEU MET PHE VAL
SEQRES 27 A 741 ARG ASN VAL GLY HIS LEU MET THR ASN ASP ALA ILE VAL
SEQRES 28 A 741 ASP THR ASP GLY SER GLU VAL PHE GLU GLY ILE MET ASP
SEQRES 29 A 741 ALA LEU PHE THR GLY LEU ILE ALA ILE HIS GLY LEU LYS
SEQRES 30 A 741 ALA SER ASP VAL ASN GLY PRO LEU ILE ASN SER ARG THR
SEQRES 31 A 741 GLY SER ILE TYR ILE VAL LYS PRO LYS MET HIS GLY PRO
SEQRES 32 A 741 ALA GLU VAL ALA PHE THR CYS GLU LEU PHE SER ARG VAL
SEQRES 33 A 741 GLU ASP VAL LEU GLY LEU PRO GLN ASN THR MET LYS ILE
SEQRES 34 A 741 GLY ILE MET ASP GLU GLU ARG ARG THR THR VAL ASN LEU
SEQRES 35 A 741 LYS ALA CYS ILE LYS ALA ALA ALA ASP ARG VAL VAL PHE
SEQRES 36 A 741 ILE ASN THR GLY PHE LEU ASP ARG THR GLY ASP GLU ILE
SEQRES 37 A 741 HIS THR SER MET GLU ALA GLY PRO MET VAL ARG LYS GLY
SEQRES 38 A 741 THR MET LYS SER GLN PRO TRP ILE LEU ALA TYR GLU ASP
SEQRES 39 A 741 HIS ASN VAL ASP ALA GLY LEU ALA ALA GLY PHE SER GLY
SEQRES 40 A 741 ARG ALA GLN VAL GLY LYS GLY MET TRP THR MET THR GLU
SEQRES 41 A 741 LEU MET ALA ASP MET VAL GLU THR LYS ILE ALA GLN PRO
SEQRES 42 A 741 ARG ALA GLY ALA SER THR ALA TRP VAL PRO SER PRO THR
SEQRES 43 A 741 ALA ALA THR LEU HIS ALA LEU HIS TYR HIS GLN VAL ASP
SEQRES 44 A 741 VAL ALA ALA VAL GLN GLN GLY LEU ALA GLY LYS ARG ARG
SEQRES 45 A 741 ALA THR ILE GLU GLN LEU LEU THR ILE PRO LEU ALA LYS
SEQRES 46 A 741 GLU LEU ALA TRP ALA PRO ASP GLU ILE ARG GLU GLU VAL
SEQRES 47 A 741 ASP ASN ASN CYS GLN SER ILE LEU GLY TYR VAL VAL ARG
SEQRES 48 A 741 TRP VAL ASP GLN GLY VAL GLY ALA SER LYS VAL PRO ASP
SEQRES 49 A 741 ILE HIS ASP VAL ALA LEU MET GLU ASP ARG ALA THR LEU
SEQRES 50 A 741 ARG ILE SER SER GLN LEU LEU ALA ASN TRP LEU ARG HIS
SEQRES 51 A 741 GLY VAL ILE THR SER ALA ASP VAL ARG ALA SER LEU GLU
SEQRES 52 A 741 ARG MET ALA PRO LEU VAL ASP ARG GLN ASN ALA GLY ASP
SEQRES 53 A 741 VAL ALA TYR ARG PRO MET ALA PRO ASN PHE ASP ASP SER
SEQRES 54 A 741 ILE ALA PHE LEU ALA ALA GLN GLU LEU ILE LEU SER GLY
SEQRES 55 A 741 ALA GLN GLN PRO ASN GLY TYR THR GLU PRO ILE LEU HIS
SEQRES 56 A 741 ARG ARG ARG ARG GLU PHE LYS ALA ARG ALA ALA GLU LYS
SEQRES 57 A 741 PRO ALA PRO SER ASP ARG ALA GLY ASP ASP ALA ALA ARG
HET MG A 801 1
HET MG A 802 1
HET ENG A 803 16
HETNAM MG MAGNESIUM ION
HETNAM ENG (2Z)-4-(2-BROMO-4-HYDROXYPHENYL)-2-HYDROXY-4-OXOBUT-2-
HETNAM 2 ENG ENOIC ACID
FORMUL 2 MG 2(MG 2+)
FORMUL 4 ENG C10 H7 BR O5
FORMUL 5 HOH *117(H2 O)
HELIX 1 AA1 ALA A 13 GLU A 23 1 11
HELIX 2 AA2 ASP A 31 ARG A 69 1 39
HELIX 3 AA3 MET A 78 ILE A 88 1 11
HELIX 4 AA4 ASP A 106 THR A 111 1 6
HELIX 5 AA5 ASN A 123 ASN A 132 1 10
HELIX 6 AA6 LEU A 138 THR A 145 1 8
HELIX 7 AA7 ASN A 161 VAL A 180 1 20
HELIX 8 AA8 SER A 186 ALA A 190 5 5
HELIX 9 AA9 ASN A 213 GLY A 215 5 3
HELIX 10 AB1 SER A 247 ASP A 253 1 7
HELIX 11 AB2 ASP A 280 GLY A 297 1 18
HELIX 12 AB3 GLU A 360 ILE A 373 1 14
HELIX 13 AB4 HIS A 374 LYS A 377 5 4
HELIX 14 AB5 GLY A 402 GLY A 421 1 20
HELIX 15 AB6 GLU A 435 VAL A 440 1 6
HELIX 16 AB7 ASN A 441 ALA A 449 1 9
HELIX 17 AB8 GLY A 459 SER A 471 1 13
HELIX 18 AB9 LYS A 480 SER A 485 5 6
HELIX 19 AC1 GLN A 486 ALA A 503 1 18
HELIX 20 AC2 LEU A 521 LYS A 529 1 9
HELIX 21 AC3 ILE A 530 ALA A 535 1 6
HELIX 22 AC4 SER A 544 VAL A 558 1 15
HELIX 23 AC5 ASP A 559 GLY A 566 1 8
HELIX 24 AC6 THR A 574 LEU A 579 1 6
HELIX 25 AC7 ASP A 592 GLY A 616 1 25
HELIX 26 AC8 ASP A 633 HIS A 650 1 18
HELIX 27 AC9 THR A 654 ASN A 673 1 20
HELIX 28 AD1 SER A 689 SER A 701 1 13
HELIX 29 AD2 GLY A 702 TYR A 709 5 8
HELIX 30 AD3 THR A 710 GLU A 727 1 18
SHEET 1 AA1 4 VAL A 5 VAL A 7 0
SHEET 2 AA1 4 LEU A 10 ILE A 12 -1 O ILE A 12 N VAL A 5
SHEET 3 AA1 4 THR A 346 ASP A 352 -1 O VAL A 351 N ARG A 11
SHEET 4 AA1 4 GLU A 357 PHE A 359 -1 O VAL A 358 N ASN A 347
SHEET 1 AA2 9 GLN A 116 PRO A 120 0
SHEET 2 AA2 9 THR A 267 ASP A 271 1 O ILE A 269 N LEU A 117
SHEET 3 AA2 9 LEU A 335 ARG A 339 1 O PHE A 337 N MET A 270
SHEET 4 AA2 9 ILE A 393 LYS A 397 1 O VAL A 396 N VAL A 338
SHEET 5 AA2 9 MET A 427 ASP A 433 1 O LYS A 428 N ILE A 393
SHEET 6 AA2 9 VAL A 453 THR A 458 1 O VAL A 454 N ILE A 429
SHEET 7 AA2 9 GLN A 510 MET A 515 1 O GLY A 512 N ILE A 456
SHEET 8 AA2 9 THR A 539 VAL A 542 1 O THR A 539 N LYS A 513
SHEET 9 AA2 9 GLN A 116 PRO A 120 1 N GLN A 116 O ALA A 540
SHEET 1 AA3 5 TRP A 135 SER A 137 0
SHEET 2 AA3 5 VAL A 257 GLU A 263 -1 O LEU A 262 N GLY A 136
SHEET 3 AA3 5 LEU A 237 ILE A 243 -1 N LEU A 242 O LYS A 258
SHEET 4 AA3 5 SER A 229 ASN A 234 -1 N LEU A 232 O ILE A 239
SHEET 5 AA3 5 PHE A 217 THR A 221 -1 N GLY A 219 O LEU A 231
SHEET 1 AA4 3 GLY A 192 GLN A 196 0
SHEET 2 AA4 3 GLN A 199 ALA A 203 -1 O VAL A 201 N THR A 194
SHEET 3 AA4 3 SER A 208 GLY A 210 -1 O THR A 209 N VAL A 202
SHEET 1 AA5 2 ARG A 318 TYR A 320 0
SHEET 2 AA5 2 PHE A 328 LEU A 330 -1 O PHE A 328 N TYR A 320
SHEET 1 AA6 2 SER A 620 PRO A 623 0
SHEET 2 AA6 2 ALA A 629 GLU A 632 -1 O GLU A 632 N SER A 620
LINK OE1 GLU A 434 MG MG A 801 1555 1555 2.12
LINK OD2 ASP A 462 MG MG A 801 1555 1555 2.13
LINK MG MG A 801 O03 ENG A 803 1555 1555 2.26
LINK MG MG A 801 O05 ENG A 803 1555 1555 1.99
LINK MG MG A 801 O HOH A 904 1555 1555 2.25
LINK MG MG A 801 O HOH A 919 1555 1555 2.19
LINK MG MG A 802 O HOH A 946 1555 1555 2.15
LINK MG MG A 802 O HOH A 984 1555 1555 2.03
LINK MG MG A 802 O HOH A 992 1555 1555 2.02
LINK MG MG A 802 O HOH A 995 1555 1555 1.98
LINK MG MG A 802 O HOH A1016 1555 1555 2.30
CISPEP 1 ALA A 683 PRO A 684 0 8.02
SITE 1 AC1 5 GLU A 434 ASP A 462 ENG A 803 HOH A 904
SITE 2 AC1 5 HOH A 919
SITE 1 AC2 6 HIS A 235 HOH A 946 HOH A 984 HOH A 992
SITE 2 AC2 6 HOH A 995 HOH A1016
SITE 1 AC3 16 VAL A 118 ARG A 339 MET A 432 GLU A 434
SITE 2 AC3 16 GLY A 459 PHE A 460 LEU A 461 ASP A 462
SITE 3 AC3 16 TRP A 541 MET A 631 ASP A 633 ALA A 635
SITE 4 AC3 16 MG A 801 HOH A 904 HOH A 919 HOH A 922
CRYST1 79.562 79.562 227.412 90.00 90.00 90.00 P 43 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 0.012569 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012569 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004397 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
