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HEADER LYASE 04-MAY-10 3MVE
TITLE CRYSTAL STRUCTURE OF A NOVEL PYRUVATE DECARBOXYLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UPF0255 PROTEIN VV1_0328;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: FRSA;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO VULNIFICUS;
SOURCE 3 ORGANISM_TAXID: 672;
SOURCE 4 STRAIN: M06-24/0;
SOURCE 5 GENE: FRSA, VV1_0328;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS FRSA,FERMENTATION/RESPIRATION SWITCH PROTEIN, HYDROLASE ACTIVATOR,
KEYWDS 2 LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.S.CHA,C.S.JEONG,Y.J.AN
REVDAT 2 08-JUN-11 3MVE 1 JRNL
REVDAT 1 18-MAY-11 3MVE 0
JRNL AUTH K.J.LEE,C.S.JEONG,Y.J.AN,H.J.LEE,S.J.PARK,Y.J.SEOK,P.KIM,
JRNL AUTH 2 J.H.LEE,K.H.LEE,S.S.CHA
JRNL TITL FRSA FUNCTIONS AS A COFACTOR-INDEPENDENT DECARBOXYLASE TO
JRNL TITL 2 CONTROL METABOLIC FLUX.
JRNL REF NAT.CHEM.BIOL. 2011
JRNL REFN ESSN 1552-4469
JRNL PMID 21623357
JRNL DOI 10.1038/NCHEMBIO.589
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.100
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 80851.970
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 39288
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1962
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5805
REMARK 3 BIN R VALUE (WORKING SET) : 0.1950
REMARK 3 BIN FREE R VALUE : 0.2470
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 303
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6136
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 65
REMARK 3 SOLVENT ATOMS : 304
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.56000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -2.56000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.72000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.14
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.78
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 41.07
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : EDO.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 4 : EDO.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3MVE COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAY-10.
REMARK 100 THE RCSB ID CODE IS RCSB059041.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ELECTRON MICROSCOPE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : PHOTON FACTORY BEAMLINE BL-17A
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99999
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41404
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.180
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06900
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.18
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.22
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.4
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 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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AM-SULFATE, 0.1M TRIS-HCL (PH
REMARK 280 8.5), 0.2M NA-ACETATE, MICRO BATH, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 44.10050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 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 SER A 2
REMARK 465 GLU A 3
REMARK 465 GLU A 4
REMARK 465 VAL A 5
REMARK 465 SER A 6
REMARK 465 LYS A 7
REMARK 465 ASN A 8
REMARK 465 LEU A 9
REMARK 465 SER A 10
REMARK 465 GLU A 11
REMARK 465 THR A 12
REMARK 465 LEU A 13
REMARK 465 PHE A 14
REMARK 465 VAL A 15
REMARK 465 LYS A 16
REMARK 465 HIS A 17
REMARK 465 LYS A 18
REMARK 465 GLN A 19
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLU B 3
REMARK 465 GLU B 4
REMARK 465 VAL B 5
REMARK 465 SER B 6
REMARK 465 LYS B 7
REMARK 465 ASN B 8
REMARK 465 LEU B 9
REMARK 465 SER B 10
REMARK 465 GLU B 11
REMARK 465 THR B 12
REMARK 465 LEU B 13
REMARK 465 PHE B 14
REMARK 465 VAL B 15
REMARK 465 LYS B 16
REMARK 465 HIS B 17
REMARK 465 LYS B 18
REMARK 465 GLN B 19
REMARK 465 ALA B 20
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 LYS A 21 CG CD CE NZ
REMARK 470 LYS A 43 CG CD CE NZ
REMARK 470 ARG A 53 CG CD NE CZ NH1 NH2
REMARK 470 TRP A 57 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 57 CZ3 CH2
REMARK 470 ARG A 104 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 141 CG CD CE NZ
REMARK 470 LYS A 179 CG CD CE NZ
REMARK 470 LYS A 219 CG CD CE NZ
REMARK 470 GLU A 242 CG CD OE1 OE2
REMARK 470 ARG A 352 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 355 CG CD CE NZ
REMARK 470 LYS A 385 CG CD CE NZ
REMARK 470 ILE A 394 CG1 CG2 CD1
REMARK 470 GLU A 399 CG CD OE1 OE2
REMARK 470 GLN A 400 CG CD OE1 NE2
REMARK 470 ASP A 403 CG OD1 OD2
REMARK 470 LYS A 407 CG CD CE NZ
REMARK 470 LYS B 21 CG CD CE NZ
REMARK 470 GLU B 42 CG CD OE1 OE2
REMARK 470 LYS B 43 CG CD CE NZ
REMARK 470 ARG B 104 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 111 CG CD CE NZ
REMARK 470 ARG B 112 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 115 CG CD OE1 OE2
REMARK 470 GLU B 119 CG CD OE1 OE2
REMARK 470 LYS B 179 CG CD CE NZ
REMARK 470 LYS B 219 CG CD CE NZ
REMARK 470 SER B 351 OG
REMARK 470 ARG B 352 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 363 CG CD1 CD2
REMARK 470 GLU B 364 CG CD OE1 OE2
REMARK 470 LYS B 385 CG CD CE NZ
REMARK 470 LYS B 387 CG CD CE NZ
REMARK 470 LYS B 388 CG CD CE NZ
REMARK 470 LYS B 392 CG CD CE NZ
REMARK 470 LEU B 402 CG CD1 CD2
REMARK 470 LEU B 404 CG CD1 CD2
REMARK 470 LYS B 407 CG CD CE NZ
REMARK 470 GLU B 410 CG CD OE1 OE2
REMARK 470 ARG B 415 CG CD NE CZ NH1 NH2
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 ASN A 118 -133.62 50.83
REMARK 500 HIS A 216 -63.13 -124.94
REMARK 500 SER A 231 0.88 81.74
REMARK 500 THR A 241 -160.80 -67.97
REMARK 500 ARG A 272 -131.08 51.54
REMARK 500 HIS A 300 -51.50 -152.13
REMARK 500 LEU A 349 73.60 -104.02
REMARK 500 SER A 350 -51.72 -158.50
REMARK 500 SER A 351 -107.44 -88.06
REMARK 500 SER A 390 -5.78 -53.26
REMARK 500 LYS B 191 157.58 178.55
REMARK 500 HIS B 216 -80.83 -131.49
REMARK 500 SER B 231 -0.10 85.71
REMARK 500 THR B 241 175.81 63.32
REMARK 500 ASP B 243 65.25 -103.91
REMARK 500 ARG B 272 -127.42 54.35
REMARK 500 HIS B 300 -57.52 -154.69
REMARK 500 SER B 327 -76.62 -69.84
REMARK 500 SER B 350 -57.11 -148.91
REMARK 500 SER B 351 -111.28 -87.24
REMARK 500 TYR B 383 17.09 86.97
REMARK 500 LYS B 392 -27.64 73.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 432 DISTANCE = 6.82 ANGSTROMS
REMARK 525 HOH A 434 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH B 574 DISTANCE = 5.72 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 418
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 419
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 420
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 421
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 422
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 423
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 424
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 418
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 419
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 420
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 421
DBREF 3MVE A 1 415 UNP Q8DF91 Y328_VIBVU 1 415
DBREF 3MVE B 1 415 UNP Q8DF91 Y328_VIBVU 1 415
SEQRES 1 A 415 MET SER GLU GLU VAL SER LYS ASN LEU SER GLU THR LEU
SEQRES 2 A 415 PHE VAL LYS HIS LYS GLN ALA LYS GLU THR SER ALA LEU
SEQRES 3 A 415 THR GLN TYR MET PRO THR SER GLN SER LEU LEU ASP GLU
SEQRES 4 A 415 ILE LYS GLU LYS ASN GLY PHE SER TRP TYR ARG ASN LEU
SEQRES 5 A 415 ARG ARG LEU GLN TRP VAL TRP GLN GLY VAL ASP PRO ILE
SEQRES 6 A 415 GLU GLN GLU GLN VAL LEU ALA ARG ILE ALA SER SER LYS
SEQRES 7 A 415 HIS SER ARG THR ASP GLU GLN TRP LEU ASP THR VAL MET
SEQRES 8 A 415 GLY TYR HIS SER GLY ASN TRP ALA TYR GLU TRP THR ARG
SEQRES 9 A 415 LEU GLY MET GLU HIS GLN LYS ARG ALA GLY GLU MET THR
SEQRES 10 A 415 ASN GLU ALA ALA SER GLU ALA LEU PHE SER ALA SER LEU
SEQRES 11 A 415 CYS TYR SER ILE ALA GLY TYR PRO HIS LEU LYS SER ASP
SEQRES 12 A 415 ASN LEU ALA ILE GLN ALA GLN VAL LEU ALA ASN SER ALA
SEQRES 13 A 415 TYR LEU GLU ALA ALA LYS LYS SER LYS TYR ILE ILE LYS
SEQRES 14 A 415 GLN LEU GLU ILE PRO PHE GLU LYS GLY LYS ILE THR ALA
SEQRES 15 A 415 HIS LEU HIS LEU THR ASN THR ASP LYS PRO HIS PRO VAL
SEQRES 16 A 415 VAL ILE VAL SER ALA GLY LEU ASP SER LEU GLN THR ASP
SEQRES 17 A 415 MET TRP ARG LEU PHE ARG ASP HIS LEU ALA LYS HIS ASP
SEQRES 18 A 415 ILE ALA MET LEU THR VAL ASP MET PRO SER VAL GLY TYR
SEQRES 19 A 415 SER SER LYS TYR PRO LEU THR GLU ASP TYR SER ARG LEU
SEQRES 20 A 415 HIS GLN ALA VAL LEU ASN GLU LEU PHE SER ILE PRO TYR
SEQRES 21 A 415 VAL ASP HIS HIS ARG VAL GLY LEU ILE GLY PHE ARG PHE
SEQRES 22 A 415 GLY GLY ASN ALA MET VAL ARG LEU SER PHE LEU GLU GLN
SEQRES 23 A 415 GLU LYS ILE LYS ALA CYS VAL ILE LEU GLY ALA PRO ILE
SEQRES 24 A 415 HIS ASP ILE PHE ALA SER PRO GLN LYS LEU GLN GLN MET
SEQRES 25 A 415 PRO LYS MET TYR LEU ASP VAL LEU ALA SER ARG LEU GLY
SEQRES 26 A 415 LYS SER VAL VAL ASP ILE TYR SER LEU SER GLY GLN MET
SEQRES 27 A 415 ALA ALA TRP SER LEU LYS VAL GLN GLY PHE LEU SER SER
SEQRES 28 A 415 ARG LYS THR LYS VAL PRO ILE LEU ALA MET SER LEU GLU
SEQRES 29 A 415 GLY ASP PRO VAL SER PRO TYR SER ASP ASN GLN MET VAL
SEQRES 30 A 415 ALA PHE PHE SER THR TYR GLY LYS ALA LYS LYS ILE SER
SEQRES 31 A 415 SER LYS THR ILE THR GLN GLY TYR GLU GLN SER LEU ASP
SEQRES 32 A 415 LEU ALA ILE LYS TRP LEU GLU ASP GLU LEU LEU ARG
SEQRES 1 B 415 MET SER GLU GLU VAL SER LYS ASN LEU SER GLU THR LEU
SEQRES 2 B 415 PHE VAL LYS HIS LYS GLN ALA LYS GLU THR SER ALA LEU
SEQRES 3 B 415 THR GLN TYR MET PRO THR SER GLN SER LEU LEU ASP GLU
SEQRES 4 B 415 ILE LYS GLU LYS ASN GLY PHE SER TRP TYR ARG ASN LEU
SEQRES 5 B 415 ARG ARG LEU GLN TRP VAL TRP GLN GLY VAL ASP PRO ILE
SEQRES 6 B 415 GLU GLN GLU GLN VAL LEU ALA ARG ILE ALA SER SER LYS
SEQRES 7 B 415 HIS SER ARG THR ASP GLU GLN TRP LEU ASP THR VAL MET
SEQRES 8 B 415 GLY TYR HIS SER GLY ASN TRP ALA TYR GLU TRP THR ARG
SEQRES 9 B 415 LEU GLY MET GLU HIS GLN LYS ARG ALA GLY GLU MET THR
SEQRES 10 B 415 ASN GLU ALA ALA SER GLU ALA LEU PHE SER ALA SER LEU
SEQRES 11 B 415 CYS TYR SER ILE ALA GLY TYR PRO HIS LEU LYS SER ASP
SEQRES 12 B 415 ASN LEU ALA ILE GLN ALA GLN VAL LEU ALA ASN SER ALA
SEQRES 13 B 415 TYR LEU GLU ALA ALA LYS LYS SER LYS TYR ILE ILE LYS
SEQRES 14 B 415 GLN LEU GLU ILE PRO PHE GLU LYS GLY LYS ILE THR ALA
SEQRES 15 B 415 HIS LEU HIS LEU THR ASN THR ASP LYS PRO HIS PRO VAL
SEQRES 16 B 415 VAL ILE VAL SER ALA GLY LEU ASP SER LEU GLN THR ASP
SEQRES 17 B 415 MET TRP ARG LEU PHE ARG ASP HIS LEU ALA LYS HIS ASP
SEQRES 18 B 415 ILE ALA MET LEU THR VAL ASP MET PRO SER VAL GLY TYR
SEQRES 19 B 415 SER SER LYS TYR PRO LEU THR GLU ASP TYR SER ARG LEU
SEQRES 20 B 415 HIS GLN ALA VAL LEU ASN GLU LEU PHE SER ILE PRO TYR
SEQRES 21 B 415 VAL ASP HIS HIS ARG VAL GLY LEU ILE GLY PHE ARG PHE
SEQRES 22 B 415 GLY GLY ASN ALA MET VAL ARG LEU SER PHE LEU GLU GLN
SEQRES 23 B 415 GLU LYS ILE LYS ALA CYS VAL ILE LEU GLY ALA PRO ILE
SEQRES 24 B 415 HIS ASP ILE PHE ALA SER PRO GLN LYS LEU GLN GLN MET
SEQRES 25 B 415 PRO LYS MET TYR LEU ASP VAL LEU ALA SER ARG LEU GLY
SEQRES 26 B 415 LYS SER VAL VAL ASP ILE TYR SER LEU SER GLY GLN MET
SEQRES 27 B 415 ALA ALA TRP SER LEU LYS VAL GLN GLY PHE LEU SER SER
SEQRES 28 B 415 ARG LYS THR LYS VAL PRO ILE LEU ALA MET SER LEU GLU
SEQRES 29 B 415 GLY ASP PRO VAL SER PRO TYR SER ASP ASN GLN MET VAL
SEQRES 30 B 415 ALA PHE PHE SER THR TYR GLY LYS ALA LYS LYS ILE SER
SEQRES 31 B 415 SER LYS THR ILE THR GLN GLY TYR GLU GLN SER LEU ASP
SEQRES 32 B 415 LEU ALA ILE LYS TRP LEU GLU ASP GLU LEU LEU ARG
HET SO4 A 416 5
HET EDO A 417 4
HET EDO A 418 4
HET EDO A 419 4
HET EDO A 420 4
HET EDO A 421 4
HET EDO A 422 4
HET EDO A 423 4
HET EDO A 424 4
HET SO4 B 416 5
HET SO4 B 417 5
HET SO4 B 418 5
HET SO4 B 419 5
HET EDO B 420 4
HET EDO B 421 4
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 SO4 5(O4 S 2-)
FORMUL 4 EDO 10(C2 H6 O2)
FORMUL 18 HOH *304(H2 O)
HELIX 1 1 GLU A 22 LEU A 26 5 5
HELIX 2 2 MET A 30 GLY A 45 1 16
HELIX 3 3 ASN A 51 GLN A 56 1 6
HELIX 4 4 TRP A 57 GLY A 61 5 5
HELIX 5 5 ASP A 63 SER A 77 1 15
HELIX 6 6 ASN A 97 GLY A 114 1 18
HELIX 7 7 THR A 117 TYR A 137 1 21
HELIX 8 8 ASP A 143 SER A 164 1 22
HELIX 9 9 LEU A 205 ASP A 208 5 4
HELIX 10 10 MET A 209 HIS A 216 1 8
HELIX 11 11 LEU A 217 ASP A 221 5 5
HELIX 12 12 VAL A 232 SER A 236 5 5
HELIX 13 13 SER A 245 LEU A 255 1 11
HELIX 14 14 PHE A 256 ILE A 258 5 3
HELIX 15 15 ARG A 272 GLU A 285 1 14
HELIX 16 16 HIS A 300 SER A 305 1 6
HELIX 17 17 SER A 305 GLN A 310 1 6
HELIX 18 18 PRO A 313 LEU A 324 1 12
HELIX 19 19 ASP A 330 MET A 338 1 9
HELIX 20 20 ALA A 339 SER A 342 5 4
HELIX 21 21 PRO A 370 PHE A 380 1 11
HELIX 22 22 THR A 393 LEU A 414 1 22
HELIX 23 23 GLU B 22 LEU B 26 5 5
HELIX 24 24 MET B 30 GLY B 45 1 16
HELIX 25 25 ARG B 53 GLN B 60 1 8
HELIX 26 26 ASP B 63 SER B 77 1 15
HELIX 27 27 ASN B 97 ALA B 113 1 17
HELIX 28 28 GLY B 114 MET B 116 5 3
HELIX 29 29 THR B 117 TYR B 137 1 21
HELIX 30 30 ASP B 143 SER B 164 1 22
HELIX 31 31 LEU B 205 ASP B 208 5 4
HELIX 32 32 MET B 209 ASP B 215 1 7
HELIX 33 33 HIS B 216 ASP B 221 5 6
HELIX 34 34 VAL B 232 SER B 236 5 5
HELIX 35 35 SER B 245 LEU B 255 1 11
HELIX 36 36 PHE B 256 ILE B 258 5 3
HELIX 37 37 ARG B 272 GLU B 285 1 14
HELIX 38 38 GLN B 286 ILE B 289 5 4
HELIX 39 39 HIS B 300 SER B 305 1 6
HELIX 40 40 SER B 305 GLN B 310 1 6
HELIX 41 41 PRO B 313 LEU B 324 1 12
HELIX 42 42 ASP B 330 MET B 338 1 9
HELIX 43 43 ALA B 339 SER B 342 5 4
HELIX 44 44 PRO B 370 PHE B 380 1 11
HELIX 45 45 GLY B 397 ARG B 415 1 19
SHEET 1 A 8 ILE A 167 PRO A 174 0
SHEET 2 A 8 LYS A 179 LEU A 186 -1 O ALA A 182 N LEU A 171
SHEET 3 A 8 ALA A 223 VAL A 227 -1 O MET A 224 N HIS A 185
SHEET 4 A 8 HIS A 193 SER A 199 1 N PRO A 194 O ALA A 223
SHEET 5 A 8 VAL A 261 PHE A 271 1 O PHE A 271 N SER A 199
SHEET 6 A 8 ALA A 291 LEU A 295 1 O VAL A 293 N LEU A 268
SHEET 7 A 8 ILE A 358 LEU A 363 1 O LEU A 359 N ILE A 294
SHEET 8 A 8 LYS A 385 ILE A 389 1 O LYS A 385 N ALA A 360
SHEET 1 B 2 GLN B 28 TYR B 29 0
SHEET 2 B 2 VAL B 328 VAL B 329 1 O VAL B 329 N GLN B 28
SHEET 1 C 8 ILE B 167 PHE B 175 0
SHEET 2 C 8 GLY B 178 LEU B 186 -1 O ALA B 182 N LEU B 171
SHEET 3 C 8 ALA B 223 VAL B 227 -1 O MET B 224 N HIS B 185
SHEET 4 C 8 HIS B 193 SER B 199 1 N VAL B 196 O LEU B 225
SHEET 5 C 8 VAL B 261 PHE B 271 1 O GLY B 267 N VAL B 195
SHEET 6 C 8 ALA B 291 LEU B 295 1 O VAL B 293 N LEU B 268
SHEET 7 C 8 ILE B 358 LEU B 363 1 O LEU B 359 N CYS B 292
SHEET 8 C 8 LYS B 385 ILE B 389 1 O LYS B 385 N ALA B 360
CISPEP 1 TYR A 137 PRO A 138 0 0.20
CISPEP 2 TYR B 137 PRO B 138 0 0.60
SITE 1 AC1 5 HIS A 79 SER A 80 HIS A 94 HOH A 521
SITE 2 AC1 5 HOH A 551
SITE 1 AC2 5 GLY A 201 LEU A 202 ARG A 272 PHE A 273
SITE 2 AC2 5 TYR A 316
SITE 1 AC3 8 TYR A 93 THR A 103 MET A 107 EDO A 419
SITE 2 AC3 8 HOH A 543 GLN B 110 SER B 155 HOH B 504
SITE 1 AC4 6 TYR A 93 THR A 103 LEU A 145 LEU A 152
SITE 2 AC4 6 EDO A 418 SER B 155
SITE 1 AC5 7 LEU A 125 GLU A 159 LYS A 162 LYS A 163
SITE 2 AC5 7 HOH A 554 GLY B 92 TYR B 93
SITE 1 AC6 4 PHE A 46 SER A 47 TRP A 48 HOH A 562
SITE 1 AC7 4 PHE A 283 GLY A 347 PHE A 348 ARG A 352
SITE 1 AC8 7 SER A 77 LYS A 78 HIS A 79 SER A 95
SITE 2 AC8 7 GLY A 96 HOH A 508 HOH A 571
SITE 1 AC9 10 LYS A 21 GLU A 22 THR A 23 ARG A 50
SITE 2 AC9 10 ASN A 97 TRP A 98 ALA A 99 LEU A 145
SITE 3 AC9 10 HOH A 505 HOH A 545
SITE 1 BC1 4 HIS B 79 SER B 80 HOH B 452 HOH B 453
SITE 1 BC2 6 GLY B 201 LEU B 202 ASP B 203 ARG B 272
SITE 2 BC2 6 PHE B 273 HOH B 522
SITE 1 BC3 3 LYS B 179 LYS B 237 HOH B 549
SITE 1 BC4 6 HIS B 216 HIS B 220 ILE B 222 ILE B 406
SITE 2 BC4 6 LYS B 407 GLU B 410
SITE 1 BC5 10 GLU B 22 THR B 23 ARG B 50 ASN B 97
SITE 2 BC5 10 ALA B 99 LEU B 145 HOH B 438 HOH B 456
SITE 3 BC5 10 HOH B 463 HOH B 565
SITE 1 BC6 7 VAL B 58 GLY B 61 VAL B 62 ASP B 63
SITE 2 BC6 7 ARG B 211 HOH B 449 HOH B 557
CRYST1 60.834 88.201 79.629 90.00 106.62 90.00 P 1 21 1 4
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 0.016438 0.000000 0.004906 0.00000
SCALE2 0.000000 0.011338 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013106 0.00000
TER 3080 ARG A 415
TER 6138 ARG B 415
MASTER 421 0 15 45 18 0 28 6 6505 2 65 64
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