HEADER OXIDOREDUCTASE 10-JUL-03 1PZG
TITLE T.GONDII LDH1 COMPLEXED WITH APAD AND SULFATE AT 1.6 ANGSTROMS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LACTATE DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: LDH;
COMPND 5 EC: 1.1.1.27;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TOXOPLASMA GONDII;
SOURCE 3 ORGANISM_TAXID: 508771;
SOURCE 4 STRAIN: ME49;
SOURCE 5 GENE: LDH1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTYB2
KEYWDS APICOMPLEXA, APAD, TETRAMER, ROSSMANN FOLD, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.L.KAVANAGH,R.A.ELLING,D.K.WILSON
REVDAT 4 16-AUG-23 1PZG 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 1PZG 1 VERSN
REVDAT 2 24-FEB-09 1PZG 1 VERSN
REVDAT 1 24-FEB-04 1PZG 0
JRNL AUTH K.L.KAVANAGH,R.A.ELLING,D.K.WILSON
JRNL TITL STRUCTURE OF TOXOPLASMA GONDII LDH1: ACTIVE-SITE DIFFERENCES
JRNL TITL 2 FROM HUMAN LACTATE DEHYDROGENASES AND THE STRUCTURAL BASIS
JRNL TITL 3 FOR EFFICIENT APAD+ USE.
JRNL REF BIOCHEMISTRY V. 43 879 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 14744130
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.8
REMARK 3 NUMBER OF REFLECTIONS : 137149
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) : 0.176
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 8417
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9881
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 196
REMARK 3 SOLVENT ATOMS : 562
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) : 0.36000
REMARK 3 B22 (A**2) : 4.11400
REMARK 3 B33 (A**2) : -4.47400
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.06700
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.470
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.099 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.671 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.961 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.884 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CME.PAR_NEW
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 5 : PAR.APAD
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : CNS_TOPPAR:PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CME.TOP
REMARK 3 TOPOLOGY FILE 3 : CNS_TOPPAR:WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : CNS_TOPPAR:ION.TOP
REMARK 3 TOPOLOGY FILE 5 : TOP.APAD
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PZG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000019724.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-DEC-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
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 : CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 167180
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.03600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.34600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASING FROM ISOMORPHOUS STRUCTURE
REMARK 200 STARTING MODEL: PDB ENTRY 1PZF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.9 M AMMONIUM SULFATE, 100 MM
REMARK 280 ACETATE, PH 4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 62.48900
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 23680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -196.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 12
REMARK 465 ALA A 13
REMARK 465 GLY A 335
REMARK 465 MET B 12
REMARK 465 ALA B 13
REMARK 465 GLY B 335
REMARK 465 MET C 12
REMARK 465 ALA C 13
REMARK 465 PRO C 14
REMARK 465 ALA C 333
REMARK 465 PRO C 334
REMARK 465 GLY C 335
REMARK 465 MET D 12
REMARK 465 ALA D 13
REMARK 465 ALA D 333
REMARK 465 PRO D 334
REMARK 465 GLY D 335
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 CYS A 131 64.36 -154.81
REMARK 500 ALA A 164 -57.01 -159.92
REMARK 500 TYR A 247 -29.05 -142.98
REMARK 500 CYS B 131 62.54 -150.81
REMARK 500 ALA B 164 -58.17 -165.33
REMARK 500 TYR B 247 -29.73 -145.53
REMARK 500 TYR B 279 11.17 52.05
REMARK 500 PRO C 114 -88.79 -32.14
REMARK 500 ALA C 164 -57.17 -161.90
REMARK 500 TYR C 247 -27.56 -146.25
REMARK 500 TYR C 279 17.04 59.46
REMARK 500 CYS D 131 62.34 -151.09
REMARK 500 ALA D 164 -57.96 -164.19
REMARK 500 TYR D 247 -26.58 -144.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 38 0.08 SIDE CHAIN
REMARK 500 TYR B 38 0.08 SIDE CHAIN
REMARK 500 TYR C 38 0.08 SIDE CHAIN
REMARK 500 TYR D 38 0.07 SIDE CHAIN
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 SO4 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A3D A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A3D B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A3D C 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A3D D 607
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PZE RELATED DB: PDB
REMARK 900 T.GONDII LDH1 APO FORM
REMARK 900 RELATED ID: 1PZF RELATED DB: PDB
REMARK 900 T.GONDII LDH1 TERNARY COMPLEX WITH APAD+ AND OXALATE
REMARK 900 RELATED ID: 1PZH RELATED DB: PDB
REMARK 900 T.GONDII LDH1 TERNARY COMPLEX WITH NAD AND OXALATE
DBREF 1PZG A 12 335 UNP P90613 P90613_TOXGO 1 329
DBREF 1PZG B 12 335 UNP P90613 P90613_TOXGO 1 329
DBREF 1PZG C 12 335 UNP P90613 P90613_TOXGO 1 329
DBREF 1PZG D 12 335 UNP P90613 P90613_TOXGO 1 329
SEQADV 1PZG CME A 150 UNP P90613 CYS 143 MODIFIED RESIDUE
SEQADV 1PZG PRO A 334 UNP P90613 CLONING ARTIFACT
SEQADV 1PZG GLY A 335 UNP P90613 CLONING ARTIFACT
SEQADV 1PZG CME B 150 UNP P90613 CYS 143 MODIFIED RESIDUE
SEQADV 1PZG PRO B 334 UNP P90613 CLONING ARTIFACT
SEQADV 1PZG GLY B 335 UNP P90613 CLONING ARTIFACT
SEQADV 1PZG CME C 150 UNP P90613 CYS 143 MODIFIED RESIDUE
SEQADV 1PZG PRO C 334 UNP P90613 CLONING ARTIFACT
SEQADV 1PZG GLY C 335 UNP P90613 CLONING ARTIFACT
SEQADV 1PZG CME D 150 UNP P90613 CYS 143 MODIFIED RESIDUE
SEQADV 1PZG PRO D 334 UNP P90613 CLONING ARTIFACT
SEQADV 1PZG GLY D 335 UNP P90613 CLONING ARTIFACT
SEQRES 1 A 331 MET ALA PRO ALA LEU VAL GLN ARG ARG LYS LYS VAL ALA
SEQRES 2 A 331 MET ILE GLY SER GLY MET ILE GLY GLY THR MET GLY TYR
SEQRES 3 A 331 LEU CYS ALA LEU ARG GLU LEU ALA ASP VAL VAL LEU TYR
SEQRES 4 A 331 ASP VAL VAL LYS GLY MET PRO GLU GLY LYS ALA LEU ASP
SEQRES 5 A 331 LEU SER HIS VAL THR SER VAL VAL ASP THR ASN VAL SER
SEQRES 6 A 331 VAL ARG ALA GLU TYR SER TYR GLU ALA ALA LEU THR GLY
SEQRES 7 A 331 ALA ASP CYS VAL ILE VAL THR ALA GLY LEU THR LYS VAL
SEQRES 8 A 331 PRO GLY LYS PRO ASP SER GLU TRP SER ARG ASN ASP LEU
SEQRES 9 A 331 LEU PRO PHE ASN SER LYS ILE ILE ARG GLU ILE GLY GLN
SEQRES 10 A 331 ASN ILE LYS LYS TYR CYS PRO LYS THR PHE ILE ILE VAL
SEQRES 11 A 331 VAL THR ASN PRO LEU ASP CYS MET VAL LYS VAL MET CME
SEQRES 12 A 331 GLU ALA SER GLY VAL PRO THR ASN MET ILE CYS GLY MET
SEQRES 13 A 331 ALA CYS MET LEU ASP SER GLY ARG PHE ARG ARG TYR VAL
SEQRES 14 A 331 ALA ASP ALA LEU SER VAL SER PRO ARG ASP VAL GLN ALA
SEQRES 15 A 331 THR VAL ILE GLY THR HIS GLY ASP CYS MET VAL PRO LEU
SEQRES 16 A 331 VAL ARG TYR ILE THR VAL ASN GLY TYR PRO ILE GLN LYS
SEQRES 17 A 331 PHE ILE LYS ASP GLY VAL VAL THR GLU LYS GLN LEU GLU
SEQRES 18 A 331 GLU ILE ALA GLU HIS THR LYS VAL SER GLY GLY GLU ILE
SEQRES 19 A 331 VAL ARG PHE LEU GLY GLN GLY SER ALA TYR TYR ALA PRO
SEQRES 20 A 331 ALA ALA SER ALA VAL ALA MET ALA THR SER PHE LEU ASN
SEQRES 21 A 331 ASP GLU LYS ARG VAL ILE PRO CYS SER VAL TYR CYS ASN
SEQRES 22 A 331 GLY GLU TYR GLY LEU LYS ASP MET PHE ILE GLY LEU PRO
SEQRES 23 A 331 ALA VAL ILE GLY GLY ALA GLY ILE GLU ARG VAL ILE GLU
SEQRES 24 A 331 LEU GLU LEU ASN GLU GLU GLU LYS LYS GLN PHE GLN LYS
SEQRES 25 A 331 SER VAL ASP ASP VAL MET ALA LEU ASN LYS ALA VAL ALA
SEQRES 26 A 331 ALA LEU GLN ALA PRO GLY
SEQRES 1 B 331 MET ALA PRO ALA LEU VAL GLN ARG ARG LYS LYS VAL ALA
SEQRES 2 B 331 MET ILE GLY SER GLY MET ILE GLY GLY THR MET GLY TYR
SEQRES 3 B 331 LEU CYS ALA LEU ARG GLU LEU ALA ASP VAL VAL LEU TYR
SEQRES 4 B 331 ASP VAL VAL LYS GLY MET PRO GLU GLY LYS ALA LEU ASP
SEQRES 5 B 331 LEU SER HIS VAL THR SER VAL VAL ASP THR ASN VAL SER
SEQRES 6 B 331 VAL ARG ALA GLU TYR SER TYR GLU ALA ALA LEU THR GLY
SEQRES 7 B 331 ALA ASP CYS VAL ILE VAL THR ALA GLY LEU THR LYS VAL
SEQRES 8 B 331 PRO GLY LYS PRO ASP SER GLU TRP SER ARG ASN ASP LEU
SEQRES 9 B 331 LEU PRO PHE ASN SER LYS ILE ILE ARG GLU ILE GLY GLN
SEQRES 10 B 331 ASN ILE LYS LYS TYR CYS PRO LYS THR PHE ILE ILE VAL
SEQRES 11 B 331 VAL THR ASN PRO LEU ASP CYS MET VAL LYS VAL MET CME
SEQRES 12 B 331 GLU ALA SER GLY VAL PRO THR ASN MET ILE CYS GLY MET
SEQRES 13 B 331 ALA CYS MET LEU ASP SER GLY ARG PHE ARG ARG TYR VAL
SEQRES 14 B 331 ALA ASP ALA LEU SER VAL SER PRO ARG ASP VAL GLN ALA
SEQRES 15 B 331 THR VAL ILE GLY THR HIS GLY ASP CYS MET VAL PRO LEU
SEQRES 16 B 331 VAL ARG TYR ILE THR VAL ASN GLY TYR PRO ILE GLN LYS
SEQRES 17 B 331 PHE ILE LYS ASP GLY VAL VAL THR GLU LYS GLN LEU GLU
SEQRES 18 B 331 GLU ILE ALA GLU HIS THR LYS VAL SER GLY GLY GLU ILE
SEQRES 19 B 331 VAL ARG PHE LEU GLY GLN GLY SER ALA TYR TYR ALA PRO
SEQRES 20 B 331 ALA ALA SER ALA VAL ALA MET ALA THR SER PHE LEU ASN
SEQRES 21 B 331 ASP GLU LYS ARG VAL ILE PRO CYS SER VAL TYR CYS ASN
SEQRES 22 B 331 GLY GLU TYR GLY LEU LYS ASP MET PHE ILE GLY LEU PRO
SEQRES 23 B 331 ALA VAL ILE GLY GLY ALA GLY ILE GLU ARG VAL ILE GLU
SEQRES 24 B 331 LEU GLU LEU ASN GLU GLU GLU LYS LYS GLN PHE GLN LYS
SEQRES 25 B 331 SER VAL ASP ASP VAL MET ALA LEU ASN LYS ALA VAL ALA
SEQRES 26 B 331 ALA LEU GLN ALA PRO GLY
SEQRES 1 C 331 MET ALA PRO ALA LEU VAL GLN ARG ARG LYS LYS VAL ALA
SEQRES 2 C 331 MET ILE GLY SER GLY MET ILE GLY GLY THR MET GLY TYR
SEQRES 3 C 331 LEU CYS ALA LEU ARG GLU LEU ALA ASP VAL VAL LEU TYR
SEQRES 4 C 331 ASP VAL VAL LYS GLY MET PRO GLU GLY LYS ALA LEU ASP
SEQRES 5 C 331 LEU SER HIS VAL THR SER VAL VAL ASP THR ASN VAL SER
SEQRES 6 C 331 VAL ARG ALA GLU TYR SER TYR GLU ALA ALA LEU THR GLY
SEQRES 7 C 331 ALA ASP CYS VAL ILE VAL THR ALA GLY LEU THR LYS VAL
SEQRES 8 C 331 PRO GLY LYS PRO ASP SER GLU TRP SER ARG ASN ASP LEU
SEQRES 9 C 331 LEU PRO PHE ASN SER LYS ILE ILE ARG GLU ILE GLY GLN
SEQRES 10 C 331 ASN ILE LYS LYS TYR CYS PRO LYS THR PHE ILE ILE VAL
SEQRES 11 C 331 VAL THR ASN PRO LEU ASP CYS MET VAL LYS VAL MET CME
SEQRES 12 C 331 GLU ALA SER GLY VAL PRO THR ASN MET ILE CYS GLY MET
SEQRES 13 C 331 ALA CYS MET LEU ASP SER GLY ARG PHE ARG ARG TYR VAL
SEQRES 14 C 331 ALA ASP ALA LEU SER VAL SER PRO ARG ASP VAL GLN ALA
SEQRES 15 C 331 THR VAL ILE GLY THR HIS GLY ASP CYS MET VAL PRO LEU
SEQRES 16 C 331 VAL ARG TYR ILE THR VAL ASN GLY TYR PRO ILE GLN LYS
SEQRES 17 C 331 PHE ILE LYS ASP GLY VAL VAL THR GLU LYS GLN LEU GLU
SEQRES 18 C 331 GLU ILE ALA GLU HIS THR LYS VAL SER GLY GLY GLU ILE
SEQRES 19 C 331 VAL ARG PHE LEU GLY GLN GLY SER ALA TYR TYR ALA PRO
SEQRES 20 C 331 ALA ALA SER ALA VAL ALA MET ALA THR SER PHE LEU ASN
SEQRES 21 C 331 ASP GLU LYS ARG VAL ILE PRO CYS SER VAL TYR CYS ASN
SEQRES 22 C 331 GLY GLU TYR GLY LEU LYS ASP MET PHE ILE GLY LEU PRO
SEQRES 23 C 331 ALA VAL ILE GLY GLY ALA GLY ILE GLU ARG VAL ILE GLU
SEQRES 24 C 331 LEU GLU LEU ASN GLU GLU GLU LYS LYS GLN PHE GLN LYS
SEQRES 25 C 331 SER VAL ASP ASP VAL MET ALA LEU ASN LYS ALA VAL ALA
SEQRES 26 C 331 ALA LEU GLN ALA PRO GLY
SEQRES 1 D 331 MET ALA PRO ALA LEU VAL GLN ARG ARG LYS LYS VAL ALA
SEQRES 2 D 331 MET ILE GLY SER GLY MET ILE GLY GLY THR MET GLY TYR
SEQRES 3 D 331 LEU CYS ALA LEU ARG GLU LEU ALA ASP VAL VAL LEU TYR
SEQRES 4 D 331 ASP VAL VAL LYS GLY MET PRO GLU GLY LYS ALA LEU ASP
SEQRES 5 D 331 LEU SER HIS VAL THR SER VAL VAL ASP THR ASN VAL SER
SEQRES 6 D 331 VAL ARG ALA GLU TYR SER TYR GLU ALA ALA LEU THR GLY
SEQRES 7 D 331 ALA ASP CYS VAL ILE VAL THR ALA GLY LEU THR LYS VAL
SEQRES 8 D 331 PRO GLY LYS PRO ASP SER GLU TRP SER ARG ASN ASP LEU
SEQRES 9 D 331 LEU PRO PHE ASN SER LYS ILE ILE ARG GLU ILE GLY GLN
SEQRES 10 D 331 ASN ILE LYS LYS TYR CYS PRO LYS THR PHE ILE ILE VAL
SEQRES 11 D 331 VAL THR ASN PRO LEU ASP CYS MET VAL LYS VAL MET CME
SEQRES 12 D 331 GLU ALA SER GLY VAL PRO THR ASN MET ILE CYS GLY MET
SEQRES 13 D 331 ALA CYS MET LEU ASP SER GLY ARG PHE ARG ARG TYR VAL
SEQRES 14 D 331 ALA ASP ALA LEU SER VAL SER PRO ARG ASP VAL GLN ALA
SEQRES 15 D 331 THR VAL ILE GLY THR HIS GLY ASP CYS MET VAL PRO LEU
SEQRES 16 D 331 VAL ARG TYR ILE THR VAL ASN GLY TYR PRO ILE GLN LYS
SEQRES 17 D 331 PHE ILE LYS ASP GLY VAL VAL THR GLU LYS GLN LEU GLU
SEQRES 18 D 331 GLU ILE ALA GLU HIS THR LYS VAL SER GLY GLY GLU ILE
SEQRES 19 D 331 VAL ARG PHE LEU GLY GLN GLY SER ALA TYR TYR ALA PRO
SEQRES 20 D 331 ALA ALA SER ALA VAL ALA MET ALA THR SER PHE LEU ASN
SEQRES 21 D 331 ASP GLU LYS ARG VAL ILE PRO CYS SER VAL TYR CYS ASN
SEQRES 22 D 331 GLY GLU TYR GLY LEU LYS ASP MET PHE ILE GLY LEU PRO
SEQRES 23 D 331 ALA VAL ILE GLY GLY ALA GLY ILE GLU ARG VAL ILE GLU
SEQRES 24 D 331 LEU GLU LEU ASN GLU GLU GLU LYS LYS GLN PHE GLN LYS
SEQRES 25 D 331 SER VAL ASP ASP VAL MET ALA LEU ASN LYS ALA VAL ALA
SEQRES 26 D 331 ALA LEU GLN ALA PRO GLY
MODRES 1PZG CME A 150 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 1PZG CME B 150 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 1PZG CME C 150 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 1PZG CME D 150 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HET CME A 150 10
HET CME B 150 10
HET CME C 150 10
HET CME D 150 10
HET SO4 A 602 5
HET A3D A 601 44
HET SO4 B 604 5
HET A3D B 603 44
HET SO4 C 606 5
HET A3D C 605 44
HET SO4 D 608 5
HET A3D D 607 44
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM SO4 SULFATE ION
HETNAM A3D 3-ACETYLPYRIDINE ADENINE DINUCLEOTIDE
FORMUL 1 CME 4(C5 H11 N O3 S2)
FORMUL 5 SO4 4(O4 S 2-)
FORMUL 6 A3D 4(C22 H28 N6 O14 P2)
FORMUL 13 HOH *562(H2 O)
HELIX 1 1 GLY A 29 GLU A 44 1 15
HELIX 2 2 GLY A 57 VAL A 73A 1 17
HELIX 3 3 SER A 84 THR A 89 1 7
HELIX 4 4 PRO A 103E TRP A 107 5 5
HELIX 5 5 SER A 108 ASP A 111 5 4
HELIX 6 6 LEU A 112 CYS A 131 1 20
HELIX 7 7 PRO A 141 GLY A 154 1 14
HELIX 8 8 PRO A 156 ASN A 158 5 3
HELIX 9 9 ALA A 164 SER A 181 1 18
HELIX 10 10 SER A 183 ARG A 185 5 3
HELIX 11 11 VAL A 203 TYR A 205 5 3
HELIX 12 12 ILE A 210A ASP A 215 1 7
HELIX 13 13 THR A 220 GLY A 242C 1 24
HELIX 14 14 TYR A 247 ASN A 263 1 17
HELIX 15 15 GLU A 278 GLY A 280 5 3
HELIX 16 16 ASN A 308 GLN A 332 1 26
HELIX 17 17 GLY B 29 GLU B 44 1 15
HELIX 18 18 GLY B 57 VAL B 73A 1 17
HELIX 19 19 SER B 84 THR B 89 1 7
HELIX 20 20 PRO B 103E TRP B 107 5 5
HELIX 21 21 ARG B 109 ASP B 111 5 3
HELIX 22 22 LEU B 112 CYS B 131 1 20
HELIX 23 23 PRO B 141 GLY B 154 1 14
HELIX 24 24 PRO B 156 ASN B 158 5 3
HELIX 25 25 ALA B 164 SER B 181 1 18
HELIX 26 26 SER B 183 ARG B 185 5 3
HELIX 27 27 VAL B 203 TYR B 205 5 3
HELIX 28 28 ILE B 210A ASP B 215 1 7
HELIX 29 29 THR B 220 GLY B 242C 1 24
HELIX 30 30 TYR B 247 ASN B 263 1 17
HELIX 31 31 GLU B 278 GLY B 280 5 3
HELIX 32 32 ASN B 308 GLN B 332 1 26
HELIX 33 33 GLY C 29 GLU C 44 1 15
HELIX 34 34 GLY C 57 VAL C 73A 1 17
HELIX 35 35 SER C 84 THR C 89 1 7
HELIX 36 36 PRO C 103E TRP C 107 5 5
HELIX 37 37 SER C 108 ASP C 111 5 4
HELIX 38 38 LEU C 112 CYS C 131 1 20
HELIX 39 39 PRO C 141 GLY C 154 1 14
HELIX 40 40 PRO C 156 ASN C 158 5 3
HELIX 41 41 ALA C 164 SER C 181 1 18
HELIX 42 42 SER C 183 ARG C 185 5 3
HELIX 43 43 VAL C 203 TYR C 205 5 3
HELIX 44 44 ILE C 210A ASP C 215 1 7
HELIX 45 45 THR C 220 GLY C 242C 1 24
HELIX 46 46 TYR C 247 ASN C 263 1 17
HELIX 47 47 GLU C 278 GLY C 280 5 3
HELIX 48 48 ASN C 308 GLN C 332 1 26
HELIX 49 49 GLY D 29 GLU D 44 1 15
HELIX 50 50 GLY D 57 VAL D 73A 1 17
HELIX 51 51 SER D 84 THR D 89 1 7
HELIX 52 52 PRO D 103E TRP D 107 5 5
HELIX 53 53 ARG D 109 ASP D 111 5 3
HELIX 54 54 LEU D 112 CYS D 131 1 20
HELIX 55 55 PRO D 141 GLY D 154 1 14
HELIX 56 56 PRO D 156 ASN D 158 5 3
HELIX 57 57 ALA D 164 SER D 181 1 18
HELIX 58 58 SER D 183 ARG D 185 5 3
HELIX 59 59 VAL D 203 TYR D 205 5 3
HELIX 60 60 ILE D 210A ASP D 215 1 7
HELIX 61 61 THR D 220 GLY D 242C 1 24
HELIX 62 62 TYR D 247 ASN D 263 1 17
HELIX 63 63 GLU D 278 GLY D 280 5 3
HELIX 64 64 ASN D 308 GLN D 332 1 26
SHEET 1 A 6 VAL A 78 ALA A 80 0
SHEET 2 A 6 ASP A 47 TYR A 52 1 N LEU A 51 O ARG A 79
SHEET 3 A 6 LYS A 22 ILE A 26 1 N MET A 25 O VAL A 50
SHEET 4 A 6 CYS A 93 VAL A 96 1 O ILE A 95 N ALA A 24
SHEET 5 A 6 PHE A 134 VAL A 137 1 O ILE A 136 N VAL A 94
SHEET 6 A 6 ILE A 160 GLY A 162 1 O CYS A 161 N VAL A 137
SHEET 1 B 3 VAL A 187 GLN A 188 0
SHEET 2 B 3 THR A 207 VAL A 208 -1 O THR A 207 N GLN A 188
SHEET 3 B 3 TYR A 209C PRO A 209D-1 O TYR A 209C N VAL A 208
SHEET 1 C 2 VAL A 191 ILE A 192 0
SHEET 2 C 2 VAL A 200 PRO A 201 -1 O VAL A 200 N ILE A 192
SHEET 1 D 3 ARG A 267 ASN A 276 0
SHEET 2 D 3 LYS A 282 GLY A 294 -1 O LEU A 289 N CYS A 271
SHEET 3 D 3 GLY A 297 VAL A 302 -1 O GLU A 299 N VAL A 292
SHEET 1 E 6 VAL B 78 ALA B 80 0
SHEET 2 E 6 ASP B 47 TYR B 52 1 N LEU B 51 O ARG B 79
SHEET 3 E 6 LYS B 22 ILE B 26 1 N MET B 25 O VAL B 50
SHEET 4 E 6 CYS B 93 VAL B 96 1 O ILE B 95 N ALA B 24
SHEET 5 E 6 PHE B 134 VAL B 137 1 O ILE B 136 N VAL B 94
SHEET 6 E 6 ILE B 160 GLY B 162 1 O CYS B 161 N VAL B 137
SHEET 1 F 3 VAL B 187 GLN B 188 0
SHEET 2 F 3 THR B 207 VAL B 208 -1 O THR B 207 N GLN B 188
SHEET 3 F 3 TYR B 209C PRO B 209D-1 O TYR B 209C N VAL B 208
SHEET 1 G 2 VAL B 191 ILE B 192 0
SHEET 2 G 2 VAL B 200 PRO B 201 -1 O VAL B 200 N ILE B 192
SHEET 1 H 3 ARG B 267 ASN B 276 0
SHEET 2 H 3 LYS B 282 GLY B 294 -1 O MET B 285 N CYS B 275
SHEET 3 H 3 GLY B 297 VAL B 302 -1 O GLU B 299 N VAL B 292
SHEET 1 I 6 VAL C 78 ALA C 80 0
SHEET 2 I 6 ASP C 47 TYR C 52 1 N LEU C 51 O ARG C 79
SHEET 3 I 6 LYS C 22 ILE C 26 1 N MET C 25 O VAL C 50
SHEET 4 I 6 CYS C 93 VAL C 96 1 O ILE C 95 N ALA C 24
SHEET 5 I 6 PHE C 134 VAL C 137 1 O ILE C 136 N VAL C 94
SHEET 6 I 6 ILE C 160 GLY C 162 1 O CYS C 161 N VAL C 137
SHEET 1 J 3 VAL C 187 GLN C 188 0
SHEET 2 J 3 THR C 207 VAL C 208 -1 O THR C 207 N GLN C 188
SHEET 3 J 3 TYR C 209C PRO C 209D-1 O TYR C 209C N VAL C 208
SHEET 1 K 2 VAL C 191 ILE C 192 0
SHEET 2 K 2 VAL C 200 PRO C 201 -1 O VAL C 200 N ILE C 192
SHEET 1 L 3 ARG C 267 ASN C 276 0
SHEET 2 L 3 LYS C 282 GLY C 294 -1 O ALA C 291 N ILE C 269
SHEET 3 L 3 GLY C 297 VAL C 302 -1 O GLY C 297 N GLY C 294
SHEET 1 M 6 VAL D 78 ALA D 80 0
SHEET 2 M 6 ASP D 47 TYR D 52 1 N LEU D 51 O ARG D 79
SHEET 3 M 6 LYS D 22 ILE D 26 1 N MET D 25 O VAL D 50
SHEET 4 M 6 CYS D 93 VAL D 96 1 O ILE D 95 N ALA D 24
SHEET 5 M 6 PHE D 134 VAL D 137 1 O ILE D 136 N VAL D 94
SHEET 6 M 6 ILE D 160 GLY D 162 1 O CYS D 161 N VAL D 137
SHEET 1 N 3 VAL D 187 GLN D 188 0
SHEET 2 N 3 THR D 207 VAL D 208 -1 O THR D 207 N GLN D 188
SHEET 3 N 3 TYR D 209C PRO D 209D-1 O TYR D 209C N VAL D 208
SHEET 1 O 2 VAL D 191 ILE D 192 0
SHEET 2 O 2 VAL D 200 PRO D 201 -1 O VAL D 200 N ILE D 192
SHEET 1 P 3 ARG D 267 ASN D 276 0
SHEET 2 P 3 LYS D 282 GLY D 294 -1 O LEU D 289 N CYS D 271
SHEET 3 P 3 GLY D 297 VAL D 302 -1 O GLU D 299 N VAL D 292
LINK C MET A 149 N CME A 150 1555 1555 1.33
LINK C CME A 150 N GLU A 151 1555 1555 1.33
LINK C MET B 149 N CME B 150 1555 1555 1.33
LINK C CME B 150 N GLU B 151 1555 1555 1.32
LINK C MET C 149 N CME C 150 1555 1555 1.33
LINK C CME C 150 N GLU C 151 1555 1555 1.32
LINK C MET D 149 N CME D 150 1555 1555 1.32
LINK C CME D 150 N GLU D 151 1555 1555 1.33
CISPEP 1 ASN A 140 PRO A 141 0 -0.60
CISPEP 2 ASN B 140 PRO B 141 0 -0.55
CISPEP 3 ASN C 140 PRO C 141 0 -0.32
CISPEP 4 ASN D 140 PRO D 141 0 -0.53
SITE 1 AC1 9 TRP A 107 ARG A 109 ASN A 140 ARG A 171
SITE 2 AC1 9 HIS A 195 GLY A 236 ALA A 246 A3D A 601
SITE 3 AC1 9 HOH A 642
SITE 1 AC2 10 TRP B 107 ARG B 109 ASN B 140 LEU B 167
SITE 2 AC2 10 ARG B 171 HIS B 195 GLY B 236 ALA B 246
SITE 3 AC2 10 A3D B 603 HOH B 618
SITE 1 AC3 7 TRP C 107 ARG C 109 ARG C 171 HIS C 195
SITE 2 AC3 7 GLY C 236 A3D C 605 HOH C 639
SITE 1 AC4 9 TRP D 107 ARG D 109 LEU D 167 ARG D 171
SITE 2 AC4 9 HIS D 195 GLY D 236 ALA D 246 A3D D 607
SITE 3 AC4 9 HOH D 635
SITE 1 AC5 30 GLY A 29 MET A 30 ILE A 31 TYR A 52
SITE 2 AC5 30 ASP A 53 VAL A 54 VAL A 55 MET A 58
SITE 3 AC5 30 THR A 97 ALA A 98 GLY A 99 LEU A 100
SITE 4 AC5 30 THR A 101 ILE A 119 VAL A 138 THR A 139
SITE 5 AC5 30 ASN A 140 LEU A 142 MET A 163 LEU A 167
SITE 6 AC5 30 HIS A 195 ALA A 246 SO4 A 602 HOH A 605
SITE 7 AC5 30 HOH A 610 HOH A 659 HOH A 678 HOH A 694
SITE 8 AC5 30 HOH A 710 HOH A 760
SITE 1 AC6 30 GLY B 29 MET B 30 ILE B 31 ASP B 53
SITE 2 AC6 30 VAL B 54 VAL B 55 MET B 58 THR B 97
SITE 3 AC6 30 ALA B 98 GLY B 99 LEU B 100 THR B 101
SITE 4 AC6 30 ILE B 119 VAL B 138 THR B 139 ASN B 140
SITE 5 AC6 30 LEU B 142 MET B 163 LEU B 167 HIS B 195
SITE 6 AC6 30 ALA B 246 PRO B 250 SO4 B 604 HOH B 615
SITE 7 AC6 30 HOH B 619 HOH B 651 HOH B 686 HOH B 716
SITE 8 AC6 30 HOH B 744 HOH B 748
SITE 1 AC7 27 GLY C 29 MET C 30 ILE C 31 TYR C 52
SITE 2 AC7 27 ASP C 53 VAL C 54 VAL C 55 MET C 58
SITE 3 AC7 27 THR C 97 ALA C 98 GLY C 99 LEU C 100
SITE 4 AC7 27 THR C 101 ILE C 119 VAL C 138 ASN C 140
SITE 5 AC7 27 LEU C 142 MET C 163 LEU C 167 HIS C 195
SITE 6 AC7 27 ALA C 246 SO4 C 606 HOH C 613 HOH C 622
SITE 7 AC7 27 HOH C 694 HOH C 721 HOH C 723
SITE 1 AC8 28 GLY D 29 MET D 30 ILE D 31 ASP D 53
SITE 2 AC8 28 VAL D 54 VAL D 55 MET D 58 THR D 97
SITE 3 AC8 28 ALA D 98 GLY D 99 LEU D 100 THR D 101
SITE 4 AC8 28 ILE D 119 VAL D 138 THR D 139 ASN D 140
SITE 5 AC8 28 LEU D 142 MET D 163 LEU D 167 HIS D 195
SITE 6 AC8 28 ALA D 246 SO4 D 608 HOH D 612 HOH D 628
SITE 7 AC8 28 HOH D 645 HOH D 716 HOH D 727 HOH D 729
CRYST1 67.935 124.978 86.388 90.00 105.94 90.00 P 1 21 1 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 0.014720 0.000000 0.004204 0.00000
SCALE2 0.000000 0.008001 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012039 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
