HEADER STRUCTURAL PROTEIN 16-OCT-06 2IS8
TITLE CRYSTAL STRUCTURE OF THE MOLYBDOPTERIN BIOSYNTHESIS ENZYME MOAB
TITLE 2 (TTHA0341) FROM THERMUS THEROMOPHILUS HB8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MOLYBDOPTERIN BIOSYNTHESIS ENZYME, MOAB;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS MOAB, GLOBULAR ALPHA/BETA FOLD, BIOSYNTHESIS ENZYME, STRUCTURAL
KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND
KEYWDS 3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.JEYAKANTHAN,S.P.KANAUJIA,C.VASUKI RANJANI,K.SEKAR,S.BABA,A.EBIHARA,
AUTHOR 2 S.KURAMITSU,A.SHINKAI,Y.SHIRO,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 3 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 5 25-OCT-23 2IS8 1 REMARK
REVDAT 4 13-JUL-11 2IS8 1 VERSN
REVDAT 3 24-FEB-09 2IS8 1 VERSN
REVDAT 2 11-DEC-07 2IS8 1 REMARK
REVDAT 1 30-OCT-07 2IS8 0
JRNL AUTH J.JEYAKANTHAN,S.P.KANAUJIA,C.VASUKI RANJANI,K.SEKAR,S.BABA,
JRNL AUTH 2 A.EBIHARA,S.KURAMITSU,A.SHINKAI,Y.SHIRO,S.YOKOYAMA
JRNL TITL CRYSTAL STRUCTURE OF THE MOLYBDOPTERIN BIOSYNTHESIS ENZYME
JRNL TITL 2 MOAB (TTHA0341) FROM THERMUS THEROMOPHILUS HB8
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.64 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 7955895.810
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 47909
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 : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2403
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.64
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.71
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5066
REMARK 3 BIN R VALUE (WORKING SET) : 0.2680
REMARK 3 BIN FREE R VALUE : 0.3010
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 265
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3652
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 748
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.70000
REMARK 3 B22 (A**2) : -0.60000
REMARK 3 B33 (A**2) : -2.11000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -6.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.18
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) : 0.20
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.17
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.990
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) : 1.780 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.680 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.870 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.150 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 70.96
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 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : LIGAND.PAR
REMARK 3 PARAMETER FILE 5 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : LIGAND.TOP
REMARK 3 TOPOLOGY FILE 5 : WATER_PROTIN.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2IS8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-OCT-06.
REMARK 100 THE DEPOSITION ID IS D_1000039951.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUL-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI 1 1 1 DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : RH COATED BENT-CYRINDRICAL
REMARK 200 MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS V
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48481
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.640
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : 0.06300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.23200
REMARK 200 R SYM FOR SHELL (I) : 0.25500
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: CNS
REMARK 200 STARTING MODEL: 1JLJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.2M TRI-POTASSIUM
REMARK 280 CITRATE MONOHYDRATE, PH 8.3, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 51.65800
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 GLU A 160
REMARK 465 GLY A 161
REMARK 465 HIS A 162
REMARK 465 HIS A 163
REMARK 465 GLU A 164
REMARK 465 HIS B 162
REMARK 465 HIS B 163
REMARK 465 GLU B 164
REMARK 465 GLU C 160
REMARK 465 GLY C 161
REMARK 465 HIS C 162
REMARK 465 HIS C 163
REMARK 465 GLU C 164
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O ARG B 15 CG GLU C 46 2746 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 15 CB - CA - C ANGL. DEV. = -24.7 DEGREES
REMARK 500 ARG B 15 N - CA - C ANGL. DEV. = 32.6 DEGREES
REMARK 500 GLY B 16 N - CA - C ANGL. DEV. = -26.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP B 45 43.30 -79.71
REMARK 500 LYS B 106 -62.38 -107.06
REMARK 500 SER C 10 118.91 -165.16
REMARK 500 ASP C 78 106.20 -59.45
REMARK 500 TRP C 158 -51.47 -138.27
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 FMT B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1003
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TTK003000251.1 RELATED DB: TARGETDB
DBREF 2IS8 A 1 164 UNP Q5SLF2 Q5SLF2_THET8 1 164
DBREF 2IS8 B 1 164 UNP Q5SLF2 Q5SLF2_THET8 1 164
DBREF 2IS8 C 1 164 UNP Q5SLF2 Q5SLF2_THET8 1 164
SEQRES 1 A 164 MET PHE ARG VAL GLY ILE LEU THR VAL SER ASP LYS GLY
SEQRES 2 A 164 PHE ARG GLY GLU ARG GLN ASP THR THR HIS LEU ALA ILE
SEQRES 3 A 164 ARG GLU VAL LEU ALA GLY GLY PRO PHE GLU VAL ALA ALA
SEQRES 4 A 164 TYR GLU LEU VAL PRO ASP GLU PRO PRO MET ILE LYS LYS
SEQRES 5 A 164 VAL LEU ARG LEU TRP ALA ASP ARG GLU GLY LEU ASP LEU
SEQRES 6 A 164 ILE LEU THR ASN GLY GLY THR GLY LEU ALA PRO ARG ASP
SEQRES 7 A 164 ARG THR PRO GLU ALA THR ARG GLU LEU LEU ASP ARG GLU
SEQRES 8 A 164 VAL PRO GLY LEU ALA GLU LEU MET ARG LEU VAL GLY LEU
SEQRES 9 A 164 ARG LYS THR PRO MET ALA ALA LEU SER ARG GLY VAL ALA
SEQRES 10 A 164 GLY VAL ARG GLY ARG THR LEU ILE LEU ASN LEU PRO GLY
SEQRES 11 A 164 SER PRO LYS GLY ALA ARG GLU SER LEU GLU ALA VAL LEU
SEQRES 12 A 164 PRO VAL LEU PRO HIS ALA LEU SER LEU VAL THR GLY LYS
SEQRES 13 A 164 PRO TRP LYS GLU GLY HIS HIS GLU
SEQRES 1 B 164 MET PHE ARG VAL GLY ILE LEU THR VAL SER ASP LYS GLY
SEQRES 2 B 164 PHE ARG GLY GLU ARG GLN ASP THR THR HIS LEU ALA ILE
SEQRES 3 B 164 ARG GLU VAL LEU ALA GLY GLY PRO PHE GLU VAL ALA ALA
SEQRES 4 B 164 TYR GLU LEU VAL PRO ASP GLU PRO PRO MET ILE LYS LYS
SEQRES 5 B 164 VAL LEU ARG LEU TRP ALA ASP ARG GLU GLY LEU ASP LEU
SEQRES 6 B 164 ILE LEU THR ASN GLY GLY THR GLY LEU ALA PRO ARG ASP
SEQRES 7 B 164 ARG THR PRO GLU ALA THR ARG GLU LEU LEU ASP ARG GLU
SEQRES 8 B 164 VAL PRO GLY LEU ALA GLU LEU MET ARG LEU VAL GLY LEU
SEQRES 9 B 164 ARG LYS THR PRO MET ALA ALA LEU SER ARG GLY VAL ALA
SEQRES 10 B 164 GLY VAL ARG GLY ARG THR LEU ILE LEU ASN LEU PRO GLY
SEQRES 11 B 164 SER PRO LYS GLY ALA ARG GLU SER LEU GLU ALA VAL LEU
SEQRES 12 B 164 PRO VAL LEU PRO HIS ALA LEU SER LEU VAL THR GLY LYS
SEQRES 13 B 164 PRO TRP LYS GLU GLY HIS HIS GLU
SEQRES 1 C 164 MET PHE ARG VAL GLY ILE LEU THR VAL SER ASP LYS GLY
SEQRES 2 C 164 PHE ARG GLY GLU ARG GLN ASP THR THR HIS LEU ALA ILE
SEQRES 3 C 164 ARG GLU VAL LEU ALA GLY GLY PRO PHE GLU VAL ALA ALA
SEQRES 4 C 164 TYR GLU LEU VAL PRO ASP GLU PRO PRO MET ILE LYS LYS
SEQRES 5 C 164 VAL LEU ARG LEU TRP ALA ASP ARG GLU GLY LEU ASP LEU
SEQRES 6 C 164 ILE LEU THR ASN GLY GLY THR GLY LEU ALA PRO ARG ASP
SEQRES 7 C 164 ARG THR PRO GLU ALA THR ARG GLU LEU LEU ASP ARG GLU
SEQRES 8 C 164 VAL PRO GLY LEU ALA GLU LEU MET ARG LEU VAL GLY LEU
SEQRES 9 C 164 ARG LYS THR PRO MET ALA ALA LEU SER ARG GLY VAL ALA
SEQRES 10 C 164 GLY VAL ARG GLY ARG THR LEU ILE LEU ASN LEU PRO GLY
SEQRES 11 C 164 SER PRO LYS GLY ALA ARG GLU SER LEU GLU ALA VAL LEU
SEQRES 12 C 164 PRO VAL LEU PRO HIS ALA LEU SER LEU VAL THR GLY LYS
SEQRES 13 C 164 PRO TRP LYS GLU GLY HIS HIS GLU
HET FMT A1003 3
HET FMT B1001 3
HET FMT C1002 3
HETNAM FMT FORMIC ACID
FORMUL 4 FMT 3(C H2 O2)
FORMUL 7 HOH *748(H2 O)
HELIX 1 1 SER A 10 GLY A 16 1 7
HELIX 2 2 THR A 21 ALA A 31 1 11
HELIX 3 3 GLU A 46 ARG A 60 1 15
HELIX 4 4 ARG A 79 GLU A 86 1 8
HELIX 5 5 VAL A 92 ARG A 100 1 9
HELIX 6 6 PRO A 108 SER A 113 5 6
HELIX 7 7 SER A 131 LEU A 143 1 13
HELIX 8 8 VAL A 145 GLY A 155 1 11
HELIX 9 9 ASP B 11 ARG B 15 5 5
HELIX 10 10 ASP B 20 ALA B 31 1 12
HELIX 11 11 GLU B 46 ARG B 60 1 15
HELIX 12 12 ARG B 79 GLU B 86 1 8
HELIX 13 13 VAL B 92 ARG B 100 1 9
HELIX 14 14 THR B 107 SER B 113 5 7
HELIX 15 15 SER B 131 LEU B 143 1 13
HELIX 16 16 VAL B 145 GLY B 155 1 11
HELIX 17 17 SER C 10 ARG C 15 1 6
HELIX 18 18 THR C 21 ALA C 31 1 11
HELIX 19 19 GLU C 46 ARG C 60 1 15
HELIX 20 20 ARG C 79 GLU C 86 1 8
HELIX 21 21 VAL C 92 ARG C 100 1 9
HELIX 22 22 PRO C 108 SER C 113 5 6
HELIX 23 23 SER C 131 LEU C 143 1 13
HELIX 24 24 VAL C 145 GLY C 155 1 11
SHEET 1 A 6 PHE A 35 VAL A 43 0
SHEET 2 A 6 PHE A 2 VAL A 9 1 N VAL A 4 O GLU A 36
SHEET 3 A 6 LEU A 65 ASN A 69 1 O LEU A 67 N GLY A 5
SHEET 4 A 6 THR A 123 LEU A 128 1 O LEU A 128 N THR A 68
SHEET 5 A 6 ALA A 117 ARG A 120 -1 N GLY A 118 O ILE A 125
SHEET 6 A 6 ARG A 90 GLU A 91 -1 N ARG A 90 O VAL A 119
SHEET 1 B 6 PHE B 35 VAL B 43 0
SHEET 2 B 6 PHE B 2 VAL B 9 1 N VAL B 4 O GLU B 36
SHEET 3 B 6 LEU B 65 ASN B 69 1 O LEU B 67 N GLY B 5
SHEET 4 B 6 THR B 123 LEU B 128 1 O LEU B 128 N THR B 68
SHEET 5 B 6 ALA B 117 ARG B 120 -1 N GLY B 118 O ILE B 125
SHEET 6 B 6 ARG B 90 GLU B 91 -1 N ARG B 90 O VAL B 119
SHEET 1 C 6 PHE C 35 VAL C 43 0
SHEET 2 C 6 PHE C 2 VAL C 9 1 N VAL C 4 O GLU C 36
SHEET 3 C 6 LEU C 65 ASN C 69 1 O LEU C 67 N GLY C 5
SHEET 4 C 6 THR C 123 LEU C 128 1 O LEU C 128 N THR C 68
SHEET 5 C 6 ALA C 117 ARG C 120 -1 N GLY C 118 O ILE C 125
SHEET 6 C 6 ARG C 90 GLU C 91 -1 N ARG C 90 O VAL C 119
SITE 1 AC1 4 ASP B 20 TYR B 40 HOH B 418 HOH B 808
SITE 1 AC2 6 SER C 10 GLN C 19 ASP C 20 HOH C 305
SITE 2 AC2 6 HOH C 824 HOH C 890
SITE 1 AC3 6 THR A 8 ASP A 20 HOH A 211 HOH A 290
SITE 2 AC3 6 HOH A 789 HOH A 859
CRYST1 33.935 103.316 59.592 90.00 101.33 90.00 P 1 21 1 6
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 0.029468 0.000000 0.005905 0.00000
SCALE2 0.000000 0.009679 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017114 0.00000
(ATOM LINES ARE NOT SHOWN.)
END