HEADER LIGASE 03-APR-07 2YS7
TITLE CRYSTAL STRUCTURE OF GAR SYNTHETASE FROM GEOBACILLUS KAUSTOPHILUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHORIBOSYLGLYCINAMIDE SYNTHETASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GLYCINAMIDE RIBONUCLEOTIDE SYNTHETASE,
COMPND 5 PHOSPHORIBOSYLGLYCINAMIDE SYNTHETASE;
COMPND 6 EC: 6.3.4.13;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS KAUSTOPHILUS;
SOURCE 3 ORGANISM_TAXID: 1462;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET-HISTEV
KEYWDS GLYCINAMIDE RIBONUCLEOTIDE SYNTHETASE, GAR SYNTHETASE, ATP BINDING,
KEYWDS 2 PURINE NUCLEOTIDE BIOSYNTHETIC PATHWAY, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 3 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 4 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BABA,M.KANAGAWA,S.KURAMITSU,S.YOKOYAMA,G.KAWAI,G.SAMPEI,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 25-OCT-23 2YS7 1 SEQADV
REVDAT 3 08-DEC-10 2YS7 1 JRNL
REVDAT 2 24-FEB-09 2YS7 1 VERSN
REVDAT 1 09-OCT-07 2YS7 0
JRNL AUTH G.SAMPEI,S.BABA,M.KANAGAWA,H.YANAI,T.ISHII,H.KAWAI,Y.FUKAI,
JRNL AUTH 2 A.EBIHARA,N.NAKAGAWA,G.KAWAI
JRNL TITL CRYSTAL STRUCTURES OF GLYCINAMIDE RIBONUCLEOTIDE SYNTHETASE,
JRNL TITL 2 PURD, FROM THERMOPHILIC EUBACTERIA
JRNL REF J.BIOCHEM. V. 148 429 2010
JRNL REFN ISSN 0021-924X
JRNL PMID 20716513
JRNL DOI 10.1093/JB/MVQ088
REMARK 2
REMARK 2 RESOLUTION. 2.21 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 : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 258577.850
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 20565
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) : 0.208
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2023
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) (%) : 84.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2627
REMARK 3 BIN R VALUE (WORKING SET) : 0.2330
REMARK 3 BIN FREE R VALUE : 0.3000
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 304
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3102
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 160
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.83000
REMARK 3 B22 (A**2) : 0.76000
REMARK 3 B33 (A**2) : -1.59000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.17
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) : 0.33
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.29
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.780
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 : 48.91
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2YS7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1000027067.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B1
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 : FIXED EXIT SI 111 DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU JUPITER 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20854
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
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) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2031.
REMARK 200 R MERGE FOR SHELL (I) : 0.15100
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: PDB ENTRY 2YRW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS HYDROCHLORIDE, 2M AMMONIUM
REMARK 280 SULFATE, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
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 25.61550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.36300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.77600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.36300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.61550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.77600
REMARK 290 SMTRY3 4 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: 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 -21
REMARK 465 GLY A -20
REMARK 465 SER A -19
REMARK 465 SER A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 GLY A -9
REMARK 465 GLU A -8
REMARK 465 ASN A -7
REMARK 465 LEU A -6
REMARK 465 TYR A -5
REMARK 465 PHE A -4
REMARK 465 GLN A -3
REMARK 465 SER A -2
REMARK 465 GLY A 146
REMARK 465 LEU A 147
REMARK 465 ALA A 148
REMARK 465 ALA A 149
REMARK 465 GLY A 150
REMARK 465 LYS A 151
REMARK 465 ARG A 419
REMARK 465 ALA A 420
REMARK 465 SER A 421
REMARK 465 ALA A 422
REMARK 465 ALA A 423
REMARK 465 TYR A 424
REMARK 465 THR A 425
REMARK 465 ARG A 426
REMARK 465 MET A 427
REMARK 465 LYS A 428
REMARK 465 GLY A 429
REMARK 465 ARG A 430
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 GLU A 134 9.18 -68.51
REMARK 500 ILE A 249 -64.04 -120.21
REMARK 500 ASN A 373 51.77 -158.61
REMARK 500 CYS A 403 110.87 -169.85
REMARK 500 TYR A 408 146.33 -171.81
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 ARG A 410 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2YRW RELATED DB: PDB
REMARK 900 GAR SYNTHETASE FROM GEOBACILLUS KAUSTOPHILUS
REMARK 900 RELATED ID: GKA001000268.4 RELATED DB: TARGETDB
DBREF 2YS7 A 1 430 UNP Q5L3C7 Q5L3C7_GEOKA 1 430
SEQADV 2YS7 MET A -21 UNP Q5L3C7 EXPRESSION TAG
SEQADV 2YS7 GLY A -20 UNP Q5L3C7 EXPRESSION TAG
SEQADV 2YS7 SER A -19 UNP Q5L3C7 EXPRESSION TAG
SEQADV 2YS7 SER A -18 UNP Q5L3C7 EXPRESSION TAG
SEQADV 2YS7 HIS A -17 UNP Q5L3C7 EXPRESSION TAG
SEQADV 2YS7 HIS A -16 UNP Q5L3C7 EXPRESSION TAG
SEQADV 2YS7 HIS A -15 UNP Q5L3C7 EXPRESSION TAG
SEQADV 2YS7 HIS A -14 UNP Q5L3C7 EXPRESSION TAG
SEQADV 2YS7 HIS A -13 UNP Q5L3C7 EXPRESSION TAG
SEQADV 2YS7 HIS A -12 UNP Q5L3C7 EXPRESSION TAG
SEQADV 2YS7 SER A -11 UNP Q5L3C7 EXPRESSION TAG
SEQADV 2YS7 SER A -10 UNP Q5L3C7 EXPRESSION TAG
SEQADV 2YS7 GLY A -9 UNP Q5L3C7 EXPRESSION TAG
SEQADV 2YS7 GLU A -8 UNP Q5L3C7 EXPRESSION TAG
SEQADV 2YS7 ASN A -7 UNP Q5L3C7 EXPRESSION TAG
SEQADV 2YS7 LEU A -6 UNP Q5L3C7 EXPRESSION TAG
SEQADV 2YS7 TYR A -5 UNP Q5L3C7 EXPRESSION TAG
SEQADV 2YS7 PHE A -4 UNP Q5L3C7 EXPRESSION TAG
SEQADV 2YS7 GLN A -3 UNP Q5L3C7 EXPRESSION TAG
SEQADV 2YS7 SER A -2 UNP Q5L3C7 EXPRESSION TAG
SEQADV 2YS7 HIS A -1 UNP Q5L3C7 EXPRESSION TAG
SEQRES 1 A 451 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 451 GLU ASN LEU TYR PHE GLN SER HIS MET ASN VAL LEU VAL
SEQRES 3 A 451 ILE GLY ARG GLY GLY ARG GLU HIS ALA ILE ALA TRP LYS
SEQRES 4 A 451 ALA ALA GLN SER PRO LEU VAL GLY LYS LEU TYR VAL ALA
SEQRES 5 A 451 PRO GLY ASN PRO GLY ILE ALA ASP VAL ALA GLU LEU VAL
SEQRES 6 A 451 HIS ILE ASP GLU LEU ASP ILE GLU ALA LEU VAL GLN PHE
SEQRES 7 A 451 ALA LYS GLN GLN ALA ILE ASP LEU THR ILE VAL GLY PRO
SEQRES 8 A 451 GLU ALA PRO LEU ALA SER GLY ILE VAL ASP ARG PHE MET
SEQRES 9 A 451 ALA GLU GLY LEU ARG ILE PHE GLY PRO SER GLN ARG ALA
SEQRES 10 A 451 ALA LEU ILE GLU GLY SER LYS ALA PHE ALA LYS GLU LEU
SEQRES 11 A 451 MET LYS LYS TYR GLY ILE PRO THR ALA ASP HIS ALA ALA
SEQRES 12 A 451 PHE THR SER TYR GLU GLU ALA LYS ALA TYR ILE GLU GLN
SEQRES 13 A 451 LYS GLY ALA PRO ILE VAL ILE LYS ALA ASP GLY LEU ALA
SEQRES 14 A 451 ALA GLY LYS GLY VAL THR VAL ALA GLN THR VAL GLU GLU
SEQRES 15 A 451 ALA LEU ALA ALA ALA LYS ALA ALA LEU VAL ASP GLY GLN
SEQRES 16 A 451 PHE GLY THR ALA GLY SER GLN VAL VAL ILE GLU GLU TYR
SEQRES 17 A 451 LEU GLU GLY GLU GLU PHE SER PHE MET ALA PHE VAL ASN
SEQRES 18 A 451 GLY GLU LYS VAL TYR PRO LEU ALA ILE ALA GLN ASP HIS
SEQRES 19 A 451 LYS ARG ALA TYR ASP GLY ASP GLU GLY PRO ASN THR GLY
SEQRES 20 A 451 GLY MET GLY ALA TYR SER PRO VAL PRO GLN ILE SER ASP
SEQRES 21 A 451 GLU MET MET ASP ALA ALA LEU GLU ALA ILE LEU ARG PRO
SEQRES 22 A 451 ALA ALA LYS ALA LEU ALA ALA GLU GLY ARG PRO PHE LEU
SEQRES 23 A 451 GLY VAL LEU TYR ALA GLY LEU MET ALA THR ALA ASN GLY
SEQRES 24 A 451 PRO LYS VAL ILE GLU PHE ASN ALA ARG PHE GLY ASP PRO
SEQRES 25 A 451 GLU ALA GLN VAL VAL LEU PRO ARG LEU LYS THR ASP LEU
SEQRES 26 A 451 VAL GLU ALA VAL LEU ALA VAL MET ASP GLY LYS GLU LEU
SEQRES 27 A 451 GLU LEU GLU TRP THR ASP GLU ALA VAL LEU GLY VAL VAL
SEQRES 28 A 451 LEU ALA ALA LYS GLY TYR PRO GLY ALA TYR GLU ARG GLY
SEQRES 29 A 451 ALA GLU ILE ARG GLY LEU ASP ARG ILE SER PRO ASP ALA
SEQRES 30 A 451 LEU LEU PHE HIS ALA GLY THR LYS ARG GLU GLY GLY ALA
SEQRES 31 A 451 TRP TYR THR ASN GLY GLY ARG VAL LEU LEU LEU ALA ALA
SEQRES 32 A 451 LYS GLY GLU THR LEU ALA LYS ALA LYS GLU LYS ALA TYR
SEQRES 33 A 451 GLU GLN LEU ALA ALA ILE ASP CYS ASP GLY LEU PHE TYR
SEQRES 34 A 451 ARG ARG ASP ILE GLY ARG ARG ALA ILE GLU ARG ALA SER
SEQRES 35 A 451 ALA ALA TYR THR ARG MET LYS GLY ARG
FORMUL 2 HOH *160(H2 O)
HELIX 1 1 GLY A 9 ALA A 20 1 12
HELIX 2 2 GLY A 36 VAL A 40 5 5
HELIX 3 3 ASP A 50 GLN A 61 1 12
HELIX 4 4 PRO A 70 SER A 76 1 7
HELIX 5 5 GLY A 77 ALA A 84 1 8
HELIX 6 6 ALA A 97 SER A 102 1 6
HELIX 7 7 SER A 102 TYR A 113 1 12
HELIX 8 8 SER A 125 GLY A 137 1 13
HELIX 9 9 THR A 158 GLY A 173 1 16
HELIX 10 10 SER A 238 ILE A 249 1 12
HELIX 11 11 ILE A 249 GLU A 260 1 12
HELIX 12 12 PRO A 291 LEU A 297 1 7
HELIX 13 13 PRO A 298 LEU A 300 5 3
HELIX 14 14 ASP A 303 ASP A 313 1 11
HELIX 15 15 THR A 386 ALA A 399 1 14
HELIX 16 16 GLY A 413 GLU A 418 1 6
SHEET 1 A 5 GLU A 42 LEU A 43 0
SHEET 2 A 5 VAL A 25 PRO A 32 1 N LEU A 28 O GLU A 42
SHEET 3 A 5 MET A 1 GLY A 7 1 N MET A 1 O GLY A 26
SHEET 4 A 5 LEU A 65 VAL A 68 1 O ILE A 67 N ILE A 6
SHEET 5 A 5 ILE A 89 PHE A 90 1 O PHE A 90 N THR A 66
SHEET 1 B 4 HIS A 120 PHE A 123 0
SHEET 2 B 4 VAL A 182 GLU A 186 -1 O ILE A 184 N ALA A 121
SHEET 3 B 4 ILE A 140 LYS A 143 -1 N LYS A 143 O VAL A 183
SHEET 4 B 4 VAL A 153 ALA A 156 -1 O THR A 154 N ILE A 142
SHEET 1 C 4 LYS A 203 PRO A 206 0
SHEET 2 C 4 GLU A 191 ASN A 200 -1 N PHE A 198 O TYR A 205
SHEET 3 C 4 LEU A 265 THR A 275 -1 O ALA A 274 N GLU A 191
SHEET 4 C 4 GLY A 278 ASN A 285 -1 O ILE A 282 N GLY A 271
SHEET 1 D 5 GLN A 211 ASP A 212 0
SHEET 2 D 5 GLY A 229 SER A 232 -1 O TYR A 231 N GLN A 211
SHEET 3 D 5 ALA A 325 ALA A 333 -1 O GLY A 328 N ALA A 230
SHEET 4 D 5 ARG A 376 GLY A 384 -1 O LEU A 378 N LEU A 331
SHEET 5 D 5 LEU A 357 HIS A 360 -1 N LEU A 357 O ALA A 381
SHEET 1 E 4 GLN A 211 ASP A 212 0
SHEET 2 E 4 GLY A 229 SER A 232 -1 O TYR A 231 N GLN A 211
SHEET 3 E 4 ALA A 325 ALA A 333 -1 O GLY A 328 N ALA A 230
SHEET 4 E 4 LEU A 406 PHE A 407 -1 O PHE A 407 N ALA A 332
SHEET 1 F 2 ARG A 215 TYR A 217 0
SHEET 2 F 2 GLU A 221 ASN A 224 -1 O GLU A 221 N TYR A 217
SHEET 1 G 3 GLU A 345 ILE A 346 0
SHEET 2 G 3 ALA A 369 THR A 372 -1 O TRP A 370 N ILE A 346
SHEET 3 G 3 THR A 363 GLU A 366 -1 N LYS A 364 O TYR A 371
CISPEP 1 ALA A 31 PRO A 32 0 -0.07
CISPEP 2 ALA A 138 PRO A 139 0 -0.08
CISPEP 3 SER A 232 PRO A 233 0 -0.01
CISPEP 4 ASP A 290 PRO A 291 0 0.72
CISPEP 5 TYR A 336 PRO A 337 0 0.20
CRYST1 51.231 83.552 94.726 90.00 90.00 90.00 P 21 21 21 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 0.019519 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011969 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010557 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
