HEADER TRANSFERASE 30-JUN-06 2DSJ
TITLE CRYSTAL STRUCTURE OF PROJECT ID TT0128 FROM THERMUS THERMOPHILUS HB8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRIMIDINE-NUCLEOSIDE (THYMIDINE) PHOSPHORYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.4.2.2;
COMPND 5 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 PYRIMIDINE-NUCLEOSIDE PHOSPHORYLASE, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.SHIMIZU,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 25-OCT-23 2DSJ 1 REMARK
REVDAT 3 13-JUL-11 2DSJ 1 VERSN
REVDAT 2 24-FEB-09 2DSJ 1 VERSN
REVDAT 1 30-DEC-06 2DSJ 0
JRNL AUTH K.SHIMIZU,N.KUNISHIMA
JRNL TITL CRYSTAL STRUCTURE OF PROJECT ID TT0128 FROM THERMUS
JRNL TITL 2 THERMOPHILUS HB8
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1101798.620
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 84608
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) : 0.198
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4264
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 13275
REMARK 3 BIN R VALUE (WORKING SET) : 0.2510
REMARK 3 BIN FREE R VALUE : 0.2750
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 673
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6384
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 830
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.32000
REMARK 3 B22 (A**2) : -0.19000
REMARK 3 B33 (A**2) : 3.51000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.57000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.16
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) : 0.23
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) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.790
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) : 1.300 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.960 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.300 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.550 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 50.53
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DSJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUL-06.
REMARK 100 THE DEPOSITION ID IS D_1000025792.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAY-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84608
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : 0.06800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.28200
REMARK 200 R SYM FOR SHELL (I) : 0.23300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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 1BRW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27.5W/W(%) PEG 4000, 0.1M HEPES, 0.01M
REMARK 280 CALCIUM DICHLORIDE, PH 7.3, MICROBACH, TEMPERATURE 301K
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 38.11700
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: 2100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 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 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 HIS A 76 66.53 34.03
REMARK 500 ALA A 114 -124.30 57.18
REMARK 500 ALA A 151 -152.83 -87.68
REMARK 500 GLU A 174 51.42 -66.74
REMARK 500 ASN A 248 -80.22 -130.49
REMARK 500 PHE A 319 4.33 -67.19
REMARK 500 ALA A 325 -159.31 -78.07
REMARK 500 HIS B 76 70.63 33.23
REMARK 500 ALA B 114 -121.01 59.53
REMARK 500 GLU B 174 48.67 -63.91
REMARK 500 ASN B 248 -77.51 -130.74
REMARK 500 ASP B 342 107.52 -54.77
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 CL B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TTK003000128.1 RELATED DB: TARGETDB
DBREF 2DSJ A 1 423 UNP Q5SHF9 Q5SHF9_THET8 1 423
DBREF 2DSJ B 1 423 UNP Q5SHF9 Q5SHF9_THET8 1 423
SEQRES 1 A 423 MET ASN PRO VAL ALA PHE ILE ARG GLU LYS ARG GLU GLY
SEQRES 2 A 423 LYS LYS HIS ARG ARG GLU ASP LEU GLU ALA PHE LEU LEU
SEQRES 3 A 423 GLY TYR LEU ARG ASP GLU VAL PRO ASP TYR GLN VAL SER
SEQRES 4 A 423 ALA TRP LEU MET ALA ALA PHE LEU ARG GLY LEU ASP PRO
SEQRES 5 A 423 GLU GLU THR LEU TRP LEU THR GLU THR MET ALA ARG SER
SEQRES 6 A 423 GLY LYS VAL LEU ASP LEU SER GLY LEU PRO HIS PRO VAL
SEQRES 7 A 423 ASP LYS HIS SER SER GLY GLY VAL GLY ASP LYS VAL SER
SEQRES 8 A 423 LEU VAL VAL GLY PRO ILE LEU ALA ALA SER GLY CYS THR
SEQRES 9 A 423 PHE ALA LYS MET SER GLY ARG GLY LEU ALA HIS THR GLY
SEQRES 10 A 423 GLY THR ILE ASP LYS LEU GLU SER VAL PRO GLY TRP ARG
SEQRES 11 A 423 GLY GLU MET THR GLU ALA GLU PHE LEU GLU ARG ALA ARG
SEQRES 12 A 423 ARG VAL GLY LEU VAL ILE ALA ALA GLN SER PRO ASP LEU
SEQRES 13 A 423 ALA PRO LEU ASP GLY LYS LEU TYR ALA LEU ARG ASP VAL
SEQRES 14 A 423 THR ALA THR VAL GLU SER VAL PRO LEU ILE ALA SER SER
SEQRES 15 A 423 ILE MET SER LYS LYS LEU ALA ALA GLY ALA ARG SER ILE
SEQRES 16 A 423 VAL LEU ASP VAL LYS VAL GLY ARG GLY ALA PHE MET LYS
SEQRES 17 A 423 THR LEU GLU GLU ALA ARG LEU LEU ALA LYS THR MET VAL
SEQRES 18 A 423 ALA ILE GLY GLN GLY ALA GLY ARG ARG VAL ARG ALA LEU
SEQRES 19 A 423 LEU THR SER MET GLU ALA PRO LEU GLY ARG ALA VAL GLY
SEQRES 20 A 423 ASN ALA ILE GLU VAL ARG GLU ALA ILE GLU ALA LEU LYS
SEQRES 21 A 423 GLY GLU GLY PRO GLY ASP LEU LEU GLU VAL ALA LEU ALA
SEQRES 22 A 423 LEU ALA GLU GLU ALA LEU ARG LEU GLU GLY LEU ASP PRO
SEQRES 23 A 423 ALA LEU ALA ARG LYS ALA LEU GLU GLY GLY ALA ALA LEU
SEQRES 24 A 423 GLU LYS PHE ARG ALA PHE LEU GLU ALA GLN GLY GLY ASP
SEQRES 25 A 423 PRO ARG ALA VAL GLU ASP PHE SER LEU LEU PRO LEU ALA
SEQRES 26 A 423 GLU GLU HIS PRO LEU ARG ALA GLU ARG GLU GLY VAL VAL
SEQRES 27 A 423 ARG GLU VAL ASP ALA TYR LYS VAL GLY LEU ALA VAL LEU
SEQRES 28 A 423 ALA LEU GLY GLY GLY ARG LYS ARG LYS GLY GLU PRO ILE
SEQRES 29 A 423 ASP HIS GLY VAL GLY VAL TYR LEU LEU LYS LYS PRO GLY
SEQRES 30 A 423 ASP ARG VAL GLU ARG GLY GLU ALA LEU ALA LEU VAL TYR
SEQRES 31 A 423 HIS ARG ARG ARG GLY LEU GLU GLU ALA LEU GLY HIS LEU
SEQRES 32 A 423 ARG GLU ALA TYR ALA LEU GLY GLU GLU ALA HIS PRO ALA
SEQRES 33 A 423 PRO LEU VAL LEU GLU ALA ILE
SEQRES 1 B 423 MET ASN PRO VAL ALA PHE ILE ARG GLU LYS ARG GLU GLY
SEQRES 2 B 423 LYS LYS HIS ARG ARG GLU ASP LEU GLU ALA PHE LEU LEU
SEQRES 3 B 423 GLY TYR LEU ARG ASP GLU VAL PRO ASP TYR GLN VAL SER
SEQRES 4 B 423 ALA TRP LEU MET ALA ALA PHE LEU ARG GLY LEU ASP PRO
SEQRES 5 B 423 GLU GLU THR LEU TRP LEU THR GLU THR MET ALA ARG SER
SEQRES 6 B 423 GLY LYS VAL LEU ASP LEU SER GLY LEU PRO HIS PRO VAL
SEQRES 7 B 423 ASP LYS HIS SER SER GLY GLY VAL GLY ASP LYS VAL SER
SEQRES 8 B 423 LEU VAL VAL GLY PRO ILE LEU ALA ALA SER GLY CYS THR
SEQRES 9 B 423 PHE ALA LYS MET SER GLY ARG GLY LEU ALA HIS THR GLY
SEQRES 10 B 423 GLY THR ILE ASP LYS LEU GLU SER VAL PRO GLY TRP ARG
SEQRES 11 B 423 GLY GLU MET THR GLU ALA GLU PHE LEU GLU ARG ALA ARG
SEQRES 12 B 423 ARG VAL GLY LEU VAL ILE ALA ALA GLN SER PRO ASP LEU
SEQRES 13 B 423 ALA PRO LEU ASP GLY LYS LEU TYR ALA LEU ARG ASP VAL
SEQRES 14 B 423 THR ALA THR VAL GLU SER VAL PRO LEU ILE ALA SER SER
SEQRES 15 B 423 ILE MET SER LYS LYS LEU ALA ALA GLY ALA ARG SER ILE
SEQRES 16 B 423 VAL LEU ASP VAL LYS VAL GLY ARG GLY ALA PHE MET LYS
SEQRES 17 B 423 THR LEU GLU GLU ALA ARG LEU LEU ALA LYS THR MET VAL
SEQRES 18 B 423 ALA ILE GLY GLN GLY ALA GLY ARG ARG VAL ARG ALA LEU
SEQRES 19 B 423 LEU THR SER MET GLU ALA PRO LEU GLY ARG ALA VAL GLY
SEQRES 20 B 423 ASN ALA ILE GLU VAL ARG GLU ALA ILE GLU ALA LEU LYS
SEQRES 21 B 423 GLY GLU GLY PRO GLY ASP LEU LEU GLU VAL ALA LEU ALA
SEQRES 22 B 423 LEU ALA GLU GLU ALA LEU ARG LEU GLU GLY LEU ASP PRO
SEQRES 23 B 423 ALA LEU ALA ARG LYS ALA LEU GLU GLY GLY ALA ALA LEU
SEQRES 24 B 423 GLU LYS PHE ARG ALA PHE LEU GLU ALA GLN GLY GLY ASP
SEQRES 25 B 423 PRO ARG ALA VAL GLU ASP PHE SER LEU LEU PRO LEU ALA
SEQRES 26 B 423 GLU GLU HIS PRO LEU ARG ALA GLU ARG GLU GLY VAL VAL
SEQRES 27 B 423 ARG GLU VAL ASP ALA TYR LYS VAL GLY LEU ALA VAL LEU
SEQRES 28 B 423 ALA LEU GLY GLY GLY ARG LYS ARG LYS GLY GLU PRO ILE
SEQRES 29 B 423 ASP HIS GLY VAL GLY VAL TYR LEU LEU LYS LYS PRO GLY
SEQRES 30 B 423 ASP ARG VAL GLU ARG GLY GLU ALA LEU ALA LEU VAL TYR
SEQRES 31 B 423 HIS ARG ARG ARG GLY LEU GLU GLU ALA LEU GLY HIS LEU
SEQRES 32 B 423 ARG GLU ALA TYR ALA LEU GLY GLU GLU ALA HIS PRO ALA
SEQRES 33 B 423 PRO LEU VAL LEU GLU ALA ILE
HET CL A1002 1
HET CL B1001 1
HETNAM CL CHLORIDE ION
FORMUL 3 CL 2(CL 1-)
FORMUL 5 HOH *830(H2 O)
HELIX 1 1 ASN A 2 GLU A 12 1 11
HELIX 2 2 ARG A 17 ARG A 30 1 14
HELIX 3 3 PRO A 34 GLY A 49 1 16
HELIX 4 4 ASP A 51 ARG A 64 1 14
HELIX 5 5 VAL A 90 ALA A 100 1 11
HELIX 6 6 GLY A 118 GLU A 124 1 7
HELIX 7 7 THR A 134 VAL A 145 1 12
HELIX 8 8 GLN A 152 LEU A 156 5 5
HELIX 9 9 ALA A 157 VAL A 169 1 13
HELIX 10 10 SER A 175 GLY A 191 1 17
HELIX 11 11 THR A 209 ALA A 227 1 19
HELIX 12 12 ASN A 248 LYS A 260 1 13
HELIX 13 13 PRO A 264 GLU A 282 1 19
HELIX 14 14 ALA A 287 GLY A 295 1 9
HELIX 15 15 GLY A 296 GLN A 309 1 14
HELIX 16 16 ASP A 312 GLU A 317 5 6
HELIX 17 17 ASP A 318 LEU A 322 5 5
HELIX 18 18 ASP A 342 GLY A 354 1 13
HELIX 19 19 GLY A 395 ALA A 406 1 12
HELIX 20 20 ASN B 2 GLU B 12 1 11
HELIX 21 21 ARG B 17 ARG B 30 1 14
HELIX 22 22 PRO B 34 GLY B 49 1 16
HELIX 23 23 ASP B 51 ARG B 64 1 14
HELIX 24 24 LYS B 89 ALA B 100 1 12
HELIX 25 25 GLY B 118 GLU B 124 1 7
HELIX 26 26 THR B 134 VAL B 145 1 12
HELIX 27 27 ALA B 157 ASP B 168 1 12
HELIX 28 28 SER B 175 GLY B 191 1 17
HELIX 29 29 ALA B 205 GLY B 228 1 24
HELIX 30 30 ASN B 248 LYS B 260 1 13
HELIX 31 31 PRO B 264 GLU B 282 1 19
HELIX 32 32 ALA B 287 GLY B 295 1 9
HELIX 33 33 GLY B 296 GLN B 309 1 14
HELIX 34 34 ASP B 312 GLU B 317 5 6
HELIX 35 35 ASP B 318 LEU B 322 5 5
HELIX 36 36 ASP B 342 GLY B 354 1 13
HELIX 37 37 GLY B 395 ALA B 406 1 12
SHEET 1 A 4 VAL A 78 SER A 83 0
SHEET 2 A 4 SER A 194 VAL A 201 1 O ASP A 198 N SER A 83
SHEET 3 A 4 ARG A 230 SER A 237 1 O LEU A 234 N LEU A 197
SHEET 4 A 4 VAL A 419 ILE A 423 -1 O ILE A 423 N ALA A 233
SHEET 1 B 2 PHE A 105 MET A 108 0
SHEET 2 B 2 LEU A 147 ALA A 150 1 O VAL A 148 N LYS A 107
SHEET 1 C 4 ALA A 245 GLY A 247 0
SHEET 2 C 4 GLY A 369 LEU A 372 -1 O VAL A 370 N VAL A 246
SHEET 3 C 4 ALA A 385 HIS A 391 -1 O TYR A 390 N GLY A 369
SHEET 4 C 4 GLU A 326 ARG A 331 -1 N LEU A 330 O LEU A 386
SHEET 1 D 3 ARG A 379 VAL A 380 0
SHEET 2 D 3 GLY A 336 VAL A 341 -1 N GLY A 336 O VAL A 380
SHEET 3 D 3 TYR A 407 GLY A 410 -1 O ALA A 408 N ARG A 339
SHEET 1 E 6 LEU B 147 ALA B 151 0
SHEET 2 E 6 THR B 104 SER B 109 1 N SER B 109 O ALA B 150
SHEET 3 E 6 PRO B 77 SER B 83 1 N VAL B 78 O THR B 104
SHEET 4 E 6 SER B 194 LYS B 200 1 O ASP B 198 N HIS B 81
SHEET 5 E 6 ARG B 230 THR B 236 1 O ARG B 230 N ILE B 195
SHEET 6 E 6 VAL B 419 ILE B 423 -1 O ILE B 423 N ALA B 233
SHEET 1 F 4 ALA B 245 GLY B 247 0
SHEET 2 F 4 GLY B 369 LEU B 372 -1 O VAL B 370 N VAL B 246
SHEET 3 F 4 ALA B 385 HIS B 391 -1 O TYR B 390 N GLY B 369
SHEET 4 F 4 GLU B 326 ARG B 331 -1 N LEU B 330 O ALA B 387
SHEET 1 G 3 ARG B 379 VAL B 380 0
SHEET 2 G 3 GLY B 336 VAL B 341 -1 N GLY B 336 O VAL B 380
SHEET 3 G 3 TYR B 407 GLY B 410 -1 O ALA B 408 N ARG B 339
SITE 1 AC1 5 ARG A 8 ARG A 11 ALA B 171 VAL B 173
SITE 2 AC1 5 GLU B 174
SITE 1 AC2 5 ALA A 171 VAL A 173 GLU A 174 ARG B 8
SITE 2 AC2 5 ARG B 11
CRYST1 58.828 76.234 103.862 90.00 91.26 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 0.016999 0.000000 0.000374 0.00000
SCALE2 0.000000 0.013118 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009630 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
