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HEADER HYDROLASE 12-FEB-10 3LS2
TITLE CRYSTAL STRUCTURE OF AN S-FORMYLGLUTATHIONE HYDROLASE FROM
TITLE 2 PSEUDOALTEROMONAS HALOPLANKTIS TAC125
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S-FORMYLGLUTATHIONE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOALTEROMONAS HALOPLANKTIS;
SOURCE 3 ORGANISM_TAXID: 326442;
SOURCE 4 STRAIN: TAC125;
SOURCE 5 GENE: PSHAA1385;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS S-FORMYLGLUTATHIONE HYDROLASE, PSYCHROPHILIC ORGANISM,
KEYWDS 2 PSEUDOALTEROMONAS HALOPLANKTIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.ALTERIO,G.DE SIMONE
REVDAT 1 23-MAR-10 3LS2 0
JRNL AUTH V.ALTERIO,V.AURILIA,A.ROMANELLI,A.PARRACINO,
JRNL AUTH 2 M.SAVIANO,S.D'AURIA,G.DE SIMONE
JRNL TITL CRYSTAL STRUCTURE OF AN S-FORMYLGLUTATHIONE
JRNL TITL 2 HYDROLASE FROM PSEUDOALTEROMONAS HALOPLANKTIS
JRNL TITL 3 TAC125.
JRNL REF BIOPOLYMERS 2010
JRNL REFN ESSN 1079-0282
JRNL PMID 20209484
JRNL DOI 10.1002/BIP.21420
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
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) (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 48748
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2434
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 : 8656
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 1054
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 : 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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3LS2 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-FEB-10.
REMARK 100 THE RCSB ID CODE IS RCSB057658.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49990
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.5000
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 (%) : 93.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.16600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1PV1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG MME 5000, 0.2 M
REMARK 280 SODIUM ACETATE, 0.1 M TRIS-HCL, PH 7.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293 K
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 24.74500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.33500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 64.87500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 76.33500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.74500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 64.87500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 1
REMARK 465 ALA A 280
REMARK 465 MET B 1
REMARK 465 ALA B 280
REMARK 465 MET C 1
REMARK 465 ALA C 280
REMARK 465 MET D 1
REMARK 465 ALA D 280
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 41 CG CD OE1 OE2
REMARK 480 ASP A 88 CG OD1 OD2
REMARK 480 GLU A 210 CD OE1 OE2
REMARK 480 ASP A 229 CG OD1 OD2
REMARK 480 GLU B 41 CG CD OE1 OE2
REMARK 480 LYS B 69 CD CE NZ
REMARK 480 GLN B 133 CD OE1 NE2
REMARK 480 LYS C 69 CD CE NZ
REMARK 480 LYS C 208 CD CE NZ
REMARK 480 ASN C 226 CG OD1 ND2
REMARK 480 LYS C 242 CD CE NZ
REMARK 480 ASN D 226 CG OD1 ND2
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 THR A 55 -9.91 71.28
REMARK 500 THR A 57 -151.98 -129.47
REMARK 500 SER A 84 174.62 177.59
REMARK 500 ALA A 99 -141.06 66.62
REMARK 500 ALA A 102 55.20 -152.16
REMARK 500 SER A 147 -110.05 55.87
REMARK 500 ASP A 257 -158.96 -107.50
REMARK 500 THR B 55 -5.16 70.38
REMARK 500 SER B 84 171.06 179.70
REMARK 500 ALA B 99 -141.27 66.67
REMARK 500 SER B 147 -108.41 52.66
REMARK 500 ASP B 257 -157.47 -111.92
REMARK 500 THR C 55 -8.17 72.47
REMARK 500 THR C 57 -156.90 -123.19
REMARK 500 SER C 84 176.19 174.71
REMARK 500 ASP C 94 46.76 -72.15
REMARK 500 ALA C 99 -135.62 69.21
REMARK 500 ALA C 102 57.81 -153.38
REMARK 500 PHE C 104 18.30 53.68
REMARK 500 SER C 147 -106.57 51.96
REMARK 500 PRO C 247 62.16 -69.73
REMARK 500 ASP C 257 -156.79 -106.34
REMARK 500 THR D 55 -4.21 74.42
REMARK 500 SER D 84 174.38 178.82
REMARK 500 ALA D 99 -138.70 68.52
REMARK 500 ALA D 102 56.61 -145.37
REMARK 500 PHE D 104 19.86 54.06
REMARK 500 SER D 147 -108.75 54.11
REMARK 500 LYS D 194 -6.65 -59.95
REMARK 500 PRO D 247 62.58 -69.66
REMARK 500 ASP D 257 -152.19 -107.11
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 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 281
DBREF 3LS2 A 1 280 UNP Q3IL66 Q3IL66_PSEHT 1 280
DBREF 3LS2 B 1 280 UNP Q3IL66 Q3IL66_PSEHT 1 280
DBREF 3LS2 C 1 280 UNP Q3IL66 Q3IL66_PSEHT 1 280
DBREF 3LS2 D 1 280 UNP Q3IL66 Q3IL66_PSEHT 1 280
SEQRES 1 A 280 MET LEU GLU ASN ILE SER SER VAL LYS VAL SER GLY GLY
SEQRES 2 A 280 TRP HIS LYS GLN TYR THR HIS SER ALA VAL SER THR HIS
SEQRES 3 A 280 CYS THR MET ARG PHE ALA VAL PHE LEU PRO PRO GLY ALA
SEQRES 4 A 280 SER GLU SER ASN LYS VAL PRO VAL LEU TYR TRP LEU SER
SEQRES 5 A 280 GLY LEU THR CYS THR ASP GLU ASN PHE MET GLN LYS ALA
SEQRES 6 A 280 GLY ALA PHE LYS LYS ALA ALA GLU LEU GLY ILE ALA ILE
SEQRES 7 A 280 VAL ALA PRO ASP THR SER PRO ARG GLY ASP ASN VAL PRO
SEQRES 8 A 280 ASN GLU ASP SER TYR ASP PHE ALA GLN GLY ALA GLY PHE
SEQRES 9 A 280 TYR VAL ASN ALA THR GLN ALA PRO TYR ASN THR HIS PHE
SEQRES 10 A 280 ASN MET TYR ASP TYR VAL VAL ASN GLU LEU PRO ALA LEU
SEQRES 11 A 280 ILE GLU GLN HIS PHE PRO VAL THR SER THR LYS ALA ILE
SEQRES 12 A 280 SER GLY HIS SER MET GLY GLY HIS GLY ALA LEU MET ILE
SEQRES 13 A 280 ALA LEU LYS ASN PRO GLN ASP TYR VAL SER ALA SER ALA
SEQRES 14 A 280 PHE SER PRO ILE VAL ASN PRO ILE ASN CYS PRO TRP GLY
SEQRES 15 A 280 VAL LYS ALA PHE THR GLY TYR LEU GLY ALA ASP LYS THR
SEQRES 16 A 280 THR TRP ALA GLN TYR ASP SER CYS LYS LEU MET ALA LYS
SEQRES 17 A 280 ALA GLU GLN SER ASN TYR LEU PRO MET LEU VAL SER GLN
SEQRES 18 A 280 GLY ASP ALA ASP ASN PHE LEU ASP GLU GLN LEU LYS PRO
SEQRES 19 A 280 GLN ASN LEU VAL ALA VAL ALA LYS GLN LYS ASP TYR PRO
SEQRES 20 A 280 LEU THR LEU GLU MET GLN THR GLY TYR ASP HIS SER TYR
SEQRES 21 A 280 PHE PHE ILE SER SER PHE ILE ASP GLN HIS LEU VAL PHE
SEQRES 22 A 280 HIS HIS GLN TYR LEU SER ALA
SEQRES 1 B 280 MET LEU GLU ASN ILE SER SER VAL LYS VAL SER GLY GLY
SEQRES 2 B 280 TRP HIS LYS GLN TYR THR HIS SER ALA VAL SER THR HIS
SEQRES 3 B 280 CYS THR MET ARG PHE ALA VAL PHE LEU PRO PRO GLY ALA
SEQRES 4 B 280 SER GLU SER ASN LYS VAL PRO VAL LEU TYR TRP LEU SER
SEQRES 5 B 280 GLY LEU THR CYS THR ASP GLU ASN PHE MET GLN LYS ALA
SEQRES 6 B 280 GLY ALA PHE LYS LYS ALA ALA GLU LEU GLY ILE ALA ILE
SEQRES 7 B 280 VAL ALA PRO ASP THR SER PRO ARG GLY ASP ASN VAL PRO
SEQRES 8 B 280 ASN GLU ASP SER TYR ASP PHE ALA GLN GLY ALA GLY PHE
SEQRES 9 B 280 TYR VAL ASN ALA THR GLN ALA PRO TYR ASN THR HIS PHE
SEQRES 10 B 280 ASN MET TYR ASP TYR VAL VAL ASN GLU LEU PRO ALA LEU
SEQRES 11 B 280 ILE GLU GLN HIS PHE PRO VAL THR SER THR LYS ALA ILE
SEQRES 12 B 280 SER GLY HIS SER MET GLY GLY HIS GLY ALA LEU MET ILE
SEQRES 13 B 280 ALA LEU LYS ASN PRO GLN ASP TYR VAL SER ALA SER ALA
SEQRES 14 B 280 PHE SER PRO ILE VAL ASN PRO ILE ASN CYS PRO TRP GLY
SEQRES 15 B 280 VAL LYS ALA PHE THR GLY TYR LEU GLY ALA ASP LYS THR
SEQRES 16 B 280 THR TRP ALA GLN TYR ASP SER CYS LYS LEU MET ALA LYS
SEQRES 17 B 280 ALA GLU GLN SER ASN TYR LEU PRO MET LEU VAL SER GLN
SEQRES 18 B 280 GLY ASP ALA ASP ASN PHE LEU ASP GLU GLN LEU LYS PRO
SEQRES 19 B 280 GLN ASN LEU VAL ALA VAL ALA LYS GLN LYS ASP TYR PRO
SEQRES 20 B 280 LEU THR LEU GLU MET GLN THR GLY TYR ASP HIS SER TYR
SEQRES 21 B 280 PHE PHE ILE SER SER PHE ILE ASP GLN HIS LEU VAL PHE
SEQRES 22 B 280 HIS HIS GLN TYR LEU SER ALA
SEQRES 1 C 280 MET LEU GLU ASN ILE SER SER VAL LYS VAL SER GLY GLY
SEQRES 2 C 280 TRP HIS LYS GLN TYR THR HIS SER ALA VAL SER THR HIS
SEQRES 3 C 280 CYS THR MET ARG PHE ALA VAL PHE LEU PRO PRO GLY ALA
SEQRES 4 C 280 SER GLU SER ASN LYS VAL PRO VAL LEU TYR TRP LEU SER
SEQRES 5 C 280 GLY LEU THR CYS THR ASP GLU ASN PHE MET GLN LYS ALA
SEQRES 6 C 280 GLY ALA PHE LYS LYS ALA ALA GLU LEU GLY ILE ALA ILE
SEQRES 7 C 280 VAL ALA PRO ASP THR SER PRO ARG GLY ASP ASN VAL PRO
SEQRES 8 C 280 ASN GLU ASP SER TYR ASP PHE ALA GLN GLY ALA GLY PHE
SEQRES 9 C 280 TYR VAL ASN ALA THR GLN ALA PRO TYR ASN THR HIS PHE
SEQRES 10 C 280 ASN MET TYR ASP TYR VAL VAL ASN GLU LEU PRO ALA LEU
SEQRES 11 C 280 ILE GLU GLN HIS PHE PRO VAL THR SER THR LYS ALA ILE
SEQRES 12 C 280 SER GLY HIS SER MET GLY GLY HIS GLY ALA LEU MET ILE
SEQRES 13 C 280 ALA LEU LYS ASN PRO GLN ASP TYR VAL SER ALA SER ALA
SEQRES 14 C 280 PHE SER PRO ILE VAL ASN PRO ILE ASN CYS PRO TRP GLY
SEQRES 15 C 280 VAL LYS ALA PHE THR GLY TYR LEU GLY ALA ASP LYS THR
SEQRES 16 C 280 THR TRP ALA GLN TYR ASP SER CYS LYS LEU MET ALA LYS
SEQRES 17 C 280 ALA GLU GLN SER ASN TYR LEU PRO MET LEU VAL SER GLN
SEQRES 18 C 280 GLY ASP ALA ASP ASN PHE LEU ASP GLU GLN LEU LYS PRO
SEQRES 19 C 280 GLN ASN LEU VAL ALA VAL ALA LYS GLN LYS ASP TYR PRO
SEQRES 20 C 280 LEU THR LEU GLU MET GLN THR GLY TYR ASP HIS SER TYR
SEQRES 21 C 280 PHE PHE ILE SER SER PHE ILE ASP GLN HIS LEU VAL PHE
SEQRES 22 C 280 HIS HIS GLN TYR LEU SER ALA
SEQRES 1 D 280 MET LEU GLU ASN ILE SER SER VAL LYS VAL SER GLY GLY
SEQRES 2 D 280 TRP HIS LYS GLN TYR THR HIS SER ALA VAL SER THR HIS
SEQRES 3 D 280 CYS THR MET ARG PHE ALA VAL PHE LEU PRO PRO GLY ALA
SEQRES 4 D 280 SER GLU SER ASN LYS VAL PRO VAL LEU TYR TRP LEU SER
SEQRES 5 D 280 GLY LEU THR CYS THR ASP GLU ASN PHE MET GLN LYS ALA
SEQRES 6 D 280 GLY ALA PHE LYS LYS ALA ALA GLU LEU GLY ILE ALA ILE
SEQRES 7 D 280 VAL ALA PRO ASP THR SER PRO ARG GLY ASP ASN VAL PRO
SEQRES 8 D 280 ASN GLU ASP SER TYR ASP PHE ALA GLN GLY ALA GLY PHE
SEQRES 9 D 280 TYR VAL ASN ALA THR GLN ALA PRO TYR ASN THR HIS PHE
SEQRES 10 D 280 ASN MET TYR ASP TYR VAL VAL ASN GLU LEU PRO ALA LEU
SEQRES 11 D 280 ILE GLU GLN HIS PHE PRO VAL THR SER THR LYS ALA ILE
SEQRES 12 D 280 SER GLY HIS SER MET GLY GLY HIS GLY ALA LEU MET ILE
SEQRES 13 D 280 ALA LEU LYS ASN PRO GLN ASP TYR VAL SER ALA SER ALA
SEQRES 14 D 280 PHE SER PRO ILE VAL ASN PRO ILE ASN CYS PRO TRP GLY
SEQRES 15 D 280 VAL LYS ALA PHE THR GLY TYR LEU GLY ALA ASP LYS THR
SEQRES 16 D 280 THR TRP ALA GLN TYR ASP SER CYS LYS LEU MET ALA LYS
SEQRES 17 D 280 ALA GLU GLN SER ASN TYR LEU PRO MET LEU VAL SER GLN
SEQRES 18 D 280 GLY ASP ALA ASP ASN PHE LEU ASP GLU GLN LEU LYS PRO
SEQRES 19 D 280 GLN ASN LEU VAL ALA VAL ALA LYS GLN LYS ASP TYR PRO
SEQRES 20 D 280 LEU THR LEU GLU MET GLN THR GLY TYR ASP HIS SER TYR
SEQRES 21 D 280 PHE PHE ILE SER SER PHE ILE ASP GLN HIS LEU VAL PHE
SEQRES 22 D 280 HIS HIS GLN TYR LEU SER ALA
HET CL A 281 1
HET CL B 281 1
HET CL C 281 1
HET CL D 281 1
HETNAM CL CHLORIDE ION
FORMUL 5 CL 4(CL 1-)
FORMUL 9 HOH *1054(H2 O)
HELIX 1 1 ASP A 58 ALA A 65 1 8
HELIX 2 2 ALA A 67 GLY A 75 1 9
HELIX 3 3 ASN A 118 ASN A 125 1 8
HELIX 4 4 ASN A 125 PHE A 135 1 11
HELIX 5 5 SER A 147 ASN A 160 1 14
HELIX 6 6 ASN A 175 ASN A 178 5 4
HELIX 7 7 CYS A 179 GLY A 191 1 13
HELIX 8 8 ASP A 193 TYR A 200 5 8
HELIX 9 9 ASP A 201 LYS A 208 1 8
HELIX 10 10 ALA A 209 TYR A 214 5 6
HELIX 11 11 LYS A 233 ASP A 245 1 13
HELIX 12 12 SER A 259 SER A 279 1 21
HELIX 13 13 ASP B 58 ALA B 65 1 8
HELIX 14 14 ALA B 67 GLY B 75 1 9
HELIX 15 15 ASN B 118 ASN B 125 1 8
HELIX 16 16 ASN B 125 PHE B 135 1 11
HELIX 17 17 SER B 147 ASN B 160 1 14
HELIX 18 18 ASN B 175 ASN B 178 5 4
HELIX 19 19 CYS B 179 GLY B 191 1 13
HELIX 20 20 ASP B 193 TYR B 200 5 8
HELIX 21 21 ASP B 201 LYS B 208 1 8
HELIX 22 22 GLU B 210 TYR B 214 5 5
HELIX 23 23 LYS B 233 ASP B 245 1 13
HELIX 24 24 SER B 259 SER B 279 1 21
HELIX 25 25 ASP C 58 ALA C 65 1 8
HELIX 26 26 ALA C 67 GLY C 75 1 9
HELIX 27 27 ASN C 118 ASN C 125 1 8
HELIX 28 28 ASN C 125 PHE C 135 1 11
HELIX 29 29 SER C 147 ASN C 160 1 14
HELIX 30 30 ASN C 175 ASN C 178 5 4
HELIX 31 31 CYS C 179 GLY C 191 1 13
HELIX 32 32 ASP C 193 TYR C 200 5 8
HELIX 33 33 ASP C 201 LYS C 208 1 8
HELIX 34 34 ALA C 209 TYR C 214 5 6
HELIX 35 35 LYS C 233 ASP C 245 1 13
HELIX 36 36 SER C 259 SER C 279 1 21
HELIX 37 37 ASP D 58 ALA D 65 1 8
HELIX 38 38 ALA D 67 GLY D 75 1 9
HELIX 39 39 ASN D 118 ASN D 125 1 8
HELIX 40 40 ASN D 125 PHE D 135 1 11
HELIX 41 41 SER D 147 ASN D 160 1 14
HELIX 42 42 ASN D 175 ASN D 178 5 4
HELIX 43 43 CYS D 179 GLY D 191 1 13
HELIX 44 44 ASP D 193 GLN D 199 1 7
HELIX 45 45 ASP D 201 LYS D 208 1 8
HELIX 46 46 ALA D 209 TYR D 214 5 6
HELIX 47 47 LYS D 233 ASP D 245 1 13
HELIX 48 48 SER D 259 SER D 279 1 21
SHEET 1 A 6 GLU A 3 VAL A 10 0
SHEET 2 A 6 GLY A 13 ALA A 22 -1 O HIS A 15 N VAL A 8
SHEET 3 A 6 CYS A 27 LEU A 35 -1 O PHE A 31 N TYR A 18
SHEET 4 A 6 ALA A 77 ALA A 80 -1 O ILE A 78 N PHE A 34
SHEET 5 A 6 VAL A 45 LEU A 51 1 N TRP A 50 O VAL A 79
SHEET 6 A 6 VAL A 137 GLY A 145 1 O SER A 144 N TYR A 49
SHEET 1 B 3 ALA A 167 PHE A 170 0
SHEET 2 B 3 MET A 217 GLY A 222 1 O SER A 220 N ALA A 169
SHEET 3 B 3 LEU A 248 GLN A 253 1 O GLU A 251 N VAL A 219
SHEET 1 C 6 GLU B 3 VAL B 10 0
SHEET 2 C 6 GLY B 13 ALA B 22 -1 O HIS B 15 N VAL B 8
SHEET 3 C 6 CYS B 27 LEU B 35 -1 O MET B 29 N HIS B 20
SHEET 4 C 6 ALA B 77 ALA B 80 -1 O ALA B 80 N ALA B 32
SHEET 5 C 6 VAL B 45 LEU B 51 1 N TRP B 50 O VAL B 79
SHEET 6 C 6 VAL B 137 GLY B 145 1 O ALA B 142 N TYR B 49
SHEET 1 D 3 ALA B 167 PHE B 170 0
SHEET 2 D 3 MET B 217 GLY B 222 1 O SER B 220 N ALA B 169
SHEET 3 D 3 LEU B 248 GLN B 253 1 O GLN B 253 N GLN B 221
SHEET 1 E 6 GLU C 3 VAL C 10 0
SHEET 2 E 6 GLY C 13 ALA C 22 -1 O THR C 19 N GLU C 3
SHEET 3 E 6 CYS C 27 LEU C 35 -1 O VAL C 33 N LYS C 16
SHEET 4 E 6 ALA C 77 ALA C 80 -1 O ALA C 80 N ALA C 32
SHEET 5 E 6 VAL C 45 LEU C 51 1 N LEU C 48 O ALA C 77
SHEET 6 E 6 VAL C 137 GLY C 145 1 O ALA C 142 N TYR C 49
SHEET 1 F 3 ALA C 167 PHE C 170 0
SHEET 2 F 3 MET C 217 GLY C 222 1 O SER C 220 N ALA C 169
SHEET 3 F 3 LEU C 248 GLN C 253 1 O GLN C 253 N GLN C 221
SHEET 1 G 6 GLU D 3 VAL D 10 0
SHEET 2 G 6 GLY D 13 ALA D 22 -1 O THR D 19 N GLU D 3
SHEET 3 G 6 CYS D 27 LEU D 35 -1 O PHE D 31 N TYR D 18
SHEET 4 G 6 ALA D 77 ALA D 80 -1 O ALA D 80 N ALA D 32
SHEET 5 G 6 VAL D 45 LEU D 51 1 N TRP D 50 O VAL D 79
SHEET 6 G 6 VAL D 137 GLY D 145 1 O SER D 144 N TYR D 49
SHEET 1 H 3 ALA D 167 PHE D 170 0
SHEET 2 H 3 MET D 217 GLY D 222 1 O SER D 220 N ALA D 169
SHEET 3 H 3 LEU D 248 GLN D 253 1 O GLU D 251 N VAL D 219
CISPEP 1 ALA A 111 PRO A 112 0 0.09
CISPEP 2 ALA B 111 PRO B 112 0 1.09
CISPEP 3 ALA C 111 PRO C 112 0 -0.06
CISPEP 4 ALA D 111 PRO D 112 0 -1.30
SITE 1 AC1 6 PRO B 91 PRO B 112 TYR B 113 THR B 115
SITE 2 AC1 6 HIS B 116 PHE B 117
SITE 1 AC2 6 PRO C 91 PRO C 112 TYR C 113 THR C 115
SITE 2 AC2 6 HIS C 116 PHE C 117
SITE 1 AC3 6 PRO A 91 PRO A 112 TYR A 113 THR A 115
SITE 2 AC3 6 HIS A 116 PHE A 117
SITE 1 AC4 6 PRO D 91 PRO D 112 TYR D 113 THR D 115
SITE 2 AC4 6 HIS D 116 PHE D 117
CRYST1 49.490 129.750 152.670 90.00 90.00 90.00 P 21 21 21 16
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 0.020206 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007707 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006550 0.00000
TER 2165 SER A 279
TER 4330 SER B 279
TER 6495 SER C 279
TER 8660 SER D 279
MASTER 315 0 4 48 36 0 8 6 9714 4 0 88
END |