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HEADER HYDROLASE 03-JUL-06 2DSN
TITLE CRYSTAL STRUCTURE OF T1 LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOSTABLE LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 30-416;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS SP. T1;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: ORIGAMI B;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX/T1S
KEYWDS T1 LIPASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.MATSUMURA,Y.KAI
REVDAT 1 17-JUL-07 2DSN 0
JRNL AUTH H.MATSUMURA,Y.KAI
JRNL TITL CRYSTAL STRUCTURE OF T1 LIPASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.50 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.33
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 753441.060
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.5
REMARK 3 NUMBER OF REFLECTIONS : 136451
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) : 0.174
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 6903
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 18434
REMARK 3 BIN R VALUE (WORKING SET) : 0.2350
REMARK 3 BIN FREE R VALUE : 0.2630
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 959
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.008
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6106
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 1148
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.15000
REMARK 3 B22 (A**2) : -1.38000
REMARK 3 B33 (A**2) : -1.77000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.30000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.15
REMARK 3 ESD FROM SIGMAA (A) : 0.13
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) : 0.17
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.15
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.75
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) : 0.980 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.470 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.860 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.800 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 57.29
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 2DSN COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006
REMARK 4
REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY.
REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-07-10)
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE RCSB ID CODE IS RCSB025796.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 140733
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 40.330
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 12.400
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.32100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.300
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 1JI3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5M NACL, 0.1M KH2PO4, 0.1M
REMARK 280 NAH2PO4, 0.1M MES BUFFER, PH 6.6, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 1/2+X,1/2+Y,Z
REMARK 290 4555 1/2-X,1/2+Y,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 58.86550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.63500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 58.86550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.63500
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH 4 LIES ON A SPECIAL POSITION.
REMARK 375 HOH 415 LIES ON A SPECIAL POSITION.
REMARK 375 HOH 506 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 THR A 17 C THR A 17 O -0.090
REMARK 500 ARG A 92 CB ARG A 92 CG -0.129
REMARK 500 ARG A 92 CG ARG A 92 CD 0.103
REMARK 500 ARG A 92 CZ ARG A 92 NH2 -0.051
REMARK 500 LEU A 170 CG LEU A 170 CD1 -0.056
REMARK 500 VAL A 174 N VAL A 174 CA -0.061
REMARK 500 VAL A 174 CB VAL A 174 CG1 -0.054
REMARK 500 VAL A 174 CB VAL A 174 CG2 -0.112
REMARK 500 ASP A 175 N ASP A 175 CA -0.053
REMARK 500 ASP A 175 CB ASP A 175 CG 0.078
REMARK 500 ASP A 175 C ASP A 175 O -0.058
REMARK 500 ASP A 175 C PHE A 176 N 0.058
REMARK 500 THR A 200 CB THR A 200 CG2 -0.117
REMARK 500 LYS A 229 CB LYS A 229 CG -0.057
REMARK 500 LYS A 251 CG LYS A 251 CD -0.056
REMARK 500 LYS A 251 CE LYS A 251 NZ 0.062
REMARK 500 LEU A 277 CG LEU A 277 CD1 -0.197
REMARK 500 LEU A 277 CG LEU A 277 CD2 -0.079
REMARK 500 LYS A 345 CB LYS A 345 CG -0.072
REMARK 500 LYS A 345 CD LYS A 345 CE -0.055
REMARK 500 LYS A 345 CE LYS A 345 NZ -0.057
REMARK 500 ILE A 361 CG1 ILE A 361 CD1 -0.245
REMARK 500 ILE A 361 C ILE A 361 O -0.064
REMARK 500 LEU B 170 C LEU B 170 O -0.064
REMARK 500 SER B 236 CB SER B 236 OG -0.069
REMARK 500 GLN B 387 CG GLN B 387 CD 0.090
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 HIS A 108 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 ILE A 110 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 MET A 173 CB - CA - C ANGL. DEV. = 7.6 DEGREES
REMARK 500 VAL A 174 CB - CA - C ANGL. DEV. = 8.9 DEGREES
REMARK 500 ASP A 175 OD1 - CG - OD2 ANGL. DEV. = -8.3 DEGREES
REMARK 500 ASP A 175 CB - CG - OD2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 ASP A 175 CA - C - O ANGL. DEV. = -8.5 DEGREES
REMARK 500 PHE A 176 N - CA - C ANGL. DEV. = 14.1 DEGREES
REMARK 500 ASP A 175 CA - C - N ANGL. DEV. = 11.1 DEGREES
REMARK 500 THR A 200 OG1 - CB - CG2 ANGL. DEV. = -9.1 DEGREES
REMARK 500 SER A 201 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 VAL A 294 N - CA - C ANGL. DEV. = 8.7 DEGREES
REMARK 500 CYS A 295 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 ARG A 303 CG - CD - NE ANGL. DEV. = 7.9 DEGREES
REMARK 500 MET A 325 N - CA - C ANGL. DEV. = 12.8 DEGREES
REMARK 500 THR B 17 N - CA - C ANGL. DEV. =-11.2 DEGREES
REMARK 500 HIS B 108 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 ILE B 110 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 VAL B 294 N - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 CYS B 295 N - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 500 ASN B 304 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 ILE B 309 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 MET B 325 N - CA - C ANGL. DEV. = 12.6 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 VAL A 203 -54.88 67.86
REMARK 500 VAL B 203 -58.33 67.42
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 175 PHE A 176 132.19
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 1080 DISTANCE = 6.87 ANGSTROMS
REMARK 525 HOH 1098 DISTANCE = 7.26 ANGSTROMS
REMARK 525 HOH 1125 DISTANCE = 6.89 ANGSTROMS
REMARK 525 HOH 1132 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH 1133 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH 1136 DISTANCE = 7.15 ANGSTROMS
DBREF 2DSN A 2 388 UNP Q842J9 Q842J9_9BACI 30 416
DBREF 2DSN B 2 388 UNP Q842J9 Q842J9_9BACI 30 416
SEQRES 1 A 387 SER LEU ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU HIS
SEQRES 2 A 387 GLY PHE THR GLY TRP GLY ARG GLU GLU MET PHE GLY PHE
SEQRES 3 A 387 LYS TYR TRP GLY GLY VAL ARG GLY ASP ILE GLU GLN TRP
SEQRES 4 A 387 LEU ASN ASP ASN GLY TYR ARG THR TYR THR LEU ALA VAL
SEQRES 5 A 387 GLY PRO LEU SER SER ASN TRP ASP ARG ALA CYS GLU ALA
SEQRES 6 A 387 TYR ALA GLN LEU VAL GLY GLY THR VAL ASP TYR GLY ALA
SEQRES 7 A 387 ALA HIS ALA ALA LYS HIS GLY HIS ALA ARG PHE GLY ARG
SEQRES 8 A 387 THR TYR PRO GLY LEU LEU PRO GLU LEU LYS ARG GLY GLY
SEQRES 9 A 387 ARG ILE HIS ILE ILE ALA HIS SER GLN GLY GLY GLN THR
SEQRES 10 A 387 ALA ARG MET LEU VAL SER LEU LEU GLU ASN GLY SER GLN
SEQRES 11 A 387 GLU GLU ARG GLU TYR ALA LYS ALA HIS ASN VAL SER LEU
SEQRES 12 A 387 SER PRO LEU PHE GLU GLY GLY HIS HIS PHE VAL LEU SER
SEQRES 13 A 387 VAL THR THR ILE ALA THR PRO HIS ASP GLY THR THR LEU
SEQRES 14 A 387 VAL ASN MET VAL ASP PHE THR ASP ARG PHE PHE ASP LEU
SEQRES 15 A 387 GLN LYS ALA VAL LEU GLU ALA ALA ALA VAL ALA SER ASN
SEQRES 16 A 387 VAL PRO TYR THR SER GLN VAL TYR ASP PHE LYS LEU ASP
SEQRES 17 A 387 GLN TRP GLY LEU ARG ARG GLN PRO GLY GLU SER PHE ASP
SEQRES 18 A 387 HIS TYR PHE GLU ARG LEU LYS ARG SER PRO VAL TRP THR
SEQRES 19 A 387 SER THR ASP THR ALA ARG TYR ASP LEU SER VAL SER GLY
SEQRES 20 A 387 ALA GLU LYS LEU ASN GLN TRP VAL GLN ALA SER PRO ASN
SEQRES 21 A 387 THR TYR TYR LEU SER PHE SER THR GLU ARG THR TYR ARG
SEQRES 22 A 387 GLY ALA LEU THR GLY ASN HIS TYR PRO GLU LEU GLY MET
SEQRES 23 A 387 ASN ALA PHE SER ALA VAL VAL CYS ALA PRO PHE LEU GLY
SEQRES 24 A 387 SER TYR ARG ASN PRO THR LEU GLY ILE ASP ASP ARG TRP
SEQRES 25 A 387 LEU GLU ASN ASP GLY ILE VAL ASN THR VAL SER MET ASN
SEQRES 26 A 387 GLY PRO LYS ARG GLY SER SER ASP ARG ILE VAL PRO TYR
SEQRES 27 A 387 ASP GLY THR LEU LYS LYS GLY VAL TRP ASN ASP MET GLY
SEQRES 28 A 387 THR TYR ASN VAL ASP HIS LEU GLU ILE ILE GLY VAL ASP
SEQRES 29 A 387 PRO ASN PRO SER PHE ASP ILE ARG ALA PHE TYR LEU ARG
SEQRES 30 A 387 LEU ALA GLU GLN LEU ALA SER LEU GLN PRO
SEQRES 1 B 387 SER LEU ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU HIS
SEQRES 2 B 387 GLY PHE THR GLY TRP GLY ARG GLU GLU MET PHE GLY PHE
SEQRES 3 B 387 LYS TYR TRP GLY GLY VAL ARG GLY ASP ILE GLU GLN TRP
SEQRES 4 B 387 LEU ASN ASP ASN GLY TYR ARG THR TYR THR LEU ALA VAL
SEQRES 5 B 387 GLY PRO LEU SER SER ASN TRP ASP ARG ALA CYS GLU ALA
SEQRES 6 B 387 TYR ALA GLN LEU VAL GLY GLY THR VAL ASP TYR GLY ALA
SEQRES 7 B 387 ALA HIS ALA ALA LYS HIS GLY HIS ALA ARG PHE GLY ARG
SEQRES 8 B 387 THR TYR PRO GLY LEU LEU PRO GLU LEU LYS ARG GLY GLY
SEQRES 9 B 387 ARG ILE HIS ILE ILE ALA HIS SER GLN GLY GLY GLN THR
SEQRES 10 B 387 ALA ARG MET LEU VAL SER LEU LEU GLU ASN GLY SER GLN
SEQRES 11 B 387 GLU GLU ARG GLU TYR ALA LYS ALA HIS ASN VAL SER LEU
SEQRES 12 B 387 SER PRO LEU PHE GLU GLY GLY HIS HIS PHE VAL LEU SER
SEQRES 13 B 387 VAL THR THR ILE ALA THR PRO HIS ASP GLY THR THR LEU
SEQRES 14 B 387 VAL ASN MET VAL ASP PHE THR ASP ARG PHE PHE ASP LEU
SEQRES 15 B 387 GLN LYS ALA VAL LEU GLU ALA ALA ALA VAL ALA SER ASN
SEQRES 16 B 387 VAL PRO TYR THR SER GLN VAL TYR ASP PHE LYS LEU ASP
SEQRES 17 B 387 GLN TRP GLY LEU ARG ARG GLN PRO GLY GLU SER PHE ASP
SEQRES 18 B 387 HIS TYR PHE GLU ARG LEU LYS ARG SER PRO VAL TRP THR
SEQRES 19 B 387 SER THR ASP THR ALA ARG TYR ASP LEU SER VAL SER GLY
SEQRES 20 B 387 ALA GLU LYS LEU ASN GLN TRP VAL GLN ALA SER PRO ASN
SEQRES 21 B 387 THR TYR TYR LEU SER PHE SER THR GLU ARG THR TYR ARG
SEQRES 22 B 387 GLY ALA LEU THR GLY ASN HIS TYR PRO GLU LEU GLY MET
SEQRES 23 B 387 ASN ALA PHE SER ALA VAL VAL CYS ALA PRO PHE LEU GLY
SEQRES 24 B 387 SER TYR ARG ASN PRO THR LEU GLY ILE ASP ASP ARG TRP
SEQRES 25 B 387 LEU GLU ASN ASP GLY ILE VAL ASN THR VAL SER MET ASN
SEQRES 26 B 387 GLY PRO LYS ARG GLY SER SER ASP ARG ILE VAL PRO TYR
SEQRES 27 B 387 ASP GLY THR LEU LYS LYS GLY VAL TRP ASN ASP MET GLY
SEQRES 28 B 387 THR TYR ASN VAL ASP HIS LEU GLU ILE ILE GLY VAL ASP
SEQRES 29 B 387 PRO ASN PRO SER PHE ASP ILE ARG ALA PHE TYR LEU ARG
SEQRES 30 B 387 LEU ALA GLU GLN LEU ALA SER LEU GLN PRO
HET ZN 2001 1
HET ZN 2002 1
HET CA 2011 1
HET CA 2012 1
HET NA 2101 1
HET NA 2102 1
HET CL 2201 1
HET CL 2202 1
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 5 CA 2(CA 2+)
FORMUL 7 NA 2(NA 1+)
FORMUL 9 CL 2(CL 1-)
FORMUL 11 HOH *1148(H2 O)
HELIX 1 1 GLU A 23 PHE A 27 5 5
HELIX 2 2 ASP A 36 ASN A 44 1 9
HELIX 3 3 SER A 58 GLY A 72 1 15
HELIX 4 4 GLY A 78 GLY A 86 1 9
HELIX 5 5 LEU A 98 ARG A 103 5 6
HELIX 6 6 GLN A 114 GLY A 129 1 16
HELIX 7 7 SER A 130 ASN A 141 1 12
HELIX 8 8 SER A 145 GLU A 149 5 5
HELIX 9 9 THR A 168 MET A 173 5 6
HELIX 10 10 ASP A 175 ALA A 191 1 17
HELIX 11 11 SER A 220 ARG A 230 1 11
HELIX 12 12 SER A 231 SER A 236 1 6
HELIX 13 13 THR A 239 SER A 245 1 7
HELIX 14 14 SER A 245 GLN A 254 1 10
HELIX 15 15 ASN A 288 CYS A 295 1 8
HELIX 16 16 CYS A 295 GLY A 300 1 6
HELIX 17 17 ASN A 304 GLY A 308 5 5
HELIX 18 18 ASP A 310 LEU A 314 5 5
HELIX 19 19 ASN A 321 MET A 325 5 5
HELIX 20 20 ASP A 371 LEU A 386 1 16
HELIX 21 21 GLU B 23 PHE B 27 5 5
HELIX 22 22 ASP B 36 ASN B 44 1 9
HELIX 23 23 SER B 58 GLY B 72 1 15
HELIX 24 24 GLY B 78 GLY B 86 1 9
HELIX 25 25 LEU B 98 ARG B 103 5 6
HELIX 26 26 GLN B 114 GLY B 129 1 16
HELIX 27 27 SER B 130 ASN B 141 1 12
HELIX 28 28 SER B 145 GLU B 149 5 5
HELIX 29 29 THR B 168 MET B 173 5 6
HELIX 30 30 ASP B 175 ALA B 191 1 17
HELIX 31 31 LEU B 208 GLY B 212 5 5
HELIX 32 32 SER B 220 ARG B 230 1 11
HELIX 33 33 SER B 231 SER B 236 1 6
HELIX 34 34 THR B 239 SER B 245 1 7
HELIX 35 35 SER B 245 VAL B 256 1 12
HELIX 36 36 ASN B 288 CYS B 295 1 8
HELIX 37 37 CYS B 295 GLY B 300 1 6
HELIX 38 38 ASN B 304 GLY B 308 5 5
HELIX 39 39 ASP B 310 LEU B 314 5 5
HELIX 40 40 ASN B 321 MET B 325 5 5
HELIX 41 41 ASP B 371 SER B 385 1 15
SHEET 1 A 7 THR A 48 LEU A 51 0
SHEET 2 A 7 ILE A 10 LEU A 13 1 N LEU A 12 O LEU A 51
SHEET 3 A 7 ILE A 107 HIS A 112 1 O HIS A 108 N VAL A 11
SHEET 4 A 7 VAL A 155 ILE A 161 1 O THR A 159 N ALA A 111
SHEET 5 A 7 TYR A 263 THR A 269 1 O LEU A 265 N THR A 160
SHEET 6 A 7 TRP A 348 TYR A 354 1 O TYR A 354 N SER A 268
SHEET 7 A 7 ILE A 336 PRO A 338 1 N VAL A 337 O TRP A 348
SHEET 1 B 2 GLY A 73 ASP A 76 0
SHEET 2 B 2 PHE A 90 TYR A 94 -1 O ARG A 92 N VAL A 75
SHEET 1 C 2 THR A 272 ARG A 274 0
SHEET 2 C 2 HIS A 281 PRO A 283 -1 O TYR A 282 N TYR A 273
SHEET 1 D 7 THR B 48 LEU B 51 0
SHEET 2 D 7 ILE B 10 LEU B 13 1 N ILE B 10 O TYR B 49
SHEET 3 D 7 ILE B 107 HIS B 112 1 O HIS B 108 N VAL B 11
SHEET 4 D 7 VAL B 155 ILE B 161 1 O THR B 159 N ALA B 111
SHEET 5 D 7 TYR B 263 THR B 269 1 O LEU B 265 N THR B 160
SHEET 6 D 7 TRP B 348 TYR B 354 1 O ASN B 349 N TYR B 264
SHEET 7 D 7 ILE B 336 PRO B 338 1 N VAL B 337 O TRP B 348
SHEET 1 E 2 GLY B 73 ASP B 76 0
SHEET 2 E 2 PHE B 90 TYR B 94 -1 O TYR B 94 N GLY B 73
SHEET 1 F 2 THR B 272 ARG B 274 0
SHEET 2 F 2 HIS B 281 PRO B 283 -1 O TYR B 282 N TYR B 273
CRYST1 117.731 81.270 99.912 90.00 97.09 90.00 C 1 2 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 0.008494 0.000000 0.001056 0.00000
SCALE2 0.000000 0.012305 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010086 0.00000
TER 3054 PRO A 388
TER 6108 PRO B 388
MASTER 350 0 8 41 22 0 0 6 7262 2 0 60
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