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HEADER HYDROLASE 29-JUN-01 1JI3
TITLE CRYSTAL STRUCTURE OF THE FIRST THERMOSTABLE BACTERIAL
TITLE 2 LIPASE FROM BACILLUS STEAROTHERMOPHILUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS STEAROTHERMOPHILUS;
SOURCE 3 VARIANT: P1;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: M15[PREP4];
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PET PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PQE-60
KEYWDS LIPASE, METAL-BINDING, THERMOPHILIC
EXPDTA X-RAY DIFFRACTION
AUTHOR J.D.A.TYNDALL,S.SINCHAIKUL,L.A.FOTHERGILL-GILMORE,P.TAYLOR,
AUTHOR 2 M.D.WALKINSHAW
REVDAT 1 01-NOV-02 1JI3 0
JRNL AUTH J.D.A.TYNDALL,S.SINCHAIKUL,L.A.FOTHERGILL-GILMORE,
JRNL AUTH 2 P.TAYLOR,M.D.WALKINSHAW
JRNL TITL CRYSTAL STRUCTURE OF A THERMOSTABLE LIPASE FROM
JRNL TITL 2 BACILLUS STEAROTHERMOPHILUS P1
JRNL REF J.MOL.BIOL. V. 323 859 2002
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
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) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 44812
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 + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2395
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1000
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : 0.2000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 6470
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.73
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6287 ; 0.005 ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8553 ; 2.427 ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 774 ; 5.453 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 899 ; 0.142 ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7179 ; 0.002 ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1513 ; 0.277 ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 17 ; 0.234 ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 852 ; 0.174 ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3839 ; 1.322 ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6149 ; 2.430 ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2448 ; 3.823 ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2404 ; 6.177 ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JI3 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PRAGUE ON 06-JUL-2001.
REMARK 100 THE RCSB ID CODE IS RCSB013797.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-2001; 27-FEB-2001
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 6.80
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : SRS ; SRS
REMARK 200 BEAMLINE : PX14.1; PX9.5
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.480; 1.200
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47208
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 24.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 4.510
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.1500
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) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.29800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.160
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, AMMONIUM SULPHATE, PH 6.8,
REMARK 280 VAPOR DIFFUSION, HANGING DROP AT 290K
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 59.25000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.61850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 59.25000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.61850
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 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, 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG B 47 CB CG CD NE CZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI
REMARK 500 OE2 GLU B 284 O HOH 738 2.18
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 MET A 24 CE MET A 24 SD -0.036
REMARK 500 MET A 173 SD MET A 173 CG 0.036
REMARK 500 VAL A 293 CG1 VAL A 293 CB 0.031
REMARK 500 PRO A 297 CG PRO A 297 CB 0.030
REMARK 500 ASP A 310 CG ASP A 310 CB -0.030
REMARK 500 PRO B 146 CG PRO B 146 CB 0.034
REMARK 500 ARG B 214 CD ARG B 214 CG 0.029
REMARK 500 MET B 325 CE MET B 325 SD -0.033
REMARK 500 PRO B 328 CD PRO B 328 CG 0.032
REMARK 500 MET B 351 CE MET B 351 SD -0.030
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 ARG A 215 CG - CD - NE ANGL. DEV. =-17.7 DEGREES
REMARK 500 ASP A 310 CB - CA - C ANGL. DEV. =-19.0 DEGREES
REMARK 500 ASP A 310 CB - CG - OD1 ANGL. DEV. =-17.2 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 -49.16 71.39
REMARK 500 VAL B 203 -37.81 60.36
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 ALA A 1 SER A 2 145.27
REMARK 500 ALA B 1 SER B 2 137.80
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CVL RELATED DB: PDB
REMARK 900 BACTERIAL LIPASE
REMARK 900 RELATED ID: 4LIP RELATED DB: PDB
REMARK 900 BACTERIAL LIPASE
DBREF 1JI3 A 1 388 GB 7208599 AAF40217 30 417
DBREF 1JI3 B 1 388 GB 7208599 AAF40217 30 417
SEQADV 1JI3 VAL A 63 GB 7208599 ALA 92 CONFLICT
SEQADV 1JI3 VAL A 68 GB 7208599 ALA 97 CONFLICT
SEQADV 1JI3 VAL B 63 GB 7208599 ALA 92 CONFLICT
SEQADV 1JI3 VAL B 68 GB 7208599 ALA 97 CONFLICT
SEQRES 1 A 388 ALA SER LEU ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU
SEQRES 2 A 388 HIS GLY PHE THR GLY TRP GLY ARG GLU GLU MET PHE GLY
SEQRES 3 A 388 PHE LYS TYR TRP GLY GLY VAL ARG GLY ASP ILE GLU GLN
SEQRES 4 A 388 TRP LEU ASN ASP ASN GLY TYR ARG THR TYR THR LEU ALA
SEQRES 5 A 388 VAL GLY PRO LEU SER SER ASN TRP ASP ARG VAL CYS GLU
SEQRES 6 A 388 ALA TYR VAL GLN LEU VAL GLY GLY THR VAL ASP TYR GLY
SEQRES 7 A 388 ALA ALA HIS ALA ALA LYS HIS GLY HIS ALA ARG PHE GLY
SEQRES 8 A 388 ARG THR TYR PRO GLY LEU LEU PRO GLU LEU LYS ARG GLY
SEQRES 9 A 388 GLY ARG ILE HIS ILE ILE ALA HIS SER GLN GLY GLY GLN
SEQRES 10 A 388 THR ALA ARG MET LEU VAL SER LEU LEU GLU ASN GLY SER
SEQRES 11 A 388 GLN GLU GLU ARG GLU TYR ALA LYS ALA HIS ASN VAL SER
SEQRES 12 A 388 LEU SER PRO LEU PHE GLU GLY GLY HIS HIS PHE VAL LEU
SEQRES 13 A 388 SER VAL THR THR ILE ALA THR PRO HIS ASP GLY THR THR
SEQRES 14 A 388 LEU VAL ASN MET VAL ASP PHE THR ASP ARG PHE PHE ASP
SEQRES 15 A 388 LEU GLN LYS ALA VAL LEU GLU ALA ALA ALA VAL ALA SER
SEQRES 16 A 388 ASN VAL PRO TYR THR SER GLN VAL TYR ASP PHE LYS LEU
SEQRES 17 A 388 ASP GLN TRP GLY LEU ARG ARG GLN PRO GLY GLU SER PHE
SEQRES 18 A 388 ASP HIS TYR PHE GLU ARG LEU LYS ARG SER PRO VAL TRP
SEQRES 19 A 388 THR SER THR ASP THR ALA ARG TYR ASP LEU SER VAL SER
SEQRES 20 A 388 GLY ALA GLU LYS LEU ASN GLN TRP VAL GLN ALA SER PRO
SEQRES 21 A 388 ASN THR TYR TYR LEU SER PHE SER THR GLU ARG THR TYR
SEQRES 22 A 388 ARG GLY ALA LEU THR GLY ASN HIS TYR PRO GLU LEU GLY
SEQRES 23 A 388 MET ASN ALA PHE SER ALA VAL VAL CYS ALA PRO PHE LEU
SEQRES 24 A 388 GLY SER TYR ARG ASN PRO THR LEU GLY ILE ASP SER HIS
SEQRES 25 A 388 TRP LEU GLU ASN ASP GLY ILE VAL ASN THR ILE SER MET
SEQRES 26 A 388 ASN GLY PRO LYS ARG GLY SER ASN ASP ARG ILE VAL PRO
SEQRES 27 A 388 TYR ASP GLY THR LEU LYS LYS GLY VAL TRP ASN ASP MET
SEQRES 28 A 388 GLY THR TYR ASN VAL ASP HIS LEU GLU ILE ILE GLY VAL
SEQRES 29 A 388 ASP PRO ASN PRO SER PHE ASP ILE ARG ALA PHE TYR LEU
SEQRES 30 A 388 ARG LEU ALA GLU GLN LEU ALA SER LEU GLN PRO
SEQRES 1 B 388 ALA SER LEU ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU
SEQRES 2 B 388 HIS GLY PHE THR GLY TRP GLY ARG GLU GLU MET PHE GLY
SEQRES 3 B 388 PHE LYS TYR TRP GLY GLY VAL ARG GLY ASP ILE GLU GLN
SEQRES 4 B 388 TRP LEU ASN ASP ASN GLY TYR ARG THR TYR THR LEU ALA
SEQRES 5 B 388 VAL GLY PRO LEU SER SER ASN TRP ASP ARG VAL CYS GLU
SEQRES 6 B 388 ALA TYR VAL GLN LEU VAL GLY GLY THR VAL ASP TYR GLY
SEQRES 7 B 388 ALA ALA HIS ALA ALA LYS HIS GLY HIS ALA ARG PHE GLY
SEQRES 8 B 388 ARG THR TYR PRO GLY LEU LEU PRO GLU LEU LYS ARG GLY
SEQRES 9 B 388 GLY ARG ILE HIS ILE ILE ALA HIS SER GLN GLY GLY GLN
SEQRES 10 B 388 THR ALA ARG MET LEU VAL SER LEU LEU GLU ASN GLY SER
SEQRES 11 B 388 GLN GLU GLU ARG GLU TYR ALA LYS ALA HIS ASN VAL SER
SEQRES 12 B 388 LEU SER PRO LEU PHE GLU GLY GLY HIS HIS PHE VAL LEU
SEQRES 13 B 388 SER VAL THR THR ILE ALA THR PRO HIS ASP GLY THR THR
SEQRES 14 B 388 LEU VAL ASN MET VAL ASP PHE THR ASP ARG PHE PHE ASP
SEQRES 15 B 388 LEU GLN LYS ALA VAL LEU GLU ALA ALA ALA VAL ALA SER
SEQRES 16 B 388 ASN VAL PRO TYR THR SER GLN VAL TYR ASP PHE LYS LEU
SEQRES 17 B 388 ASP GLN TRP GLY LEU ARG ARG GLN PRO GLY GLU SER PHE
SEQRES 18 B 388 ASP HIS TYR PHE GLU ARG LEU LYS ARG SER PRO VAL TRP
SEQRES 19 B 388 THR SER THR ASP THR ALA ARG TYR ASP LEU SER VAL SER
SEQRES 20 B 388 GLY ALA GLU LYS LEU ASN GLN TRP VAL GLN ALA SER PRO
SEQRES 21 B 388 ASN THR TYR TYR LEU SER PHE SER THR GLU ARG THR TYR
SEQRES 22 B 388 ARG GLY ALA LEU THR GLY ASN HIS TYR PRO GLU LEU GLY
SEQRES 23 B 388 MET ASN ALA PHE SER ALA VAL VAL CYS ALA PRO PHE LEU
SEQRES 24 B 388 GLY SER TYR ARG ASN PRO THR LEU GLY ILE ASP SER HIS
SEQRES 25 B 388 TRP LEU GLU ASN ASP GLY ILE VAL ASN THR ILE SER MET
SEQRES 26 B 388 ASN GLY PRO LYS ARG GLY SER ASN ASP ARG ILE VAL PRO
SEQRES 27 B 388 TYR ASP GLY THR LEU LYS LYS GLY VAL TRP ASN ASP MET
SEQRES 28 B 388 GLY THR TYR ASN VAL ASP HIS LEU GLU ILE ILE GLY VAL
SEQRES 29 B 388 ASP PRO ASN PRO SER PHE ASP ILE ARG ALA PHE TYR LEU
SEQRES 30 B 388 ARG LEU ALA GLU GLN LEU ALA SER LEU GLN PRO
HET CA A 401 1
HET ZN A 402 1
HET CA B 403 1
HET ZN B 404 1
HETNAM CA CALCIUM ION
HETNAM ZN ZINC ION
FORMUL 3 CA 2(CA1 2+)
FORMUL 4 ZN 2(ZN1 2+)
FORMUL 7 HOH *347(H2 O1)
HELIX 1 1 GLY A 31 GLY A 35 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 GLY A 104 5 7
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 LEU A 208 GLY A 212 5 5
HELIX 12 12 SER A 220 ARG A 230 1 11
HELIX 13 13 SER A 231 SER A 236 1 6
HELIX 14 14 THR A 239 SER A 245 1 7
HELIX 15 15 SER A 245 VAL A 256 1 12
HELIX 16 16 ASN A 288 CYS A 295 1 8
HELIX 17 17 CYS A 295 GLY A 300 1 6
HELIX 18 18 PRO A 305 GLY A 308 5 4
HELIX 19 19 ASP A 310 LEU A 314 5 5
HELIX 20 20 THR A 322 MET A 325 5 4
HELIX 21 21 ASP A 371 SER A 385 1 15
HELIX 22 22 GLU B 23 PHE B 27 5 5
HELIX 23 23 GLY B 31 GLY B 35 5 5
HELIX 24 24 ASP B 36 ASN B 44 1 9
HELIX 25 25 SER B 58 GLY B 72 1 15
HELIX 26 26 GLY B 78 GLY B 86 1 9
HELIX 27 27 LEU B 98 GLY B 104 5 7
HELIX 28 28 GLN B 114 GLY B 129 1 16
HELIX 29 29 SER B 130 HIS B 140 1 11
HELIX 30 30 SER B 145 GLU B 149 5 5
HELIX 31 31 THR B 168 MET B 173 5 6
HELIX 32 32 ASP B 175 ALA B 191 1 17
HELIX 33 33 LEU B 208 GLY B 212 5 5
HELIX 34 34 SER B 220 LYS B 229 1 10
HELIX 35 35 SER B 231 SER B 236 1 6
HELIX 36 36 THR B 239 SER B 245 1 7
HELIX 37 37 SER B 245 VAL B 256 1 12
HELIX 38 38 ASN B 288 CYS B 295 1 8
HELIX 39 39 CYS B 295 GLY B 300 1 6
HELIX 40 40 PRO B 305 GLY B 308 5 4
HELIX 41 41 ASP B 310 LEU B 314 5 5
HELIX 42 42 THR B 322 MET B 325 5 4
HELIX 43 43 ASP B 371 SER B 385 1 15
SHEET 1 A 7 THR A 48 THR A 50 0
SHEET 2 A 7 ILE A 10 LEU A 13 1 O ILE A 10 N TYR A 49
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 N LEU A 156 O ILE A 107
SHEET 5 A 7 TYR A 263 THR A 269 1 N TYR A 263 O LEU A 156
SHEET 6 A 7 TRP A 348 TYR A 354 1 N ASN A 349 O TYR A 264
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 N GLY A 91 O 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 N TYR A 282 O TYR A 273
SHEET 1 D 7 THR B 48 THR B 50 0
SHEET 2 D 7 ILE B 10 LEU B 13 1 O ILE B 10 N 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 N LEU B 156 O ILE B 107
SHEET 5 D 7 TYR B 263 GLU B 270 1 O TYR B 263 N VAL B 158
SHEET 6 D 7 TRP B 348 ASN B 355 1 N ASN B 349 O 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 N GLY B 91 O VAL B 75
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 118.500 81.237 99.782 90.00 96.33 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 0.008439 0.000000 0.000937 0.00000
SCALE2 0.000000 0.012310 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010083 0.00000
END |