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HEADER HYDROLASE 08-FEB-11 3AUK
TITLE CRYSTAL STRUCTURE OF A LIPASE FROM GEOBACILLUS SP. SBS-4S
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS;
SOURCE 3 ORGANISM_TAXID: 558164;
SOURCE 4 STRAIN: SBS-4S;
SOURCE 5 GENE: LIP;
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: PET
KEYWDS ALPHA/BETA HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.ANGKAWIDJAJA,M.TAYYAB,N.RASHID,S.KANAYA
REVDAT 1 08-FEB-12 3AUK 0
JRNL AUTH M.TAYYAB,C.ANGKAWIDJAJA,S.KANAYA,N.RASHID
JRNL TITL CRYSTAL STRUCTURE OF A LIPASE FROM GEOBACILLUS SP. SBS-4S
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.66 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.15
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 56338
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) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.66
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.70
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4116
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE SET COUNT : 214
REMARK 3 BIN FREE R VALUE : 0.2740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3045
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 592
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.77000
REMARK 3 B22 (A**2) : 0.11000
REMARK 3 B33 (A**2) : -0.88000
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): 0.082
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.052
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.539
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.960
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3134 ; 0.007 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4264 ; 0.981 ; 1.933
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 387 ; 6.937 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 158 ;34.584 ;23.165
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 474 ;14.671 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;17.730 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 446 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2482 ; 0.022 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; 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 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION 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): 1912 ; 1.889 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3058 ; 2.945 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1222 ; 4.614 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1205 ; 7.250 ; 4.500
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3AUK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-FEB-11.
REMARK 100 THE RCSB ID CODE IS RCSB029712.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-APR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL38B1
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 : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59613
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : 0.04900
REMARK 200 FOR THE DATA SET : 23.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.47200
REMARK 200 R SYM FOR SHELL (I) : 0.41200
REMARK 200 FOR SHELL : 2.700
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 1KUO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M IMIDAZOLE PH 8.0, 10% PEG 8000,
REMARK 280 0.2M CA-ACETATE, 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 27.56550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.13100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.87250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.13100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.56550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.87250
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 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
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 SER A 114 -132.76 60.47
REMARK 500 VAL A 204 -60.51 66.23
REMARK 500 ARG A 272 47.86 -147.65
REMARK 500 ASP A 311 -164.74 -122.22
REMARK 500 ILE A 320 -38.78 -136.83
REMARK 500 LYS A 330 -44.53 -130.68
REMARK 500 ASN A 368 91.56 -162.04
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 90 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 390 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 82 NE2
REMARK 620 2 ASP A 239 OD2 109.2
REMARK 620 3 ASP A 62 OD1 100.7 124.9
REMARK 620 4 HIS A 88 NE2 106.0 96.4 118.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 391 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 287 O
REMARK 620 2 GLU A 361 OE2 81.4
REMARK 620 3 ASP A 366 OD2 96.9 94.3
REMARK 620 4 PRO A 367 O 172.7 91.7 85.9
REMARK 620 5 HOH A 415 O 90.2 167.5 95.8 96.3
REMARK 620 6 HOH A 864 O 92.2 90.6 170.2 85.5 80.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 390
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 391
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 392
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 393
DBREF 3AUK A 1 389 UNP B9ZZP0 B9ZZP0_9BACI 1 389
SEQRES 1 A 389 MET ALA ALA SER ARG ALA ASN ASP ALA PRO ILE VAL LEU
SEQRES 2 A 389 LEU HIS GLY PHE THR GLY TRP GLY ARG GLU GLU MET PHE
SEQRES 3 A 389 GLY PHE LYS TYR TRP GLY GLY VAL ARG GLY ASP ILE GLU
SEQRES 4 A 389 GLN TRP LEU ASN ASP ASN GLY TYR ARG THR TYR THR LEU
SEQRES 5 A 389 ALA VAL GLY PRO LEU SER SER ASN TRP ASP ARG ALA CYS
SEQRES 6 A 389 GLU ALA TYR ALA GLN LEU VAL GLY GLY THR VAL ASP TYR
SEQRES 7 A 389 GLY ALA ALA HIS ALA ALA LYS HIS GLY HIS ALA ARG PHE
SEQRES 8 A 389 GLY ARG THR TYR LEU GLY LEU LEU PRO GLU LEU LYS ARG
SEQRES 9 A 389 GLY GLY ARG ILE HIS ILE ILE ALA HIS SER GLN GLY GLY
SEQRES 10 A 389 GLN THR ALA ARG MET LEU VAL SER LEU LEU GLU ASN GLY
SEQRES 11 A 389 SER GLN GLU GLU ARG GLU TYR ALA LYS ALA HIS ASN VAL
SEQRES 12 A 389 SER LEU SER PRO LEU PHE GLU GLY GLY HIS HIS PHE VAL
SEQRES 13 A 389 LEU SER VAL THR THR ILE ALA THR PRO HIS ASP GLY THR
SEQRES 14 A 389 THR LEU VAL ASN MET VAL ASP PHE THR ASP ARG PHE PHE
SEQRES 15 A 389 ASP LEU GLN LYS ALA VAL LEU GLU ALA ALA ALA VAL ALA
SEQRES 16 A 389 SER ASN VAL PRO TYR THR SER GLN VAL TYR ASP PHE LYS
SEQRES 17 A 389 LEU ASP GLN TRP GLY LEU ARG ARG GLN PRO GLY GLU SER
SEQRES 18 A 389 PHE ASP HIS TYR PHE GLU ARG LEU LYS ARG SER PRO VAL
SEQRES 19 A 389 TRP THR SER THR ASP THR ALA ARG TYR ASP LEU SER VAL
SEQRES 20 A 389 SER GLY ALA GLU LYS LEU ASN GLN TRP VAL GLN ALA SER
SEQRES 21 A 389 PRO ASN THR TYR TYR LEU SER PHE ALA THR GLU ARG THR
SEQRES 22 A 389 TYR ARG GLY ALA LEU THR GLY ASN TYR TYR PRO GLU LEU
SEQRES 23 A 389 GLY MET ASN ALA PHE SER ALA VAL VAL CYS ALA PRO PHE
SEQRES 24 A 389 LEU GLY SER TYR ARG ASN PRO THR LEU GLY ILE ASP ASP
SEQRES 25 A 389 ARG TRP LEU GLU ASN ASP GLY ILE VAL ASN THR VAL SER
SEQRES 26 A 389 MET ASN GLY PRO LYS ARG GLY SER SER ASP ARG ILE VAL
SEQRES 27 A 389 PRO TYR ASP GLY ALA LEU LYS LYS GLY VAL TRP ASN ASP
SEQRES 28 A 389 MET GLY THR TYR ASN VAL ASP HIS LEU GLU ILE ILE GLY
SEQRES 29 A 389 VAL ASP PRO ASN PRO SER PHE ASP ILE ARG ALA PHE TYR
SEQRES 30 A 389 LEU ARG LEU ALA GLU GLN LEU ALA SER LEU GLN PRO
HET ZN A 390 1
HET CA A 391 1
HET CL A 392 1
HET CL A 393 1
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
FORMUL 2 ZN ZN 2+
FORMUL 3 CA CA 2+
FORMUL 4 CL 2(CL 1-)
FORMUL 6 HOH *592(H2 O)
HELIX 1 1 GLU A 24 PHE A 28 5 5
HELIX 2 2 GLY A 32 GLY A 36 5 5
HELIX 3 3 ASP A 37 ASN A 45 1 9
HELIX 4 4 SER A 59 GLY A 73 1 15
HELIX 5 5 GLY A 79 GLY A 87 1 9
HELIX 6 6 LEU A 99 LYS A 103 5 5
HELIX 7 7 GLN A 115 GLY A 130 1 16
HELIX 8 8 SER A 131 ASN A 142 1 12
HELIX 9 9 SER A 146 GLY A 151 5 6
HELIX 10 10 THR A 169 MET A 174 5 6
HELIX 11 11 ASP A 176 ALA A 192 1 17
HELIX 12 12 LEU A 209 GLY A 213 5 5
HELIX 13 13 SER A 221 ARG A 231 1 11
HELIX 14 14 SER A 232 SER A 237 1 6
HELIX 15 15 THR A 240 SER A 246 1 7
HELIX 16 16 SER A 246 VAL A 257 1 12
HELIX 17 17 ASN A 289 CYS A 296 1 8
HELIX 18 18 CYS A 296 GLY A 301 1 6
HELIX 19 19 ASN A 305 GLY A 309 5 5
HELIX 20 20 ASP A 311 LEU A 315 5 5
HELIX 21 21 ASN A 322 MET A 326 5 5
HELIX 22 22 ASP A 372 SER A 386 1 15
SHEET 1 A 7 THR A 49 LEU A 52 0
SHEET 2 A 7 ILE A 11 LEU A 14 1 N LEU A 13 O LEU A 52
SHEET 3 A 7 ILE A 108 HIS A 113 1 O ILE A 111 N VAL A 12
SHEET 4 A 7 VAL A 156 ILE A 162 1 O THR A 160 N ALA A 112
SHEET 5 A 7 TYR A 264 THR A 270 1 O LEU A 266 N VAL A 159
SHEET 6 A 7 TRP A 349 TYR A 355 1 O ASN A 350 N TYR A 265
SHEET 7 A 7 ILE A 337 PRO A 339 1 N VAL A 338 O TRP A 349
SHEET 1 B 2 GLY A 74 ASP A 77 0
SHEET 2 B 2 PHE A 91 TYR A 95 -1 O ARG A 93 N VAL A 76
SHEET 1 C 2 THR A 273 ARG A 275 0
SHEET 2 C 2 TYR A 282 PRO A 284 -1 O TYR A 283 N TYR A 274
LINK NE2 HIS A 82 ZN ZN A 390 1555 1555 1.97
LINK OD2 ASP A 239 ZN ZN A 390 1555 1555 1.98
LINK OD1 ASP A 62 ZN ZN A 390 1555 1555 2.03
LINK NE2 HIS A 88 ZN ZN A 390 1555 1555 2.07
LINK O GLY A 287 CA CA A 391 1555 1555 2.26
LINK OE2 GLU A 361 CA CA A 391 1555 1555 2.32
LINK OD2 ASP A 366 CA CA A 391 1555 1555 2.33
LINK O PRO A 367 CA CA A 391 1555 1555 2.34
LINK CA CA A 391 O HOH A 415 1555 1555 2.37
LINK CA CA A 391 O HOH A 864 1555 1555 2.41
SITE 1 AC1 4 ASP A 62 HIS A 82 HIS A 88 ASP A 239
SITE 1 AC2 6 GLY A 287 GLU A 361 ASP A 366 PRO A 367
SITE 2 AC2 6 HOH A 415 HOH A 864
SITE 1 AC3 2 SER A 248 HOH A 880
SITE 1 AC4 6 ARG A 35 PRO A 367 ASN A 368 PRO A 369
SITE 2 AC4 6 HOH A 866 HOH A 925
CRYST1 55.131 71.745 126.262 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 0.018139 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013938 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007920 0.00000
TER 3055 PRO A 389
MASTER 321 0 4 22 11 0 6 6 3641 1 13 30
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