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HEADER HYDROLASE 11-NOV-16 5H6B
TITLE CRYSTAL STRUCTURE OF A THERMOSTABLE LIPASE FROM MARINE STREPTOMYCES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE SECRETED LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES SP. W007;
SOURCE 3 ORGANISM_TAXID: 1055352;
SOURCE 4 STRAIN: W007;
SOURCE 5 GENE: SPW_1544;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: X33;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS LIPASE, THERMOSTABILITY, MARINE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HOU,Z.ZHAO,J.LIU
REVDAT 1 20-SEP-17 5H6B 0
JRNL AUTH Z.ZHAO,S.HOU,D.LAN,X.WANG,J.LIU,F.I.KHAN,Y.WANG
JRNL TITL CRYSTAL STRUCTURE OF A LIPASE FROM STREPTOMYCES SP. STRAIN
JRNL TITL 2 W007:IMPLICATIONS FOR THERMOSTABILITY AND REGIOSPECIFICITY
JRNL REF FEBS J. 2017
JRNL REFN ISSN 1742-4658
JRNL PMID 28857479
JRNL DOI 10.1111/FEBS.14211
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 13955
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.600
REMARK 3 FREE R VALUE TEST SET COUNT : 827
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1036
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE SET COUNT : 54
REMARK 3 BIN FREE R VALUE : 0.2830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1903
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 45
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.11000
REMARK 3 B22 (A**2) : -1.11000
REMARK 3 B33 (A**2) : 3.62000
REMARK 3 B12 (A**2) : -0.56000
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): 0.238
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.181
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.136
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.781
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1972 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1865 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2695 ; 1.360 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4289 ; 0.968 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 251 ; 6.105 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 79 ;35.132 ;24.177
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 283 ;13.365 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;13.106 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 307 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2250 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 444 ; 0.002 ; 0.020
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): 1009 ; 2.201 ; 4.459
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1006 ; 2.196 ; 4.452
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1257 ; 3.258 ; 6.672
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; 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 : 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 : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5H6B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1300002106.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.2822
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.15
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14806
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 70.630
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.80
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.90
REMARK 200 R MERGE FOR SHELL (I) : 0.71800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M ZN(AC)2, 0.1M IMIDAZOLE, PH 6.5,
REMARK 280 10% PEG 8000, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 23.54000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 47.08000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 23.54000
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 47.08000
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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -103.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 136.09500
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 78.57448
REMARK 350 BIOMT3 2 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 ALA A 1
REMARK 465 THR A 2
REMARK 465 ALA A 3
REMARK 465 THR A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 THR A 7
REMARK 465 PRO A 8
REMARK 465 ALA A 9
REMARK 465 ALA A 10
REMARK 465 GLU A 11
REMARK 465 ALA A 12
REMARK 465 GLY A 265
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 PHE A 73 -37.26 77.41
REMARK 500 HIS A 75 -161.01 -107.72
REMARK 500 SER A 109 -127.46 62.85
REMARK 500 THR A 141 -157.22 -156.68
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 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 44 OD1
REMARK 620 2 HOH A 441 O 118.3
REMARK 620 3 HOH A 440 O 87.1 121.8
REMARK 620 4 ACT A 306 OXT 96.2 97.1 133.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 64 OD2
REMARK 620 2 HIS A 75 NE2 100.7
REMARK 620 3 IMD A 308 N1 97.5 137.0
REMARK 620 4 ASP A 212 OD2 54.2 55.8 109.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 303 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 139 NE2
REMARK 620 2 ASP A 185 OD1 106.5
REMARK 620 3 ACT A 305 O 101.0 142.0
REMARK 620 4 ACT A 305 OXT 125.7 93.5 48.8
REMARK 620 5 IMD A 307 N3 104.5 121.3 74.8 106.7
REMARK 620 N 1 2 3 4
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 308
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5H6G RELATED DB: PDB
DBREF 5H6B A 1 265 UNP H0B8D4 H0B8D4_9ACTN 32 296
SEQRES 1 A 265 ALA THR ALA THR ALA ALA THR PRO ALA ALA GLU ALA THR
SEQRES 2 A 265 SER ARG GLY TRP ASN ASP TYR SER CYS LYS PRO SER ALA
SEQRES 3 A 265 ALA HIS PRO ARG PRO VAL VAL LEU VAL HIS GLY THR PHE
SEQRES 4 A 265 GLY ASN SER ILE ASP ASN TRP LEU VAL LEU ALA PRO TYR
SEQRES 5 A 265 LEU VAL ASN ARG GLY TYR CYS VAL PHE SER LEU ASP TYR
SEQRES 6 A 265 GLY GLN LEU PRO GLY VAL PRO PHE PHE HIS GLY LEU GLY
SEQRES 7 A 265 PRO ILE ASP LYS SER ALA GLU GLN LEU ASP VAL PHE VAL
SEQRES 8 A 265 ASP LYS VAL LEU ASP ALA THR GLY ALA PRO LYS ALA ASP
SEQRES 9 A 265 LEU VAL GLY HIS SER GLN GLY GLY MET MET PRO ASN TYR
SEQRES 10 A 265 TYR LEU LYS PHE LEU GLY GLY ALA ASP LYS VAL ASN ALA
SEQRES 11 A 265 LEU VAL GLY ILE ALA PRO ASP ASN HIS GLY THR THR LEU
SEQRES 12 A 265 LEU GLY LEU THR LYS LEU LEU PRO PHE PHE PRO GLY VAL
SEQRES 13 A 265 GLU LYS PHE ILE SER ASP ASN THR PRO GLY LEU ALA ASP
SEQRES 14 A 265 GLN VAL ALA GLY SER PRO PHE ILE THR LYS LEU THR ALA
SEQRES 15 A 265 GLY GLY ASP THR VAL PRO GLY VAL ARG TYR THR VAL ILE
SEQRES 16 A 265 ALA THR LYS TYR ASP GLN VAL VAL THR PRO TYR ARG THR
SEQRES 17 A 265 GLN TYR LEU ASP GLY PRO ASN VAL ARG ASN VAL LEU LEU
SEQRES 18 A 265 GLN ASP LEU CYS PRO VAL ASP LEU SER GLU HIS VAL ALA
SEQRES 19 A 265 ILE GLY THR ILE ASP ARG ILE ALA PHE HIS GLU VAL ALA
SEQRES 20 A 265 ASN ALA LEU ASP PRO ALA ARG ALA THR PRO THR THR CYS
SEQRES 21 A 265 ALA SER VAL ILE GLY
HET ZN A 301 1
HET ZN A 302 1
HET ZN A 303 1
HET ZN A 304 1
HET ACT A 305 4
HET ACT A 306 4
HET IMD A 307 5
HET IMD A 308 5
HETNAM ZN ZINC ION
HETNAM ACT ACETATE ION
HETNAM IMD IMIDAZOLE
FORMUL 2 ZN 4(ZN 2+)
FORMUL 6 ACT 2(C2 H3 O2 1-)
FORMUL 8 IMD 2(C3 H5 N2 1+)
FORMUL 10 HOH *45(H2 O)
HELIX 1 AA1 ILE A 43 LEU A 47 5 5
HELIX 2 AA2 VAL A 48 ASN A 55 1 8
HELIX 3 AA3 PRO A 79 GLY A 99 1 21
HELIX 4 AA4 SER A 109 MET A 114 1 6
HELIX 5 AA5 MET A 114 LEU A 122 1 9
HELIX 6 AA6 GLY A 123 ASP A 126 5 4
HELIX 7 AA7 THR A 142 LYS A 148 1 7
HELIX 8 AA8 LEU A 149 PHE A 153 5 5
HELIX 9 AA9 VAL A 156 ILE A 160 5 5
HELIX 10 AB1 THR A 164 ASP A 169 1 6
HELIX 11 AB2 SER A 174 ALA A 182 1 9
HELIX 12 AB3 PRO A 205 TYR A 210 5 6
HELIX 13 AB4 LEU A 221 CYS A 225 1 5
HELIX 14 AB5 GLU A 231 ILE A 238 1 8
HELIX 15 AB6 ASP A 239 ASP A 251 1 13
HELIX 16 AB7 PRO A 252 ALA A 255 5 4
HELIX 17 AB8 THR A 259 ILE A 264 5 6
SHEET 1 AA1 7 GLY A 16 TRP A 17 0
SHEET 2 AA1 7 CYS A 59 LEU A 63 1 O VAL A 60 N GLY A 16
SHEET 3 AA1 7 VAL A 32 VAL A 35 1 N LEU A 34 O PHE A 61
SHEET 4 AA1 7 ALA A 103 HIS A 108 1 O VAL A 106 N VAL A 33
SHEET 5 AA1 7 VAL A 128 ILE A 134 1 O ALA A 130 N LEU A 105
SHEET 6 AA1 7 ARG A 191 ALA A 196 1 O ARG A 191 N ASN A 129
SHEET 7 AA1 7 VAL A 216 LEU A 220 1 O VAL A 219 N VAL A 194
SSBOND 1 CYS A 22 CYS A 59 1555 1555 2.07
SSBOND 2 CYS A 225 CYS A 260 1555 1555 2.10
LINK OD1 ASP A 44 ZN ZN A 301 1555 1555 2.15
LINK OD2 ASP A 64 ZN ZN A 302 1555 1555 1.85
LINK NE2 HIS A 75 ZN ZN A 302 1555 1555 2.15
LINK OD1 ASP A 88 ZN ZN A 304 1555 1555 2.65
LINK NE2 HIS A 139 ZN ZN A 303 1555 1555 2.26
LINK OD1 ASP A 185 ZN ZN A 303 1555 1555 1.97
LINK ZN ZN A 301 O HOH A 441 1555 1555 2.06
LINK ZN ZN A 301 O HOH A 440 1555 1555 2.59
LINK ZN ZN A 301 OXT ACT A 306 1555 1555 2.42
LINK ZN ZN A 302 N1 IMD A 308 1555 1555 2.13
LINK ZN ZN A 303 O ACT A 305 1555 1555 2.61
LINK ZN ZN A 303 OXT ACT A 305 1555 1555 2.67
LINK ZN ZN A 303 N3 IMD A 307 1555 1555 2.06
LINK OD2 ASP A 212 ZN ZN A 302 1555 6544 2.05
CISPEP 1 THR A 204 PRO A 205 0 -9.72
SITE 1 AC1 4 ASP A 44 ACT A 306 HOH A 440 HOH A 441
SITE 1 AC2 4 ASP A 64 HIS A 75 ASP A 212 IMD A 308
SITE 1 AC3 4 HIS A 139 ASP A 185 ACT A 305 IMD A 307
SITE 1 AC4 4 ASP A 88 ASP A 92 LYS A 127 HOH A 408
SITE 1 AC5 8 GLN A 67 PRO A 69 HIS A 139 THR A 181
SITE 2 AC5 8 GLY A 183 ASP A 185 ZN A 303 IMD A 307
SITE 1 AC6 3 ASP A 44 PHE A 73 ZN A 301
SITE 1 AC7 10 GLN A 67 LEU A 68 VAL A 71 HIS A 75
SITE 2 AC7 10 HIS A 139 ASP A 185 ASP A 212 ZN A 303
SITE 3 AC7 10 ACT A 305 HOH A 426
SITE 1 AC8 6 ASN A 41 SER A 42 ILE A 43 ASP A 64
SITE 2 AC8 6 ASP A 212 ZN A 302
CRYST1 90.730 90.730 70.620 90.00 90.00 120.00 P 64 6
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 0.011022 0.006363 0.000000 0.00000
SCALE2 0.000000 0.012727 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014160 0.00000
TER 1904 ILE A 264
MASTER 364 0 8 17 7 0 12 6 1970 1 35 21
END |