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HEADER HYDROLASE 11-NOV-16 5H6G
TITLE CRYSTAL STRUCTURE OF A THERMOSTABLE LIPASE FROM MARINE STREPTOMYCES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE SECRETED LIPASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 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 5H6G 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. 2.34 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 : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 64.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 53333
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) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2850
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) : 2.34
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.40
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3885
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.2930
REMARK 3 BIN FREE R VALUE SET COUNT : 207
REMARK 3 BIN FREE R VALUE : 0.3230
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5731
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.47000
REMARK 3 B22 (A**2) : 0.47000
REMARK 3 B33 (A**2) : -1.51000
REMARK 3 B12 (A**2) : 0.23000
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): 0.203
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.176
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.139
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.237
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5912 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5570 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8096 ; 1.530 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12824 ; 1.003 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 757 ; 6.465 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 238 ;37.301 ;24.160
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 850 ;15.489 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;19.727 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 923 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6730 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1310 ; 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): 3037 ; 2.402 ; 4.168
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3036 ; 2.401 ; 4.167
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3791 ; 3.709 ; 6.241
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 : MASK
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 5H6G 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_1300002112.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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) : 0.9791
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.1.30
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56185
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.340
REMARK 200 RESOLUTION RANGE LOW (A) : 64.750
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 10.50
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.41
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 10.40
REMARK 200 R MERGE FOR SHELL (I) : 0.92900
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 5H6B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M SODIUM PHOSPHATE MONOBASIC
REMARK 280 MONOHYDRATE, POTASSIUM PHOSPHATE DIBASIC (PH 5.0), VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-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 91.88667
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 45.94333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 45.94333
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 91.88667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 CL CL A 302 LIES ON A SPECIAL POSITION.
REMARK 375 CL CL A 303 LIES ON A SPECIAL POSITION.
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 HIS A 266
REMARK 465 HIS A 267
REMARK 465 HIS A 268
REMARK 465 HIS A 269
REMARK 465 HIS A 270
REMARK 465 HIS A 271
REMARK 465 ALA B 1
REMARK 465 THR B 2
REMARK 465 ALA B 3
REMARK 465 THR B 4
REMARK 465 ALA B 5
REMARK 465 ALA B 6
REMARK 465 THR B 7
REMARK 465 PRO B 8
REMARK 465 ALA B 9
REMARK 465 ALA B 10
REMARK 465 GLU B 11
REMARK 465 ALA B 12
REMARK 465 HIS B 267
REMARK 465 HIS B 268
REMARK 465 HIS B 269
REMARK 465 HIS B 270
REMARK 465 HIS B 271
REMARK 465 ALA C 1
REMARK 465 THR C 2
REMARK 465 ALA C 3
REMARK 465 THR C 4
REMARK 465 ALA C 5
REMARK 465 ALA C 6
REMARK 465 THR C 7
REMARK 465 PRO C 8
REMARK 465 ALA C 9
REMARK 465 ALA C 10
REMARK 465 GLU C 11
REMARK 465 ALA C 12
REMARK 465 HIS C 266
REMARK 465 HIS C 267
REMARK 465 HIS C 268
REMARK 465 HIS C 269
REMARK 465 HIS C 270
REMARK 465 HIS C 271
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 -42.25 78.45
REMARK 500 SER A 109 -124.18 55.64
REMARK 500 THR A 141 -155.85 -149.51
REMARK 500 ASN A 215 51.18 -110.27
REMARK 500 PHE B 73 -45.90 72.85
REMARK 500 HIS B 75 -168.95 -109.32
REMARK 500 SER B 109 -125.57 62.97
REMARK 500 THR B 141 -151.82 -149.65
REMARK 500 ASN B 215 50.27 -113.26
REMARK 500 PHE C 39 -2.04 74.53
REMARK 500 ILE C 43 -60.83 -102.88
REMARK 500 PHE C 73 -46.00 70.06
REMARK 500 SER C 109 -122.15 66.72
REMARK 500 ASN C 163 55.18 -90.15
REMARK 500 ASP C 251 70.55 -151.21
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 K B 301 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 88 OD1
REMARK 620 2 ASP B 88 OD2 38.2
REMARK 620 3 ASP B 92 OD2 78.3 110.5
REMARK 620 4 HOH B 421 O 57.4 89.4 67.3
REMARK 620 5 ASP C 88 OD1 42.6 80.5 49.5 26.7
REMARK 620 6 ASP C 92 OD2 43.8 81.9 46.7 28.7 2.8
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 PO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5H6B RELATED DB: PDB
DBREF 5H6G A 1 265 UNP H0B8D4 H0B8D4_9ACTN 32 296
DBREF 5H6G B 1 265 UNP H0B8D4 H0B8D4_9ACTN 32 296
DBREF 5H6G C 1 265 UNP H0B8D4 H0B8D4_9ACTN 32 296
SEQADV 5H6G HIS A 266 UNP H0B8D4 EXPRESSION TAG
SEQADV 5H6G HIS A 267 UNP H0B8D4 EXPRESSION TAG
SEQADV 5H6G HIS A 268 UNP H0B8D4 EXPRESSION TAG
SEQADV 5H6G HIS A 269 UNP H0B8D4 EXPRESSION TAG
SEQADV 5H6G HIS A 270 UNP H0B8D4 EXPRESSION TAG
SEQADV 5H6G HIS A 271 UNP H0B8D4 EXPRESSION TAG
SEQADV 5H6G HIS B 266 UNP H0B8D4 EXPRESSION TAG
SEQADV 5H6G HIS B 267 UNP H0B8D4 EXPRESSION TAG
SEQADV 5H6G HIS B 268 UNP H0B8D4 EXPRESSION TAG
SEQADV 5H6G HIS B 269 UNP H0B8D4 EXPRESSION TAG
SEQADV 5H6G HIS B 270 UNP H0B8D4 EXPRESSION TAG
SEQADV 5H6G HIS B 271 UNP H0B8D4 EXPRESSION TAG
SEQADV 5H6G HIS C 266 UNP H0B8D4 EXPRESSION TAG
SEQADV 5H6G HIS C 267 UNP H0B8D4 EXPRESSION TAG
SEQADV 5H6G HIS C 268 UNP H0B8D4 EXPRESSION TAG
SEQADV 5H6G HIS C 269 UNP H0B8D4 EXPRESSION TAG
SEQADV 5H6G HIS C 270 UNP H0B8D4 EXPRESSION TAG
SEQADV 5H6G HIS C 271 UNP H0B8D4 EXPRESSION TAG
SEQRES 1 A 271 ALA THR ALA THR ALA ALA THR PRO ALA ALA GLU ALA THR
SEQRES 2 A 271 SER ARG GLY TRP ASN ASP TYR SER CYS LYS PRO SER ALA
SEQRES 3 A 271 ALA HIS PRO ARG PRO VAL VAL LEU VAL HIS GLY THR PHE
SEQRES 4 A 271 GLY ASN SER ILE ASP ASN TRP LEU VAL LEU ALA PRO TYR
SEQRES 5 A 271 LEU VAL ASN ARG GLY TYR CYS VAL PHE SER LEU ASP TYR
SEQRES 6 A 271 GLY GLN LEU PRO GLY VAL PRO PHE PHE HIS GLY LEU GLY
SEQRES 7 A 271 PRO ILE ASP LYS SER ALA GLU GLN LEU ASP VAL PHE VAL
SEQRES 8 A 271 ASP LYS VAL LEU ASP ALA THR GLY ALA PRO LYS ALA ASP
SEQRES 9 A 271 LEU VAL GLY HIS SER GLN GLY GLY MET MET PRO ASN TYR
SEQRES 10 A 271 TYR LEU LYS PHE LEU GLY GLY ALA ASP LYS VAL ASN ALA
SEQRES 11 A 271 LEU VAL GLY ILE ALA PRO ASP ASN HIS GLY THR THR LEU
SEQRES 12 A 271 LEU GLY LEU THR LYS LEU LEU PRO PHE PHE PRO GLY VAL
SEQRES 13 A 271 GLU LYS PHE ILE SER ASP ASN THR PRO GLY LEU ALA ASP
SEQRES 14 A 271 GLN VAL ALA GLY SER PRO PHE ILE THR LYS LEU THR ALA
SEQRES 15 A 271 GLY GLY ASP THR VAL PRO GLY VAL ARG TYR THR VAL ILE
SEQRES 16 A 271 ALA THR LYS TYR ASP GLN VAL VAL THR PRO TYR ARG THR
SEQRES 17 A 271 GLN TYR LEU ASP GLY PRO ASN VAL ARG ASN VAL LEU LEU
SEQRES 18 A 271 GLN ASP LEU CYS PRO VAL ASP LEU SER GLU HIS VAL ALA
SEQRES 19 A 271 ILE GLY THR ILE ASP ARG ILE ALA PHE HIS GLU VAL ALA
SEQRES 20 A 271 ASN ALA LEU ASP PRO ALA ARG ALA THR PRO THR THR CYS
SEQRES 21 A 271 ALA SER VAL ILE GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 B 271 ALA THR ALA THR ALA ALA THR PRO ALA ALA GLU ALA THR
SEQRES 2 B 271 SER ARG GLY TRP ASN ASP TYR SER CYS LYS PRO SER ALA
SEQRES 3 B 271 ALA HIS PRO ARG PRO VAL VAL LEU VAL HIS GLY THR PHE
SEQRES 4 B 271 GLY ASN SER ILE ASP ASN TRP LEU VAL LEU ALA PRO TYR
SEQRES 5 B 271 LEU VAL ASN ARG GLY TYR CYS VAL PHE SER LEU ASP TYR
SEQRES 6 B 271 GLY GLN LEU PRO GLY VAL PRO PHE PHE HIS GLY LEU GLY
SEQRES 7 B 271 PRO ILE ASP LYS SER ALA GLU GLN LEU ASP VAL PHE VAL
SEQRES 8 B 271 ASP LYS VAL LEU ASP ALA THR GLY ALA PRO LYS ALA ASP
SEQRES 9 B 271 LEU VAL GLY HIS SER GLN GLY GLY MET MET PRO ASN TYR
SEQRES 10 B 271 TYR LEU LYS PHE LEU GLY GLY ALA ASP LYS VAL ASN ALA
SEQRES 11 B 271 LEU VAL GLY ILE ALA PRO ASP ASN HIS GLY THR THR LEU
SEQRES 12 B 271 LEU GLY LEU THR LYS LEU LEU PRO PHE PHE PRO GLY VAL
SEQRES 13 B 271 GLU LYS PHE ILE SER ASP ASN THR PRO GLY LEU ALA ASP
SEQRES 14 B 271 GLN VAL ALA GLY SER PRO PHE ILE THR LYS LEU THR ALA
SEQRES 15 B 271 GLY GLY ASP THR VAL PRO GLY VAL ARG TYR THR VAL ILE
SEQRES 16 B 271 ALA THR LYS TYR ASP GLN VAL VAL THR PRO TYR ARG THR
SEQRES 17 B 271 GLN TYR LEU ASP GLY PRO ASN VAL ARG ASN VAL LEU LEU
SEQRES 18 B 271 GLN ASP LEU CYS PRO VAL ASP LEU SER GLU HIS VAL ALA
SEQRES 19 B 271 ILE GLY THR ILE ASP ARG ILE ALA PHE HIS GLU VAL ALA
SEQRES 20 B 271 ASN ALA LEU ASP PRO ALA ARG ALA THR PRO THR THR CYS
SEQRES 21 B 271 ALA SER VAL ILE GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 C 271 ALA THR ALA THR ALA ALA THR PRO ALA ALA GLU ALA THR
SEQRES 2 C 271 SER ARG GLY TRP ASN ASP TYR SER CYS LYS PRO SER ALA
SEQRES 3 C 271 ALA HIS PRO ARG PRO VAL VAL LEU VAL HIS GLY THR PHE
SEQRES 4 C 271 GLY ASN SER ILE ASP ASN TRP LEU VAL LEU ALA PRO TYR
SEQRES 5 C 271 LEU VAL ASN ARG GLY TYR CYS VAL PHE SER LEU ASP TYR
SEQRES 6 C 271 GLY GLN LEU PRO GLY VAL PRO PHE PHE HIS GLY LEU GLY
SEQRES 7 C 271 PRO ILE ASP LYS SER ALA GLU GLN LEU ASP VAL PHE VAL
SEQRES 8 C 271 ASP LYS VAL LEU ASP ALA THR GLY ALA PRO LYS ALA ASP
SEQRES 9 C 271 LEU VAL GLY HIS SER GLN GLY GLY MET MET PRO ASN TYR
SEQRES 10 C 271 TYR LEU LYS PHE LEU GLY GLY ALA ASP LYS VAL ASN ALA
SEQRES 11 C 271 LEU VAL GLY ILE ALA PRO ASP ASN HIS GLY THR THR LEU
SEQRES 12 C 271 LEU GLY LEU THR LYS LEU LEU PRO PHE PHE PRO GLY VAL
SEQRES 13 C 271 GLU LYS PHE ILE SER ASP ASN THR PRO GLY LEU ALA ASP
SEQRES 14 C 271 GLN VAL ALA GLY SER PRO PHE ILE THR LYS LEU THR ALA
SEQRES 15 C 271 GLY GLY ASP THR VAL PRO GLY VAL ARG TYR THR VAL ILE
SEQRES 16 C 271 ALA THR LYS TYR ASP GLN VAL VAL THR PRO TYR ARG THR
SEQRES 17 C 271 GLN TYR LEU ASP GLY PRO ASN VAL ARG ASN VAL LEU LEU
SEQRES 18 C 271 GLN ASP LEU CYS PRO VAL ASP LEU SER GLU HIS VAL ALA
SEQRES 19 C 271 ILE GLY THR ILE ASP ARG ILE ALA PHE HIS GLU VAL ALA
SEQRES 20 C 271 ASN ALA LEU ASP PRO ALA ARG ALA THR PRO THR THR CYS
SEQRES 21 C 271 ALA SER VAL ILE GLY HIS HIS HIS HIS HIS HIS
HET PO4 A 301 5
HET CL A 302 1
HET CL A 303 1
HET K B 301 1
HET PO4 B 302 5
HET PO4 B 303 5
HET PO4 B 304 5
HET GOL C 301 6
HETNAM PO4 PHOSPHATE ION
HETNAM CL CHLORIDE ION
HETNAM K POTASSIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 PO4 4(O4 P 3-)
FORMUL 5 CL 2(CL 1-)
FORMUL 7 K K 1+
FORMUL 11 GOL C3 H8 O3
FORMUL 12 HOH *110(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
HELIX 18 AB9 ILE B 43 LEU B 47 5 5
HELIX 19 AC1 VAL B 48 ARG B 56 1 9
HELIX 20 AC2 PRO B 79 GLY B 99 1 21
HELIX 21 AC3 SER B 109 MET B 114 1 6
HELIX 22 AC4 MET B 114 LEU B 122 1 9
HELIX 23 AC5 GLY B 123 ASP B 126 5 4
HELIX 24 AC6 THR B 142 LYS B 148 1 7
HELIX 25 AC7 LEU B 149 PHE B 153 5 5
HELIX 26 AC8 VAL B 156 ILE B 160 5 5
HELIX 27 AC9 THR B 164 ASP B 169 1 6
HELIX 28 AD1 SER B 174 THR B 181 1 8
HELIX 29 AD2 PRO B 205 TYR B 210 5 6
HELIX 30 AD3 LEU B 221 CYS B 225 1 5
HELIX 31 AD4 GLU B 231 ILE B 238 1 8
HELIX 32 AD5 ASP B 239 ASP B 251 1 13
HELIX 33 AD6 PRO B 252 ALA B 255 5 4
HELIX 34 AD7 THR B 259 ILE B 264 5 6
HELIX 35 AD8 ILE C 43 LEU C 47 5 5
HELIX 36 AD9 VAL C 48 ARG C 56 1 9
HELIX 37 AE1 PRO C 79 GLY C 99 1 21
HELIX 38 AE2 SER C 109 MET C 114 1 6
HELIX 39 AE3 MET C 114 LEU C 122 1 9
HELIX 40 AE4 THR C 142 LYS C 148 1 7
HELIX 41 AE5 LEU C 149 PHE C 153 5 5
HELIX 42 AE6 THR C 164 ASP C 169 1 6
HELIX 43 AE7 SER C 174 ALA C 182 1 9
HELIX 44 AE8 PRO C 205 TYR C 210 5 6
HELIX 45 AE9 LEU C 221 CYS C 225 1 5
HELIX 46 AF1 GLU C 231 ILE C 238 1 8
HELIX 47 AF2 ASP C 239 LEU C 250 1 12
HELIX 48 AF3 ASP C 251 ALA C 255 5 5
HELIX 49 AF4 THR C 259 ILE C 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 ASP A 104 N VAL A 33
SHEET 5 AA1 7 VAL A 128 ILE A 134 1 O ILE A 134 N GLY A 107
SHEET 6 AA1 7 ARG A 191 ALA A 196 1 O THR A 193 N GLY A 133
SHEET 7 AA1 7 VAL A 216 LEU A 220 1 O VAL A 219 N VAL A 194
SHEET 1 AA2 7 GLY B 16 TRP B 17 0
SHEET 2 AA2 7 CYS B 59 LEU B 63 1 O VAL B 60 N GLY B 16
SHEET 3 AA2 7 VAL B 32 VAL B 35 1 N LEU B 34 O PHE B 61
SHEET 4 AA2 7 ALA B 103 HIS B 108 1 O ASP B 104 N VAL B 33
SHEET 5 AA2 7 VAL B 128 ILE B 134 1 O VAL B 132 N LEU B 105
SHEET 6 AA2 7 ARG B 191 ALA B 196 1 O ILE B 195 N GLY B 133
SHEET 7 AA2 7 VAL B 216 LEU B 220 1 O VAL B 219 N VAL B 194
SHEET 1 AA3 7 GLY C 16 TRP C 17 0
SHEET 2 AA3 7 CYS C 59 LEU C 63 1 O VAL C 60 N GLY C 16
SHEET 3 AA3 7 VAL C 32 VAL C 35 1 N LEU C 34 O PHE C 61
SHEET 4 AA3 7 ALA C 103 HIS C 108 1 O ASP C 104 N VAL C 33
SHEET 5 AA3 7 VAL C 128 ILE C 134 1 O ILE C 134 N GLY C 107
SHEET 6 AA3 7 ARG C 191 ALA C 196 1 O THR C 193 N GLY C 133
SHEET 7 AA3 7 VAL C 216 LEU C 220 1 O VAL C 219 N VAL C 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
SSBOND 3 CYS B 22 CYS B 59 1555 1555 2.07
SSBOND 4 CYS B 225 CYS B 260 1555 1555 2.11
SSBOND 5 CYS C 22 CYS C 59 1555 1555 2.06
SSBOND 6 CYS C 225 CYS C 260 1555 1555 2.12
LINK OD1 ASP B 88 K K B 301 1555 1555 2.48
LINK OD2 ASP B 88 K K B 301 1555 1555 3.48
LINK OD2 ASP B 92 K K B 301 1555 1555 2.64
LINK K K B 301 O HOH B 421 1555 1555 3.41
LINK OD1 ASP C 88 K K B 301 1555 5544 2.65
LINK OD2 ASP C 92 K K B 301 1555 5544 2.45
CISPEP 1 THR A 204 PRO A 205 0 -14.86
CISPEP 2 THR B 204 PRO B 205 0 -3.31
CISPEP 3 THR C 204 PRO C 205 0 -11.10
SITE 1 AC1 2 TYR A 206 ARG A 207
SITE 1 AC2 4 ASP B 88 ASP B 92 ASP C 88 ASP C 92
SITE 1 AC3 3 LYS B 198 TYR B 206 ARG B 207
SITE 1 AC4 3 TRP B 17 ASN B 18 ILE B 43
SITE 1 AC5 2 PRO B 29 ARG B 30
SITE 1 AC6 3 TRP C 17 ASN C 18 ILE C 43
CRYST1 129.500 129.500 137.830 90.00 90.00 120.00 P 32 2 1 18
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 0.007722 0.004458 0.000000 0.00000
SCALE2 0.000000 0.008917 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007255 0.00000
TER 1908 GLY A 265
TER 3826 HIS B 266
TER 5734 GLY C 265
MASTER 415 0 8 49 21 0 6 6 5870 3 43 63
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