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HEADER HYDROLASE 02-DEC-20 7B4Q
TITLE STRUCTURE OF A COLD ACTIVE HSL FAMILY ESTERASE REVEALS MECHANISMS OF
TITLE 2 LOW TEMPERATURE ADAPTATION AND SUBSTRATE SPECIFICITY
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 COHNII NBRC 15565;
SOURCE 3 ORGANISM_TAXID: 1314751;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BACILLUS COHNII, ESTERASE, LOW TEMPERATURE ADAPTED, REGIO-SELECTIVE
KEYWDS 2 ESTERASE, HORMONE-SENSITIVE FAMILY, HYDROLASE, LIPASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.RIZKALLAH,D.D.JONES,N.NOBY,H.AUHIM
REVDAT 1 15-DEC-21 7B4Q 0
JRNL AUTH N.NOBY,H.S.AUHIM,S.WINTER,H.L.WORTHY,A.M.EMBABY,H.SAEED,
JRNL AUTH 2 A.HUSSEIN,C.R.PUDNEY,P.J.RIZKALLAH,S.A.WELLS,D.D.JONES
JRNL TITL STRUCTURE AND IN SILICO SIMULATIONS OF A COLD-ACTIVE
JRNL TITL 2 ESTERASE REVEALS ITS PRIME COLD-ADAPTATION MECHANISM.
JRNL REF OPEN BIOLOGY V. 11 10182 2021
JRNL REFN ESSN 2046-2441
JRNL PMID 34847772
JRNL DOI 10.1098/RSOB.210182
REMARK 2
REMARK 2 RESOLUTION. 1.61 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.61
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 83.03
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 95500
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5029
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) : 1.61
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.65
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6897
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.40
REMARK 3 BIN R VALUE (WORKING SET) : 0.2880
REMARK 3 BIN FREE R VALUE SET COUNT : 395
REMARK 3 BIN FREE R VALUE : 0.2930
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4886
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 584
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.12000
REMARK 3 B22 (A**2) : -0.12000
REMARK 3 B33 (A**2) : 0.25000
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): 0.076
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.077
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.541
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.964
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5145 ; 0.013 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4811 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7015 ; 1.766 ; 1.648
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11123 ; 1.513 ; 1.580
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 652 ; 6.611 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 275 ;33.458 ;22.836
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 824 ;13.100 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;21.398 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 632 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5939 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1123 ; 0.001 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 314 B 1 314 10174 0.100 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 314
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6358 33.3895 42.9796
REMARK 3 T TENSOR
REMARK 3 T11: 0.0108 T22: 0.0121
REMARK 3 T33: 0.0202 T12: 0.0073
REMARK 3 T13: 0.0072 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 1.7727 L22: 1.3421
REMARK 3 L33: 1.9147 L12: 0.0618
REMARK 3 L13: -1.1011 L23: 0.0052
REMARK 3 S TENSOR
REMARK 3 S11: -0.0879 S12: -0.0132 S13: -0.0927
REMARK 3 S21: -0.0079 S22: 0.0089 S23: 0.1325
REMARK 3 S31: 0.1104 S32: 0.0066 S33: 0.0790
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 314
REMARK 3 ORIGIN FOR THE GROUP (A): 44.2899 31.8432 23.7337
REMARK 3 T TENSOR
REMARK 3 T11: 0.0276 T22: 0.0859
REMARK 3 T33: 0.0657 T12: 0.0440
REMARK 3 T13: 0.0271 T23: 0.0338
REMARK 3 L TENSOR
REMARK 3 L11: 1.7667 L22: 1.5355
REMARK 3 L33: 2.2449 L12: 0.1263
REMARK 3 L13: -0.4889 L23: 0.0541
REMARK 3 S TENSOR
REMARK 3 S11: -0.0562 S12: -0.0262 S13: -0.1774
REMARK 3 S21: -0.0696 S22: 0.0010 S23: -0.2152
REMARK 3 S31: 0.2014 S32: 0.3172 S33: 0.0552
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 : WITH TLS ADDED
REMARK 4
REMARK 4 7B4Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-DEC-20.
REMARK 100 THE DEPOSITION ID IS D_1292112466.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97629
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS, XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 100631
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.610
REMARK 200 RESOLUTION RANGE LOW (A) : 83.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.50
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.61
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.70
REMARK 200 R MERGE FOR SHELL (I) : 2.26000
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: PHASER
REMARK 200 STARTING MODEL: 1LZK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LITHIUM CHLORIDE, 0.1M SODIUM
REMARK 280 ACETATE, 20% (W/V) PEG 6000, PH 5.0, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 63.38600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 54.94150
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 54.94150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 95.07900
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 54.94150
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 54.94150
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 31.69300
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 54.94150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.94150
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 95.07900
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 54.94150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.94150
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 31.69300
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 63.38600
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 13.0 KCAL/MOL
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 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 B 740 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 LYS A 315
REMARK 465 VAL A 316
REMARK 465 VAL A 317
REMARK 465 GLU A 318
REMARK 465 ARG A 319
REMARK 465 LYS A 320
REMARK 465 LYS B 315
REMARK 465 VAL B 316
REMARK 465 VAL B 317
REMARK 465 GLU B 318
REMARK 465 ARG B 319
REMARK 465 LYS B 320
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 DISTANCE
REMARK 500 O HOH A 576 O HOH A 761 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 760 O HOH B 760 7555 2.11
REMARK 500 O HOH B 639 O HOH B 753 8665 2.12
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 63 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 GLY A 175 C - N - CA ANGL. DEV. = 14.6 DEGREES
REMARK 500 GLY B 175 C - N - CA ANGL. DEV. = 13.4 DEGREES
REMARK 500 ARG B 298 CG - CD - NE ANGL. DEV. = 13.5 DEGREES
REMARK 500 HIS B 309 CB - CA - C ANGL. DEV. = 13.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 TYR A 87 -1.41 77.22
REMARK 500 SER A 157 -118.84 62.62
REMARK 500 SER A 157 -118.96 62.74
REMARK 500 TYR A 185 62.91 34.49
REMARK 500 ILE A 205 -54.80 75.75
REMARK 500 ASP A 227 49.58 -92.71
REMARK 500 TYR A 245 128.76 -37.33
REMARK 500 ASN B 59 71.64 -169.81
REMARK 500 TYR B 87 -1.91 78.27
REMARK 500 SER B 157 -118.72 62.93
REMARK 500 SER B 157 -119.83 65.74
REMARK 500 TYR B 185 63.30 32.40
REMARK 500 ILE B 205 -58.45 79.42
REMARK 500 ASP B 227 33.90 -86.43
REMARK 500 TYR B 245 130.15 -39.67
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 63 0.08 SIDE CHAIN
REMARK 500 TYR A 303 0.07 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 MG A 404 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 532 O
REMARK 620 2 HOH A 574 O 84.4
REMARK 620 3 HOH A 576 O 108.0 91.4
REMARK 620 4 HOH A 617 O 91.3 91.0 160.8
REMARK 620 5 HOH A 761 O 171.8 91.5 65.0 95.9
REMARK 620 6 HOH A 806 O 88.2 171.7 94.5 85.4 96.3
REMARK 620 N 1 2 3 4 5
DBREF1 7B4Q A 1 320 UNP A0A2K9UV39_9BACI
DBREF2 7B4Q A A0A2K9UV39 1 320
DBREF1 7B4Q B 1 320 UNP A0A2K9UV39_9BACI
DBREF2 7B4Q B A0A2K9UV39 1 320
SEQRES 1 A 320 MET LYS ASN ARG ILE ASP PRO GLU LEU ARG ALA MET LEU
SEQRES 2 A 320 ASP MET PHE PRO PRO LEU ASN LEU ASP ASP VAL GLN ALA
SEQRES 3 A 320 THR ARG LYS ALA MET GLU GLU ALA ALA GLN LEU THR GLU
SEQRES 4 A 320 LEU PRO VAL ASP GLU GLU VAL VAL VAL SER ASN ARG MET
SEQRES 5 A 320 VAL PRO GLY PRO GLU ASP ASN PRO TYR VAL ARG VAL ARG
SEQRES 6 A 320 ILE TYR GLU PRO LYS GLU LYS ILE GLU LYS LEU PRO GLY
SEQRES 7 A 320 LEU LEU TRP ILE HIS GLY GLY GLY TYR VAL LEU GLY ALA
SEQRES 8 A 320 PRO GLU GLY ASP ASP LEU LEU CYS GLN ARG PHE VAL LYS
SEQRES 9 A 320 GLU ALA ASN CYS VAL VAL VAL SER VAL ASP TYR ARG LEU
SEQRES 10 A 320 ALA PRO GLU HIS PRO TYR PRO ALA PRO LEU GLU ASP CYS
SEQRES 11 A 320 TYR ALA ALA LEU GLN TRP PHE ALA LYS LYS VAL ASP GLU
SEQRES 12 A 320 LEU GLY VAL ASP ALA SER ARG ILE GLY VAL GLY GLY GLN
SEQRES 13 A 320 SER ALA GLY GLY GLY LEU THR ALA ALA LEU ALA LEU LEU
SEQRES 14 A 320 ALA ARG ASP ARG LYS GLY PRO GLU LEU CYS PHE GLN MET
SEQRES 15 A 320 PRO LEU TYR PRO MET ILE ASP ASP LYS ASN ASN SER PRO
SEQRES 16 A 320 SER SER LEU GLU ILE THR GLY ASN LEU ILE TRP ASN HIS
SEQRES 17 A 320 ASP LEU ASN GLU LYS GLY TRP SER MET TYR LEU ASP GLY
SEQRES 18 A 320 LYS ASN GLY THR ASP ASP VAL PRO VAL HIS ALA ALA PRO
SEQRES 19 A 320 ALA ARG ALA THR ASP LEU THR ASN LEU PRO TYR THR TYR
SEQRES 20 A 320 THR CYS VAL GLY GLN LEU ASP PRO PHE ARG ASP GLU THR
SEQRES 21 A 320 LEU ASP TYR VAL LYS ARG LEU CYS GLN ALA GLY VAL ASP
SEQRES 22 A 320 VAL GLU PHE HIS LEU TYR PRO GLY ALA TYR HIS GLY PHE
SEQRES 23 A 320 GLU THR LEU ASN PRO ALA ALA ALA VAL SER GLN ARG ALA
SEQRES 24 A 320 LEU ALA GLU TYR VAL GLY ALA VAL LYS HIS VAL LEU ASN
SEQRES 25 A 320 ARG GLU LYS VAL VAL GLU ARG LYS
SEQRES 1 B 320 MET LYS ASN ARG ILE ASP PRO GLU LEU ARG ALA MET LEU
SEQRES 2 B 320 ASP MET PHE PRO PRO LEU ASN LEU ASP ASP VAL GLN ALA
SEQRES 3 B 320 THR ARG LYS ALA MET GLU GLU ALA ALA GLN LEU THR GLU
SEQRES 4 B 320 LEU PRO VAL ASP GLU GLU VAL VAL VAL SER ASN ARG MET
SEQRES 5 B 320 VAL PRO GLY PRO GLU ASP ASN PRO TYR VAL ARG VAL ARG
SEQRES 6 B 320 ILE TYR GLU PRO LYS GLU LYS ILE GLU LYS LEU PRO GLY
SEQRES 7 B 320 LEU LEU TRP ILE HIS GLY GLY GLY TYR VAL LEU GLY ALA
SEQRES 8 B 320 PRO GLU GLY ASP ASP LEU LEU CYS GLN ARG PHE VAL LYS
SEQRES 9 B 320 GLU ALA ASN CYS VAL VAL VAL SER VAL ASP TYR ARG LEU
SEQRES 10 B 320 ALA PRO GLU HIS PRO TYR PRO ALA PRO LEU GLU ASP CYS
SEQRES 11 B 320 TYR ALA ALA LEU GLN TRP PHE ALA LYS LYS VAL ASP GLU
SEQRES 12 B 320 LEU GLY VAL ASP ALA SER ARG ILE GLY VAL GLY GLY GLN
SEQRES 13 B 320 SER ALA GLY GLY GLY LEU THR ALA ALA LEU ALA LEU LEU
SEQRES 14 B 320 ALA ARG ASP ARG LYS GLY PRO GLU LEU CYS PHE GLN MET
SEQRES 15 B 320 PRO LEU TYR PRO MET ILE ASP ASP LYS ASN ASN SER PRO
SEQRES 16 B 320 SER SER LEU GLU ILE THR GLY ASN LEU ILE TRP ASN HIS
SEQRES 17 B 320 ASP LEU ASN GLU LYS GLY TRP SER MET TYR LEU ASP GLY
SEQRES 18 B 320 LYS ASN GLY THR ASP ASP VAL PRO VAL HIS ALA ALA PRO
SEQRES 19 B 320 ALA ARG ALA THR ASP LEU THR ASN LEU PRO TYR THR TYR
SEQRES 20 B 320 THR CYS VAL GLY GLN LEU ASP PRO PHE ARG ASP GLU THR
SEQRES 21 B 320 LEU ASP TYR VAL LYS ARG LEU CYS GLN ALA GLY VAL ASP
SEQRES 22 B 320 VAL GLU PHE HIS LEU TYR PRO GLY ALA TYR HIS GLY PHE
SEQRES 23 B 320 GLU THR LEU ASN PRO ALA ALA ALA VAL SER GLN ARG ALA
SEQRES 24 B 320 LEU ALA GLU TYR VAL GLY ALA VAL LYS HIS VAL LEU ASN
SEQRES 25 B 320 ARG GLU LYS VAL VAL GLU ARG LYS
HET EDO A 401 4
HET GOL A 402 6
HET PEG A 403 7
HET MG A 404 1
HET EDO B 401 4
HET EDO B 402 4
HET EDO B 403 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM MG MAGNESIUM ION
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 EDO 4(C2 H6 O2)
FORMUL 4 GOL C3 H8 O3
FORMUL 5 PEG C4 H10 O3
FORMUL 6 MG MG 2+
FORMUL 10 HOH *584(H2 O)
HELIX 1 AA1 MET A 1 ILE A 5 5 5
HELIX 2 AA2 ASP A 6 GLU A 8 5 3
HELIX 3 AA3 LEU A 9 MET A 15 1 7
HELIX 4 AA4 ASP A 23 THR A 38 1 16
HELIX 5 AA5 ALA A 91 GLY A 94 5 4
HELIX 6 AA6 ASP A 95 ASN A 107 1 13
HELIX 7 AA7 PRO A 124 LYS A 140 1 17
HELIX 8 AA8 LYS A 140 GLY A 145 1 6
HELIX 9 AA9 SER A 157 ARG A 173 1 17
HELIX 10 AB1 SER A 194 ILE A 200 1 7
HELIX 11 AB2 ASN A 207 LEU A 219 1 13
HELIX 12 AB3 ALA A 233 ALA A 237 5 5
HELIX 13 AB4 PHE A 256 ALA A 270 1 15
HELIX 14 AB5 GLY A 285 ASN A 290 1 6
HELIX 15 AB6 ALA A 293 ARG A 313 1 21
HELIX 16 AB7 MET B 1 ILE B 5 5 5
HELIX 17 AB8 ASP B 6 GLU B 8 5 3
HELIX 18 AB9 LEU B 9 PHE B 16 1 8
HELIX 19 AC1 ASP B 23 LEU B 37 1 15
HELIX 20 AC2 ALA B 91 GLY B 94 5 4
HELIX 21 AC3 ASP B 95 ASN B 107 1 13
HELIX 22 AC4 PRO B 124 LYS B 140 1 17
HELIX 23 AC5 LYS B 140 GLY B 145 1 6
HELIX 24 AC6 SER B 157 ARG B 173 1 17
HELIX 25 AC7 SER B 194 ILE B 200 1 7
HELIX 26 AC8 ASN B 207 LEU B 219 1 13
HELIX 27 AC9 ALA B 233 ALA B 237 5 5
HELIX 28 AD1 PHE B 256 ALA B 270 1 15
HELIX 29 AD2 GLY B 285 ASN B 290 1 6
HELIX 30 AD3 ALA B 293 ARG B 313 1 21
SHEET 1 AA1 6 VAL A 46 VAL A 53 0
SHEET 2 AA1 6 VAL A 62 PRO A 69 -1 O ILE A 66 N SER A 49
SHEET 3 AA1 6 VAL A 109 ASP A 114 -1 O SER A 112 N ARG A 65
SHEET 4 AA1 6 LEU A 76 ILE A 82 1 N TRP A 81 O VAL A 111
SHEET 5 AA1 6 VAL A 146 GLN A 156 1 O GLY A 152 N LEU A 80
SHEET 6 AA1 6 PHE A 180 LEU A 184 1 O MET A 182 N VAL A 153
SHEET 1 AA2 4 THR A 246 GLY A 251 0
SHEET 2 AA2 4 VAL A 274 TYR A 279 1 O TYR A 279 N VAL A 250
SHEET 3 AA2 4 VAL B 274 TYR B 279 -1 O LEU B 278 N PHE A 276
SHEET 4 AA2 4 THR B 246 GLY B 251 1 N THR B 246 O GLU B 275
SHEET 1 AA3 6 VAL B 46 PRO B 54 0
SHEET 2 AA3 6 TYR B 61 PRO B 69 -1 O ILE B 66 N SER B 49
SHEET 3 AA3 6 VAL B 109 ASP B 114 -1 O SER B 112 N ARG B 65
SHEET 4 AA3 6 LEU B 76 ILE B 82 1 N TRP B 81 O VAL B 111
SHEET 5 AA3 6 VAL B 146 GLN B 156 1 O GLY B 152 N LEU B 80
SHEET 6 AA3 6 PHE B 180 LEU B 184 1 O MET B 182 N VAL B 153
LINK MG MG A 404 O HOH A 532 1555 1555 2.14
LINK MG MG A 404 O HOH A 574 1555 1555 2.09
LINK MG MG A 404 O HOH A 576 1555 3554 2.11
LINK MG MG A 404 O HOH A 617 1555 1555 2.06
LINK MG MG A 404 O HOH A 761 1555 3554 1.92
LINK MG MG A 404 O HOH A 806 1555 3554 2.04
CISPEP 1 ALA A 118 PRO A 119 0 2.03
CISPEP 2 TYR A 123 PRO A 124 0 5.37
CISPEP 3 ALA B 118 PRO B 119 0 -0.44
CISPEP 4 TYR B 123 PRO B 124 0 5.41
CRYST1 109.883 109.883 126.772 90.00 90.00 90.00 P 43 21 2 16
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 0.009101 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009101 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007888 0.00000
TER 2497 GLU A 314
TER 4992 GLU B 314
MASTER 439 0 7 30 16 0 0 6 5500 2 33 50
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