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HEADER HYDROLASE 12-MAY-15 4ZRS
TITLE CRYSTAL STRUCTURE OF A CLONED FERULOYL ESTERASE FROM A SOIL
TITLE 2 METAGENOMIC LIBRARY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: FERULOYL ESTERASE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A(+)
KEYWDS FERULOYL ESTERASE, METAGENOMIC LIBRARY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.XIE,R.CHEN,L.CAO,Y.LIU
REVDAT 1 03-FEB-16 4ZRS 0
JRNL AUTH L.C.CAO,R.CHEN,W.XIE,Y.H.LIU
JRNL TITL ENHANCING THE THERMOSTABILITY OF FERULOYL ESTERASE ESTF27 BY
JRNL TITL 2 DIRECTED EVOLUTION AND THE UNDERLYING STRUCTURAL BASIS
JRNL REF J.AGRIC.FOOD CHEM. V. 63 8225 2015
JRNL REFN ESSN 1520-5118
JRNL PMID 26329893
JRNL DOI 10.1021/ACS.JAFC.5B03424
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.35
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 43584
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) : 0.152
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2322
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3209
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.2220
REMARK 3 BIN FREE R VALUE SET COUNT : 184
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4438
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 615
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.28000
REMARK 3 B22 (A**2) : 0.03000
REMARK 3 B33 (A**2) : -0.36000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.20000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.142
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.138
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.097
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 : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4563 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4261 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6201 ; 1.740 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9781 ; 2.424 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 582 ; 6.151 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 199 ;33.681 ;23.266
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 678 ;14.474 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;19.814 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 672 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5246 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1072 ; 0.011 ; 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): 2334 ; 1.545 ; 1.648
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2333 ; 1.544 ; 1.647
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2914 ; 2.284 ; 2.459
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2915 ; 2.283 ; 2.460
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2229 ; 2.689 ; 1.916
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2229 ; 2.689 ; 1.916
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3288 ; 4.101 ; 2.758
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5826 ; 6.471 ;15.307
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5826 ; 6.471 ;15.307
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
REMARK 4
REMARK 4 4ZRS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000209594.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : OTHER
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54056
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : OXFORD ONYX CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSALISPRO
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45906
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 65.350
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.43500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.000
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: 4NSP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M AMMONIUM SULFATE, 100 MM HEPES,
REMARK 280 PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 50.89500
REMARK 290 SMTRY3 2 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: DIMERIC
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 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 -15
REMARK 465 GLY A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 GLU A -7
REMARK 465 ASN A -6
REMARK 465 LEU A -5
REMARK 465 TYR A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
REMARK 465 MET B -15
REMARK 465 GLY B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 GLU B -7
REMARK 465 ASN B -6
REMARK 465 LEU B -5
REMARK 465 TYR B -4
REMARK 465 PHE B -3
REMARK 465 GLN B -2
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 HIS A 0 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 19 CG CD OE1 OE2
REMARK 470 HIS B 0 CG ND1 CD2 CE1 NE2
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 458 O HOH A 621 1.24
REMARK 500 O HOH A 441 O HOH A 637 1.49
REMARK 500 O HOH B 407 O HOH B 660 1.60
REMARK 500 O HOH A 594 O HOH A 680 1.73
REMARK 500 O HOH B 681 O HOH B 697 1.75
REMARK 500 O HIS B 0 O HOH B 401 1.80
REMARK 500 O LEU B 16 O HOH B 402 1.80
REMARK 500 O HOH B 418 O HOH B 581 1.86
REMARK 500 NE ARG A 129 O HOH A 401 1.87
REMARK 500 O HOH A 682 O HOH A 711 1.87
REMARK 500 O HOH A 527 O HOH A 600 1.89
REMARK 500 OD1 SEB B 151 O HOH B 403 1.92
REMARK 500 OE1 GLU B 40 O HOH B 404 1.93
REMARK 500 O HOH B 599 O HOH B 684 1.95
REMARK 500 OD1 SEB A 151 O HOH A 402 1.96
REMARK 500 O HOH A 602 O HOH A 679 1.97
REMARK 500 O HOH A 498 O HOH A 602 1.98
REMARK 500 O HOH A 527 O HOH A 673 1.99
REMARK 500 O ALA A 85 O HOH A 403 2.02
REMARK 500 O HOH A 612 O HOH A 650 2.03
REMARK 500 ND2 ASN A 217 O HOH A 404 2.03
REMARK 500 O HOH B 578 O HOH B 621 2.03
REMARK 500 O HOH A 402 O HOH A 603 2.04
REMARK 500 N LEU B 16 O HOH B 405 2.04
REMARK 500 CB LEU B 16 O HOH B 673 2.05
REMARK 500 O HOH A 701 O HOH A 708 2.07
REMARK 500 O HOH B 491 O HOH B 520 2.08
REMARK 500 O HOH A 687 O HOH A 688 2.08
REMARK 500 O HOH B 681 O HOH B 692 2.10
REMARK 500 O HOH B 601 O HOH B 620 2.13
REMARK 500 O HOH A 479 O HOH A 485 2.13
REMARK 500 O HOH A 600 O HOH A 673 2.13
REMARK 500 O HOH A 584 O HOH A 684 2.15
REMARK 500 O HOH A 657 O HOH A 667 2.17
REMARK 500 O HOH B 437 O HOH B 559 2.17
REMARK 500 O HOH B 416 O HOH B 498 2.18
REMARK 500 O HOH B 584 O HOH B 651 2.18
REMARK 500 O HOH A 628 O HOH A 642 2.19
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 A 688 O HOH B 675 2646 1.64
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 B 14 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 54 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 54 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG B 59 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG B 129 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG B 129 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 CYS B 243 CA - CB - SG ANGL. DEV. = 9.9 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 PHE A 77 -12.34 75.13
REMARK 500 PRO A 118 32.70 -95.71
REMARK 500 SEB A 151 -118.55 49.94
REMARK 500 ASN A 262 -159.78 -117.47
REMARK 500 PHE B 77 -11.68 72.68
REMARK 500 PRO B 118 39.52 -98.51
REMARK 500 SEB B 151 -119.87 54.58
REMARK 500 LYS B 164 -38.15 -137.78
REMARK 500 ASN B 262 -158.17 -115.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 301
DBREF 4ZRS A 1 290 UNP E7DJY5 E7DJY5_9BACT 1 290
DBREF 4ZRS B 1 290 UNP E7DJY5 E7DJY5_9BACT 1 290
SEQADV 4ZRS MET A -15 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS GLY A -14 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS HIS A -13 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS HIS A -12 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS HIS A -11 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS HIS A -10 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS HIS A -9 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS HIS A -8 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS GLU A -7 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS ASN A -6 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS LEU A -5 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS TYR A -4 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS PHE A -3 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS GLN A -2 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS GLY A -1 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS HIS A 0 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS ILE A 27 UNP E7DJY5 THR 27 ENGINEERED MUTATION
SEQADV 4ZRS LEU A 84 UNP E7DJY5 SER 84 ENGINEERED MUTATION
SEQADV 4ZRS ILE A 161 UNP E7DJY5 VAL 161 ENGINEERED MUTATION
SEQADV 4ZRS LEU A 195 UNP E7DJY5 HIS 195 ENGINEERED MUTATION
SEQADV 4ZRS CYS A 243 UNP E7DJY5 GLY 243 ENGINEERED MUTATION
SEQADV 4ZRS VAL A 259 UNP E7DJY5 ALA 259 ENGINEERED MUTATION
SEQADV 4ZRS MET B -15 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS GLY B -14 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS HIS B -13 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS HIS B -12 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS HIS B -11 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS HIS B -10 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS HIS B -9 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS HIS B -8 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS GLU B -7 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS ASN B -6 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS LEU B -5 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS TYR B -4 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS PHE B -3 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS GLN B -2 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS GLY B -1 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS HIS B 0 UNP E7DJY5 EXPRESSION TAG
SEQADV 4ZRS ILE B 27 UNP E7DJY5 THR 27 ENGINEERED MUTATION
SEQADV 4ZRS LEU B 84 UNP E7DJY5 SER 84 ENGINEERED MUTATION
SEQADV 4ZRS ILE B 161 UNP E7DJY5 VAL 161 ENGINEERED MUTATION
SEQADV 4ZRS LEU B 195 UNP E7DJY5 HIS 195 ENGINEERED MUTATION
SEQADV 4ZRS CYS B 243 UNP E7DJY5 GLY 243 ENGINEERED MUTATION
SEQADV 4ZRS VAL B 259 UNP E7DJY5 ALA 259 ENGINEERED MUTATION
SEQRES 1 A 306 MET GLY HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE
SEQRES 2 A 306 GLN GLY HIS MET THR PRO GLU LEU ARG ALA LYS LEU GLU
SEQRES 3 A 306 SER LEU GLY ARG ASP LEU THR PRO GLU MET LEU GLY GLY
SEQRES 4 A 306 THR THR GLN ILE PHE ALA ALA MET ALA THR GLY SER ASP
SEQRES 5 A 306 PRO GLU VAL GLU VAL THR ARG ASP LEU GLU TYR GLY GLU
SEQRES 6 A 306 ASP PRO ARG HIS ARG LEU ASP LEU PHE ARG LYS ALA ASP
SEQRES 7 A 306 THR ARG ASP ALA PRO VAL LEU VAL PHE VAL HIS GLY GLY
SEQRES 8 A 306 GLY PHE VAL MET GLY ASP LYS ARG LEU ALA GLU THR PRO
SEQRES 9 A 306 PHE TYR ASP ASN ILE GLY VAL PHE ALA ALA GLN GLN GLY
SEQRES 10 A 306 PHE VAL GLY VAL THR ILE THR TYR ARG LEU ALA PRO ALA
SEQRES 11 A 306 HIS GLN PHE PRO SER GLY PRO GLU ASP LEU ALA ALA VAL
SEQRES 12 A 306 VAL ARG TRP LEU LYS ALA ASN VAL ALA GLN TYR GLY GLY
SEQRES 13 A 306 ASP PRO ASP LYS ILE VAL LEU SER GLY GLN SEB ALA GLY
SEQRES 14 A 306 ALA ALA HIS VAL ALA SER TYR ILE ALA HIS LYS ALA HIS
SEQRES 15 A 306 HIS ALA THR GLU GLY GLY GLY ILE ALA GLY ALA ILE LEU
SEQRES 16 A 306 MET SER GLY ILE TYR ASP THR LEU THR ALA THR PRO ASN
SEQRES 17 A 306 GLU PHE LEU ILE ALA TYR TYR GLY ASP ASP PRO LYS GLY
SEQRES 18 A 306 TRP GLY PRO ALA SER SER MET ALA GLY LEU ILE ASN THR
SEQRES 19 A 306 GLU ILE PRO LEU MET LEU THR VAL SER GLU PHE ASP PRO
SEQRES 20 A 306 GLU ASP PHE GLN ARG GLN ALA ALA GLN PHE VAL CYS ALA
SEQRES 21 A 306 TRP GLY MET ALA HIS ALA ALA TYR PRO GLU MET HIS TYR
SEQRES 22 A 306 LEU VAL GLY HIS ASN HIS LEU SER PRO ALA GLN SER ILE
SEQRES 23 A 306 GLY THR GLU ILE LYS ALA ILE GLY ARG MET VAL ALA GLY
SEQRES 24 A 306 PHE VAL ARG ARG VAL THR ARG
SEQRES 1 B 306 MET GLY HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE
SEQRES 2 B 306 GLN GLY HIS MET THR PRO GLU LEU ARG ALA LYS LEU GLU
SEQRES 3 B 306 SER LEU GLY ARG ASP LEU THR PRO GLU MET LEU GLY GLY
SEQRES 4 B 306 THR THR GLN ILE PHE ALA ALA MET ALA THR GLY SER ASP
SEQRES 5 B 306 PRO GLU VAL GLU VAL THR ARG ASP LEU GLU TYR GLY GLU
SEQRES 6 B 306 ASP PRO ARG HIS ARG LEU ASP LEU PHE ARG LYS ALA ASP
SEQRES 7 B 306 THR ARG ASP ALA PRO VAL LEU VAL PHE VAL HIS GLY GLY
SEQRES 8 B 306 GLY PHE VAL MET GLY ASP LYS ARG LEU ALA GLU THR PRO
SEQRES 9 B 306 PHE TYR ASP ASN ILE GLY VAL PHE ALA ALA GLN GLN GLY
SEQRES 10 B 306 PHE VAL GLY VAL THR ILE THR TYR ARG LEU ALA PRO ALA
SEQRES 11 B 306 HIS GLN PHE PRO SER GLY PRO GLU ASP LEU ALA ALA VAL
SEQRES 12 B 306 VAL ARG TRP LEU LYS ALA ASN VAL ALA GLN TYR GLY GLY
SEQRES 13 B 306 ASP PRO ASP LYS ILE VAL LEU SER GLY GLN SEB ALA GLY
SEQRES 14 B 306 ALA ALA HIS VAL ALA SER TYR ILE ALA HIS LYS ALA HIS
SEQRES 15 B 306 HIS ALA THR GLU GLY GLY GLY ILE ALA GLY ALA ILE LEU
SEQRES 16 B 306 MET SER GLY ILE TYR ASP THR LEU THR ALA THR PRO ASN
SEQRES 17 B 306 GLU PHE LEU ILE ALA TYR TYR GLY ASP ASP PRO LYS GLY
SEQRES 18 B 306 TRP GLY PRO ALA SER SER MET ALA GLY LEU ILE ASN THR
SEQRES 19 B 306 GLU ILE PRO LEU MET LEU THR VAL SER GLU PHE ASP PRO
SEQRES 20 B 306 GLU ASP PHE GLN ARG GLN ALA ALA GLN PHE VAL CYS ALA
SEQRES 21 B 306 TRP GLY MET ALA HIS ALA ALA TYR PRO GLU MET HIS TYR
SEQRES 22 B 306 LEU VAL GLY HIS ASN HIS LEU SER PRO ALA GLN SER ILE
SEQRES 23 B 306 GLY THR GLU ILE LYS ALA ILE GLY ARG MET VAL ALA GLY
SEQRES 24 B 306 PHE VAL ARG ARG VAL THR ARG
MODRES 4ZRS SEB A 151 SER MODIFIED RESIDUE
MODRES 4ZRS SEB B 151 SER MODIFIED RESIDUE
HET SEB A 151 16
HET SEB B 151 16
HET GOL A 301 6
HET GOL B 301 6
HETNAM SEB O-BENZYLSULFONYL-SERINE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 SEB 2(C10 H13 N O5 S)
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 HOH *615(H2 O)
HELIX 1 AA1 THR A 2 GLY A 13 1 12
HELIX 2 AA2 THR A 17 ALA A 30 1 14
HELIX 3 AA3 TYR A 90 GLN A 100 1 11
HELIX 4 AA4 PRO A 118 VAL A 135 1 18
HELIX 5 AA5 ALA A 136 TYR A 138 5 3
HELIX 6 AA6 SEB A 151 HIS A 163 1 13
HELIX 7 AA7 LYS A 164 HIS A 167 5 4
HELIX 8 AA8 THR A 169 GLY A 173 5 5
HELIX 9 AA9 ASN A 192 GLY A 200 1 9
HELIX 10 AB1 ASP A 202 SER A 210 5 9
HELIX 11 AB2 SER A 211 THR A 218 1 8
HELIX 12 AB3 PRO A 231 ALA A 250 1 20
HELIX 13 AB4 LEU A 264 SER A 269 1 6
HELIX 14 AB5 LYS A 275 THR A 289 1 15
HELIX 15 AB6 THR B 2 GLY B 13 1 12
HELIX 16 AB7 THR B 17 ALA B 30 1 14
HELIX 17 AB8 TYR B 90 GLN B 100 1 11
HELIX 18 AB9 PRO B 118 VAL B 135 1 18
HELIX 19 AC1 ALA B 136 TYR B 138 5 3
HELIX 20 AC2 SEB B 151 LYS B 164 1 14
HELIX 21 AC3 HIS B 167 GLY B 171 5 5
HELIX 22 AC4 ASN B 192 GLY B 200 1 9
HELIX 23 AC5 ASP B 202 SER B 210 5 9
HELIX 24 AC6 SER B 211 THR B 218 1 8
HELIX 25 AC7 PRO B 231 ALA B 250 1 20
HELIX 26 AC8 LEU B 264 SER B 269 1 6
HELIX 27 AC9 LYS B 275 THR B 289 1 15
SHEET 1 AA1 8 GLU A 40 GLU A 46 0
SHEET 2 AA1 8 ARG A 54 ARG A 59 -1 O ARG A 59 N GLU A 40
SHEET 3 AA1 8 VAL A 103 ILE A 107 -1 O GLY A 104 N PHE A 58
SHEET 4 AA1 8 ALA A 66 VAL A 72 1 N PRO A 67 O VAL A 103
SHEET 5 AA1 8 GLY A 140 GLN A 150 1 O ASP A 141 N ALA A 66
SHEET 6 AA1 8 GLY A 176 MET A 180 1 O MET A 180 N GLY A 149
SHEET 7 AA1 8 LEU A 222 SER A 227 1 O MET A 223 N LEU A 179
SHEET 8 AA1 8 MET A 255 LEU A 258 1 O HIS A 256 N LEU A 224
SHEET 1 AA2 8 GLU B 40 GLU B 46 0
SHEET 2 AA2 8 ARG B 54 ARG B 59 -1 O ARG B 59 N GLU B 40
SHEET 3 AA2 8 VAL B 103 ILE B 107 -1 O GLY B 104 N PHE B 58
SHEET 4 AA2 8 ALA B 66 VAL B 72 1 N PRO B 67 O VAL B 103
SHEET 5 AA2 8 GLY B 140 GLN B 150 1 O VAL B 146 N VAL B 68
SHEET 6 AA2 8 GLY B 176 MET B 180 1 O MET B 180 N GLY B 149
SHEET 7 AA2 8 LEU B 222 SER B 227 1 O MET B 223 N LEU B 179
SHEET 8 AA2 8 MET B 255 LEU B 258 1 O HIS B 256 N LEU B 224
SSBOND 1 CYS A 243 CYS B 243 1555 1555 2.04
LINK C GLN A 150 N SEB A 151 1555 1555 1.32
LINK C SEB A 151 N ALA A 152 1555 1555 1.32
LINK C GLN B 150 N SEB B 151 1555 1555 1.33
LINK C SEB B 151 N ALA B 152 1555 1555 1.34
CISPEP 1 GLY A -1 HIS A 0 0 -12.67
CISPEP 2 PHE A 89 TYR A 90 0 -0.60
CISPEP 3 ALA A 112 PRO A 113 0 2.85
CISPEP 4 PHE A 117 PRO A 118 0 4.93
CISPEP 5 GLY B -1 HIS B 0 0 -1.60
CISPEP 6 PHE B 89 TYR B 90 0 2.42
CISPEP 7 ALA B 112 PRO B 113 0 3.65
CISPEP 8 PHE B 117 PRO B 118 0 6.86
SITE 1 AC1 8 PRO A 221 LEU A 222 TRP A 245 PRO A 253
SITE 2 AC1 8 GLU A 254 HOH A 475 HOH A 528 HOH A 609
SITE 1 AC2 7 PRO B 221 LEU B 222 TRP B 245 GLU B 254
SITE 2 AC2 7 HOH B 480 HOH B 496 HOH B 589
CRYST1 52.156 101.790 69.822 90.00 110.62 90.00 P 1 21 1 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 0.019173 0.000000 0.007215 0.00000
SCALE2 0.000000 0.009824 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015303 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 0.999961 -0.008652 -0.001736 0.19362 1
MTRIX2 2 -0.008653 -0.999963 -0.000424 17.91032 1
MTRIX3 2 -0.001733 0.000439 -0.999998 65.31759 1
TER 2218 ARG A 290
TER 4440 ARG B 290
MASTER 395 0 4 27 16 0 4 12 5065 2 50 48
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