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HEADER HYDROLASE 04-JAN-16 5HC0
TITLE STRUCTURE OF ESTERASE EST22 WITH P-NITROPHENOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPOLYTIC ENZYME;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ESTERASE, EST22, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LI,J.HUANG
REVDAT 1 18-JAN-17 5HC0 0
JRNL AUTH J.HUANG,Y.Y.HUO,R.JI,S.KUANG,C.JI,X.W.XU,J.LI
JRNL TITL STRUCTURAL INSIGHTS OF A HORMONE SENSITIVE LIPASE HOMOLOGUE
JRNL TITL 2 EST22.
JRNL REF SCI REP V. 6 28550 2016
JRNL REFN ESSN 2045-2322
JRNL PMID 27328716
JRNL DOI 10.1038/SREP28550
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 3 NUMBER OF REFLECTIONS : 62736
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) : 0.133
REMARK 3 R VALUE (WORKING SET) : 0.132
REMARK 3 FREE R VALUE : 0.158
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3321
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3215
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 63.29
REMARK 3 BIN R VALUE (WORKING SET) : 0.2000
REMARK 3 BIN FREE R VALUE SET COUNT : 164
REMARK 3 BIN FREE R VALUE : 0.2500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2534
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 483
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.11000
REMARK 3 B22 (A**2) : 0.22000
REMARK 3 B33 (A**2) : -0.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.06000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.048
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.052
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.030
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.761
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.977
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.967
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2685 ; 0.027 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2486 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3647 ; 2.393 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5751 ; 1.214 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 354 ; 6.319 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 114 ;35.248 ;24.561
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 417 ;11.488 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;15.329 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 396 ; 0.152 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3115 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 581 ; 0.003 ; 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): 1384 ; 1.589 ; 1.313
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1382 ; 1.568 ; 1.310
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1736 ; 2.145 ; 1.963
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1737 ; 2.145 ; 1.964
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1301 ; 3.088 ; 1.586
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1300 ; 3.073 ; 1.581
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1907 ; 4.525 ; 2.272
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3657 ; 8.446 ;13.945
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3658 ; 8.445 ;13.952
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 5HC0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000216807.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72570
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: 5HC4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, PH 5.5, 0.2M CA(AC)2, 20%
REMARK 280 PEG 8000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 60.91150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.61000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 60.91150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 28.61000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -7.08608
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 54.11604
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 A 920 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 MET A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 ASN A 3
REMARK 465 ASP A 23
REMARK 465 LEU A 24
REMARK 465 GLY A 25
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 596 O HOH A 815 1.23
REMARK 500 O CYS A 286 O HOH A 501 1.27
REMARK 500 O HOH A 633 O HOH A 798 1.37
REMARK 500 C CYS A 286 O HOH A 501 1.44
REMARK 500 O HOH A 576 O HOH A 729 1.46
REMARK 500 OD1 ASP A 74 O HOH A 502 1.53
REMARK 500 O HOH A 646 O HOH A 752 1.56
REMARK 500 C3 GOL A 405 O HOH A 753 1.67
REMARK 500 O HOH A 617 O HOH A 624 1.80
REMARK 500 O HOH A 630 O HOH A 835 1.80
REMARK 500 O HOH A 808 O HOH A 815 1.82
REMARK 500 CD1 LEU A 299 O HOH A 866 1.87
REMARK 500 O HOH A 634 O HOH A 812 1.90
REMARK 500 O HOH A 904 O HOH A 971 1.91
REMARK 500 O HOH A 555 O HOH A 580 1.94
REMARK 500 O HOH A 520 O HOH A 728 1.97
REMARK 500 CG LEU A 299 O HOH A 866 1.98
REMARK 500 O3 NPO A 402 O HOH A 503 1.99
REMARK 500 NE2 GLN A 203 O HOH A 504 2.02
REMARK 500 CD ARG A 121 O HOH A 513 2.03
REMARK 500 O HOH A 578 O HOH A 938 2.03
REMARK 500 O HOH A 505 O HOH A 523 2.04
REMARK 500 O1 GOL A 403 O HOH A 505 2.06
REMARK 500 O HOH A 617 O HOH A 969 2.06
REMARK 500 O HOH A 651 O HOH A 869 2.06
REMARK 500 O HOH A 513 O HOH A 857 2.07
REMARK 500 OG SER A 129 O HOH A 506 2.08
REMARK 500 N ASP A 287 O HOH A 501 2.09
REMARK 500 O HOH A 638 O HOH A 897 2.10
REMARK 500 O HOH A 769 O HOH A 905 2.13
REMARK 500 CD2 LEU A 299 O HOH A 866 2.13
REMARK 500 O HOH A 578 O HOH A 732 2.13
REMARK 500 O HOH A 729 O HOH A 955 2.14
REMARK 500 OD1 ASP A 208 O HOH A 507 2.14
REMARK 500 O HOH A 798 O HOH A 864 2.15
REMARK 500 O HOH A 516 O HOH A 851 2.17
REMARK 500 O HOH A 728 O HOH A 885 2.18
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 511 O HOH A 682 4546 1.25
REMARK 500 OG1 THR A 96 OE2 GLU A 227 1565 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLY A 28 N GLY A 28 CA -0.115
REMARK 500 GLU A 34 CD GLU A 34 OE1 0.070
REMARK 500 CYS A 59 CB CYS A 59 SG -0.145
REMARK 500 TYR A 116 CZ TYR A 116 CE2 -0.080
REMARK 500 TYR A 117 CE1 TYR A 117 CZ -0.083
REMARK 500 GLU A 254 CG GLU A 254 CD 0.112
REMARK 500 GLU A 254 CD GLU A 254 OE1 0.088
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 14 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG A 49 NE - CZ - NH2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP A 74 CB - CG - OD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 74 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 173 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP A 241 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 GLU A 254 CG - CD - OE1 ANGL. DEV. = 12.3 DEGREES
REMARK 500 ASP A 287 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 290 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 PHE A 296 CB - CG - CD2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 302 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ILE A 324 CG1 - CB - CG2 ANGL. DEV. = 14.1 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 LEU A 113 175.83 82.59
REMARK 500 LEU A 143 -53.14 -133.66
REMARK 500 SER A 146 -153.40 -80.93
REMARK 500 SER A 188 -120.51 65.11
REMARK 500 CYS A 217 55.56 29.94
REMARK 500 LEU A 239 -57.81 74.86
REMARK 500 CYS A 286 47.59 -102.98
REMARK 500 PHE A 322 69.61 -116.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 CYS A 286 10.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 982 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH A 983 DISTANCE = 6.26 ANGSTROMS
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO A 407
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5HC2 RELATED DB: PDB
REMARK 900 RELATED ID: 5HC3 RELATED DB: PDB
REMARK 900 RELATED ID: 5HC4 RELATED DB: PDB
REMARK 900 RELATED ID: 5HC5 RELATED DB: PDB
DBREF 5HC0 A 1 344 UNP H6BDX1 H6BDX1_9BACT 1 344
SEQADV 5HC0 MET A -20 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC0 GLY A -19 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC0 SER A -18 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC0 SER A -17 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC0 HIS A -16 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC0 HIS A -15 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC0 HIS A -14 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC0 HIS A -13 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC0 HIS A -12 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC0 HIS A -11 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC0 HIS A -10 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC0 SER A -9 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC0 SER A -8 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC0 GLY A -7 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC0 LEU A -6 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC0 VAL A -5 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC0 PRO A -4 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC0 ARG A -3 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC0 GLY A -2 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC0 SER A -1 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC0 HIS A 0 UNP H6BDX1 EXPRESSION TAG
SEQRES 1 A 365 MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS SER SER
SEQRES 2 A 365 GLY LEU VAL PRO ARG GLY SER HIS MET THR ASN LYS ILE
SEQRES 3 A 365 ALA GLU ASP PRO ARG ILE ASP PRO ARG ILE LYS ALA ILE
SEQRES 4 A 365 PHE SER GLY MET ASP LEU GLY GLY GLY GLY ASP VAL GLU
SEQRES 5 A 365 SER ARG GLU ALA MET LEU GLU ALA ALA SER SER GLU GLU
SEQRES 6 A 365 ALA THR ALA VAL ARG ASP GLY LEU ARG VAL PHE LEU ASP
SEQRES 7 A 365 ALA CYS ASP ASN GLU GLU ILE ALA PRO SER ALA GLY LEU
SEQRES 8 A 365 LYS ILE GLU ASP TYR GLU PHE THR SER GLU PRO ASP GLY
SEQRES 9 A 365 ASN ILE ALA LYS ILE GLN TYR ILE ARG PRO ASP SER THR
SEQRES 10 A 365 ASP LYS LEU PRO CYS VAL TYR TYR ILE HIS GLY GLY GLY
SEQRES 11 A 365 MET GLN SER LEU SER CYS TYR TYR GLY ASN TYR ARG ALA
SEQRES 12 A 365 TRP GLY LYS ILE ILE ALA SER ASN GLY VAL ALA VAL ALA
SEQRES 13 A 365 MET VAL GLU PHE ARG ASN ALA LEU VAL PRO SER ALA LEU
SEQRES 14 A 365 PRO GLU VAL ALA PRO TYR PRO ALA GLY LEU ASN ASP CYS
SEQRES 15 A 365 VAL SER GLY VAL LYS TRP VAL ALA SER HIS ALA ASP GLU
SEQRES 16 A 365 LEU GLY ILE ASP ALA SER ARG ILE ILE ILE ALA GLY GLU
SEQRES 17 A 365 SER GLY GLY GLY ASN LEU THR LEU ALA ALA GLY LEU ARG
SEQRES 18 A 365 LEU LYS GLN GLU GLY SER GLN ASP LEU ILE GLN GLY LEU
SEQRES 19 A 365 TYR ALA LEU CYS PRO TYR ILE ALA GLY SER TRP PRO SER
SEQRES 20 A 365 GLU ASP SER PRO SER SER THR GLU ASN ASN GLY ILE LEU
SEQRES 21 A 365 LEU ASP LEU HIS ASN ASN GLN GLY ALA MET GLY TYR GLY
SEQRES 22 A 365 ILE GLU ALA TYR GLU MET ARG ASP PRO LEU ALA TRP PRO
SEQRES 23 A 365 GLY PHE ALA THR GLU GLU ASP VAL SER GLY LEU VAL PRO
SEQRES 24 A 365 THR PHE ILE SER VAL ASN GLU CYS ASP PRO LEU ARG ASP
SEQRES 25 A 365 GLU GLY ILE ASN PHE TYR ARG LEU LEU LEU ARG ALA GLY
SEQRES 26 A 365 VAL SER ALA LYS CYS ARG GLN VAL MET GLY THR ILE HIS
SEQRES 27 A 365 GLY THR GLU ILE PHE PRO ILE ALA CYS PRO ASP VAL SER
SEQRES 28 A 365 ARG ASP THR ALA ALA SER ILE ALA ASN PHE CYS LYS GLY
SEQRES 29 A 365 GLY
HET GOL A 401 6
HET NPO A 402 10
HET GOL A 403 6
HET GOL A 404 6
HET GOL A 405 6
HET ACY A 406 4
HET NPO A 407 10
HETNAM GOL GLYCEROL
HETNAM NPO P-NITROPHENOL
HETNAM ACY ACETIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 4(C3 H8 O3)
FORMUL 3 NPO 2(C6 H5 N O3)
FORMUL 7 ACY C2 H4 O2
FORMUL 9 HOH *483(H2 O)
HELIX 1 AA1 ASP A 12 SER A 20 1 9
HELIX 2 AA2 SER A 32 SER A 41 1 10
HELIX 3 AA3 SER A 42 ALA A 58 1 17
HELIX 4 AA4 TYR A 117 SER A 129 1 13
HELIX 5 AA5 PRO A 155 HIS A 171 1 17
HELIX 6 AA6 HIS A 171 GLY A 176 1 6
HELIX 7 AA7 SER A 188 GLY A 205 1 18
HELIX 8 AA8 SER A 206 ILE A 210 5 5
HELIX 9 AA9 SER A 229 ASN A 235 1 7
HELIX 10 AB1 ASN A 245 MET A 258 1 14
HELIX 11 AB2 TRP A 264 ALA A 268 5 5
HELIX 12 AB3 THR A 269 SER A 274 1 6
HELIX 13 AB4 LEU A 289 ALA A 303 1 15
HELIX 14 AB5 GLY A 318 PHE A 322 5 5
HELIX 15 AB6 CYS A 326 GLY A 343 1 18
SHEET 1 AA1 8 LEU A 70 THR A 78 0
SHEET 2 AA1 8 ILE A 85 PRO A 93 -1 O TYR A 90 N GLU A 73
SHEET 3 AA1 8 ALA A 133 GLU A 138 -1 O GLU A 138 N LYS A 87
SHEET 4 AA1 8 LEU A 99 ILE A 105 1 N VAL A 102 O ALA A 133
SHEET 5 AA1 8 ILE A 177 GLU A 187 1 O ILE A 183 N TYR A 103
SHEET 6 AA1 8 GLY A 212 LEU A 216 1 O LEU A 216 N GLY A 186
SHEET 7 AA1 8 THR A 279 CYS A 286 1 O PHE A 280 N LEU A 213
SHEET 8 AA1 8 ALA A 307 ILE A 316 1 O THR A 315 N CYS A 286
CISPEP 1 GLU A 80 PRO A 81 0 14.05
CISPEP 2 TYR A 154 PRO A 155 0 0.51
CISPEP 3 TRP A 224 PRO A 225 0 -5.34
SITE 1 AC1 9 GLU A 80 ASN A 159 VAL A 162 SER A 163
SITE 2 AC1 9 LYS A 166 ARG A 200 GLU A 204 HOH A 607
SITE 3 AC1 9 HOH A 741
SITE 1 AC2 4 ILE A 18 VAL A 54 PHE A 55 HOH A 503
SITE 1 AC3 12 ILE A 183 GLN A 211 PRO A 278 PHE A 340
SITE 2 AC3 12 HOH A 505 HOH A 512 HOH A 523 HOH A 593
SITE 3 AC3 12 HOH A 650 HOH A 723 HOH A 733 HOH A 765
SITE 1 AC4 9 TYR A 219 TRP A 224 LEU A 242 ASN A 244
SITE 2 AC4 9 GLN A 246 GLY A 247 ACY A 406 HOH A 517
SITE 3 AC4 9 HOH A 718
SITE 1 AC5 12 LYS A 166 GLU A 204 SER A 206 TYR A 256
SITE 2 AC5 12 GLU A 257 ARG A 259 HOH A 511 HOH A 519
SITE 3 AC5 12 HOH A 682 HOH A 726 HOH A 753 HOH A 797
SITE 1 AC6 7 GLY A 108 GLY A 109 SER A 188 GOL A 404
SITE 2 AC6 7 HOH A 509 HOH A 528 HOH A 901
SITE 1 AC7 9 LEU A 113 TYR A 120 GLU A 187 SER A 188
SITE 2 AC7 9 HIS A 317 ILE A 321 HOH A 509 HOH A 515
SITE 3 AC7 9 HOH A 575
CRYST1 121.823 57.220 54.578 90.00 97.46 90.00 C 1 2 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 0.008209 0.000000 0.001074 0.00000
SCALE2 0.000000 0.017476 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018479 0.00000
TER 2582 GLY A 344
MASTER 489 0 7 15 8 0 18 6 3065 1 48 29
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