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HEADER HYDROLASE 08-NOV-13 3WL6
TITLE CRYSTAL STRUCTURE OF POPH NATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OXIDIZED POLYVINYL ALCOHOL HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 30-379;
COMPND 5 SYNONYM: OPH, OXIDIZED PVA HYDROLASE, BETA-DIKETONE HYDROLASE;
COMPND 6 EC: 3.7.1.7;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS SP.;
SOURCE 3 ORGANISM_TAXID: 306;
SOURCE 4 STRAIN: VM15C;
SOURCE 5 GENE: PVAB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET32A
KEYWDS ALPHA/BETA-HYDROLASE, OXI-POLYVINYL ALCOHOL HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.YANG,T.P.KO,J.H.LI,L.LIU,C.H.HUANG,H.C.CHAN,F.F.REN,D.X.JIA,A.H.-
AUTHOR 2 J.WANG,R.T.GUO,J.CHEN,G.C.DU
REVDAT 1 24-SEP-14 3WL6 0
JRNL AUTH Y.YANG,T.P.KO,L.LIU,J.LI,C.H.HUANG,H.C.CHAN,F.REN,D.JIA,
JRNL AUTH 2 A.H.-J.WANG,R.T.GUO,J.CHEN,G.DU
JRNL TITL STRUCTURAL INSIGHTS INTO ENZYMATIC DEGRADATION OF OXIDIZED
JRNL TITL 2 POLYVINYL ALCOHOL
JRNL REF CHEMBIOCHEM V. 15 1882 2014
JRNL REFN ISSN 1439-4227
JRNL PMID 25044912
JRNL DOI 10.1002/CBIC.201402166
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.21
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 83750
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.174
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4254
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2090
REMARK 3 BIN FREE R VALUE : 0.2240
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 446
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5002
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 1049
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.82300
REMARK 3 B22 (A**2) : 2.87500
REMARK 3 B33 (A**2) : 4.94800
REMARK 3 B12 (A**2) : 5.13800
REMARK 3 B13 (A**2) : 0.10600
REMARK 3 B23 (A**2) : -1.38100
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.14
REMARK 3 ESD FROM SIGMAA (A) : 0.10
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.17
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.12
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 1.620
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.134 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.685 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.032 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.894 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 41.33
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3WL6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-NOV-13.
REMARK 100 THE RCSB ID CODE IS RCSB096473.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAY-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL13B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
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 : 85743
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 22.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.22000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.500
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: PDB ENTRY 3WL5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRI-SODIUM CITRATE, PH 5.6, 29%
REMARK 280 W/V POLYETHYLENE GLYCOL 4000, 3% W/V N-OCTYL-BETA-D-GLUCOSIDE,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 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 -4
REMARK 465 GLY A -3
REMARK 465 ALA A -2
REMARK 465 GLY A -1
REMARK 465 ALA A 0
REMARK 465 ASP A 1
REMARK 465 ARG A 2
REMARK 465 THR A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 THR A 6
REMARK 465 PRO A 7
REMARK 465 ALA A 8
REMARK 465 ALA A 9
REMARK 465 ALA A 10
REMARK 465 ASN A 11
REMARK 465 PRO A 12
REMARK 465 ALA A 13
REMARK 465 ALA A 14
REMARK 465 THR A 15
REMARK 465 GLU A 16
REMARK 465 PRO A 17
REMARK 465 VAL A 18
REMARK 465 TRP A 352
REMARK 465 SER A 353
REMARK 465 HIS A 354
REMARK 465 PRO A 355
REMARK 465 GLN A 356
REMARK 465 PHE A 357
REMARK 465 GLU A 358
REMARK 465 LYS A 359
REMARK 465 ALA B -4
REMARK 465 GLY B -3
REMARK 465 ALA B -2
REMARK 465 GLY B -1
REMARK 465 ALA B 0
REMARK 465 ASP B 1
REMARK 465 ARG B 2
REMARK 465 THR B 3
REMARK 465 ALA B 4
REMARK 465 ALA B 5
REMARK 465 THR B 6
REMARK 465 PRO B 7
REMARK 465 ALA B 8
REMARK 465 ALA B 9
REMARK 465 ALA B 10
REMARK 465 ASN B 11
REMARK 465 PRO B 12
REMARK 465 ALA B 13
REMARK 465 ALA B 14
REMARK 465 THR B 15
REMARK 465 GLU B 16
REMARK 465 PRO B 17
REMARK 465 VAL B 18
REMARK 465 TRP B 255
REMARK 465 ASN B 256
REMARK 465 CYS B 257
REMARK 465 THR B 258
REMARK 465 ARG B 259
REMARK 465 PRO B 260
REMARK 465 ASP B 261
REMARK 465 GLY B 262
REMARK 465 SER B 263
REMARK 465 ARG B 264
REMARK 465 PHE B 265
REMARK 465 ALA B 351
REMARK 465 TRP B 352
REMARK 465 SER B 353
REMARK 465 HIS B 354
REMARK 465 PRO B 355
REMARK 465 GLN B 356
REMARK 465 PHE B 357
REMARK 465 GLU B 358
REMARK 465 LYS B 359
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 B 734 O HOH B 1030 2.07
REMARK 500 N LEU B 266 O HOH B 1019 2.11
REMARK 500 O HOH B 571 O HOH B 581 2.12
REMARK 500 O HOH A 870 O HOH A 871 2.12
REMARK 500 O HOH A 435 O HOH A 498 2.14
REMARK 500 O HOH A 866 O HOH B 581 2.16
REMARK 500 O HOH A 702 O HOH A 910 2.17
REMARK 500 O HOH A 693 O HOH A 914 2.18
REMARK 500 O HOH B 912 O HOH B 1016 2.18
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 LEU B 168 CA - CB - CG ANGL. DEV. = 14.4 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 ALA A 81 55.44 38.13
REMARK 500 ARG A 107 -100.03 -100.99
REMARK 500 SER A 172 -124.49 61.33
REMARK 500 HIS A 298 78.01 -110.40
REMARK 500 ALA B 81 57.64 36.16
REMARK 500 ARG B 107 -95.97 -99.68
REMARK 500 SER B 172 -119.58 60.58
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 618 DISTANCE = 7.64 ANGSTROMS
REMARK 525 HOH A 635 DISTANCE = 5.40 ANGSTROMS
REMARK 525 HOH A 636 DISTANCE = 5.19 ANGSTROMS
REMARK 525 HOH A 650 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH A 667 DISTANCE = 7.60 ANGSTROMS
REMARK 525 HOH A 678 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH A 683 DISTANCE = 5.40 ANGSTROMS
REMARK 525 HOH A 689 DISTANCE = 5.54 ANGSTROMS
REMARK 525 HOH A 702 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH A 713 DISTANCE = 5.54 ANGSTROMS
REMARK 525 HOH A 717 DISTANCE = 7.01 ANGSTROMS
REMARK 525 HOH A 730 DISTANCE = 5.26 ANGSTROMS
REMARK 525 HOH A 750 DISTANCE = 9.44 ANGSTROMS
REMARK 525 HOH A 763 DISTANCE = 6.72 ANGSTROMS
REMARK 525 HOH A 777 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH A 784 DISTANCE = 9.80 ANGSTROMS
REMARK 525 HOH A 786 DISTANCE = 9.76 ANGSTROMS
REMARK 525 HOH A 792 DISTANCE = 6.95 ANGSTROMS
REMARK 525 HOH A 799 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH A 804 DISTANCE = 7.07 ANGSTROMS
REMARK 525 HOH A 808 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH A 814 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH A 818 DISTANCE = 9.44 ANGSTROMS
REMARK 525 HOH A 820 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH A 831 DISTANCE = 9.80 ANGSTROMS
REMARK 525 HOH A 844 DISTANCE = 6.92 ANGSTROMS
REMARK 525 HOH A 845 DISTANCE = 9.40 ANGSTROMS
REMARK 525 HOH A 885 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A 886 DISTANCE = 6.49 ANGSTROMS
REMARK 525 HOH A 888 DISTANCE = 7.61 ANGSTROMS
REMARK 525 HOH A 908 DISTANCE = 6.76 ANGSTROMS
REMARK 525 HOH A 909 DISTANCE = 8.30 ANGSTROMS
REMARK 525 HOH A 910 DISTANCE = 6.53 ANGSTROMS
REMARK 525 HOH A 918 DISTANCE = 9.74 ANGSTROMS
REMARK 525 HOH B 501 DISTANCE = 10.23 ANGSTROMS
REMARK 525 HOH B 502 DISTANCE = 11.34 ANGSTROMS
REMARK 525 HOH B 503 DISTANCE = 7.05 ANGSTROMS
REMARK 525 HOH B 504 DISTANCE = 11.89 ANGSTROMS
REMARK 525 HOH B 505 DISTANCE = 7.95 ANGSTROMS
REMARK 525 HOH B 506 DISTANCE = 10.86 ANGSTROMS
REMARK 525 HOH B 759 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH B 765 DISTANCE = 6.78 ANGSTROMS
REMARK 525 HOH B 773 DISTANCE = 5.31 ANGSTROMS
REMARK 525 HOH B 788 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH B 789 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH B 812 DISTANCE = 7.26 ANGSTROMS
REMARK 525 HOH B 818 DISTANCE = 5.63 ANGSTROMS
REMARK 525 HOH B 820 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH B 842 DISTANCE = 9.38 ANGSTROMS
REMARK 525 HOH B 849 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH B 850 DISTANCE = 8.04 ANGSTROMS
REMARK 525 HOH B 856 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH B 860 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH B 872 DISTANCE = 5.45 ANGSTROMS
REMARK 525 HOH B 892 DISTANCE = 5.71 ANGSTROMS
REMARK 525 HOH B 893 DISTANCE = 7.27 ANGSTROMS
REMARK 525 HOH B 899 DISTANCE = 9.25 ANGSTROMS
REMARK 525 HOH B 907 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH B 908 DISTANCE = 9.68 ANGSTROMS
REMARK 525 HOH B 910 DISTANCE = 5.39 ANGSTROMS
REMARK 525 HOH B 924 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH B 925 DISTANCE = 5.42 ANGSTROMS
REMARK 525 HOH B 926 DISTANCE = 5.46 ANGSTROMS
REMARK 525 HOH B 931 DISTANCE = 5.21 ANGSTROMS
REMARK 525 HOH B 950 DISTANCE = 8.24 ANGSTROMS
REMARK 525 HOH B 951 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH B 963 DISTANCE = 7.50 ANGSTROMS
REMARK 525 HOH B 984 DISTANCE = 5.46 ANGSTROMS
REMARK 525 HOH B 999 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH B1001 DISTANCE = 8.23 ANGSTROMS
REMARK 525 HOH B1002 DISTANCE = 9.16 ANGSTROMS
REMARK 525 HOH B1009 DISTANCE = 6.70 ANGSTROMS
REMARK 525 HOH B1017 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH B1021 DISTANCE = 6.72 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WL5 RELATED DB: PDB
REMARK 900 RELATED ID: 3WL7 RELATED DB: PDB
REMARK 900 RELATED ID: 3WL8 RELATED DB: PDB
REMARK 900 RELATED ID: 3WLA RELATED DB: PDB
DBREF 3WL6 A -1 348 UNP Q9LCQ7 OPH_PSESP 30 379
DBREF 3WL6 B -1 348 UNP Q9LCQ7 OPH_PSESP 30 379
SEQADV 3WL6 ALA A -4 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 GLY A -3 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 ALA A -2 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 ALA A 349 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 SER A 350 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 ALA A 351 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 TRP A 352 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 SER A 353 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 HIS A 354 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 PRO A 355 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 GLN A 356 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 PHE A 357 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 GLU A 358 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 LYS A 359 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 ALA B -4 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 GLY B -3 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 ALA B -2 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 ALA B 349 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 SER B 350 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 ALA B 351 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 TRP B 352 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 SER B 353 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 HIS B 354 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 PRO B 355 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 GLN B 356 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 PHE B 357 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 GLU B 358 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL6 LYS B 359 UNP Q9LCQ7 EXPRESSION TAG
SEQRES 1 A 364 ALA GLY ALA GLY ALA ASP ARG THR ALA ALA THR PRO ALA
SEQRES 2 A 364 ALA ALA ASN PRO ALA ALA THR GLU PRO VAL LYS TRP GLU
SEQRES 3 A 364 CYS PRO ALA GLY TYR GLU VAL LYS GLU GLY LEU ASN VAL
SEQRES 4 A 364 ASP PHE PRO HIS LYS GLY MET LYS ARG ALA PHE ILE VAL
SEQRES 5 A 364 TYR PRO ALA LYS ASN VAL SER GLY PRO ALA PRO VAL TRP
SEQRES 6 A 364 VAL PRO MET THR GLY SER VAL GLU SER THR ASN ASP ASN
SEQRES 7 A 364 LEU THR VAL ALA ARG SER GLY ALA ASN SER ILE LEU ALA
SEQRES 8 A 364 ASP HIS GLY TYR THR VAL ILE ALA PRO VAL ARG ALA CYS
SEQRES 9 A 364 ALA ASN GLN ASP PRO ASN ILE ARG GLY GLU ARG CYS ASN
SEQRES 10 A 364 GLY PRO GLY SER ASN GLY TRP ASN TRP ASN PRO TRP PHE
SEQRES 11 A 364 GLU GLY ARG ALA ALA ASP PRO SER GLY GLU HIS TRP LYS
SEQRES 12 A 364 ASN ASP GLU GLY PRO ASP SER SER PHE PHE VAL ALA MET
SEQRES 13 A 364 VAL GLN CYS VAL GLY THR LYS TYR LYS LEU ASP ALA ARG
SEQRES 14 A 364 ARG LEU PHE LEU GLY GLY ILE SER SER GLY GLY THR MET
SEQRES 15 A 364 THR ASN ARG ALA LEU LEU PHE ARG SER ASN PHE TRP ALA
SEQRES 16 A 364 GLY GLY LEU PRO ILE SER GLY GLU TRP TYR VAL THR SER
SEQRES 17 A 364 ASP ASP GLY THR PRO LEU SER PHE ASP ASP ALA ARG ALA
SEQRES 18 A 364 ALA VAL ALA ALA ALA PRO THR LYS ILE HIS GLN GLY ARG
SEQRES 19 A 364 VAL GLY PRO TYR PRO LEU PRO ALA LYS VAL GLY PRO LEU
SEQRES 20 A 364 ILE VAL MET THR VAL TRP GLY GLY GLU LYS ASP LEU TRP
SEQRES 21 A 364 ASN CYS THR ARG PRO ASP GLY SER ARG PHE LEU CYS ALA
SEQRES 22 A 364 ASP TYR ARG PRO SER THR GLN ALA GLY SER ASN PHE PHE
SEQRES 23 A 364 SER ALA GLN PRO ASP VAL VAL HIS VAL ALA CYS SER SER
SEQRES 24 A 364 THR HIS GLY HIS MET TRP PRO GLN LEU ASN THR GLN GLU
SEQRES 25 A 364 PHE ASN ARG TRP ALA LEU ASP THR LEU ALA SER HIS PRO
SEQRES 26 A 364 LYS GLY SER ASP PRO ARG SER PHE LYS LEU THR GLN PRO
SEQRES 27 A 364 PRO GLU GLY TYR THR CYS HIS VAL GLY PRO PHE THR GLY
SEQRES 28 A 364 LEU TYR ALA SER ALA TRP SER HIS PRO GLN PHE GLU LYS
SEQRES 1 B 364 ALA GLY ALA GLY ALA ASP ARG THR ALA ALA THR PRO ALA
SEQRES 2 B 364 ALA ALA ASN PRO ALA ALA THR GLU PRO VAL LYS TRP GLU
SEQRES 3 B 364 CYS PRO ALA GLY TYR GLU VAL LYS GLU GLY LEU ASN VAL
SEQRES 4 B 364 ASP PHE PRO HIS LYS GLY MET LYS ARG ALA PHE ILE VAL
SEQRES 5 B 364 TYR PRO ALA LYS ASN VAL SER GLY PRO ALA PRO VAL TRP
SEQRES 6 B 364 VAL PRO MET THR GLY SER VAL GLU SER THR ASN ASP ASN
SEQRES 7 B 364 LEU THR VAL ALA ARG SER GLY ALA ASN SER ILE LEU ALA
SEQRES 8 B 364 ASP HIS GLY TYR THR VAL ILE ALA PRO VAL ARG ALA CYS
SEQRES 9 B 364 ALA ASN GLN ASP PRO ASN ILE ARG GLY GLU ARG CYS ASN
SEQRES 10 B 364 GLY PRO GLY SER ASN GLY TRP ASN TRP ASN PRO TRP PHE
SEQRES 11 B 364 GLU GLY ARG ALA ALA ASP PRO SER GLY GLU HIS TRP LYS
SEQRES 12 B 364 ASN ASP GLU GLY PRO ASP SER SER PHE PHE VAL ALA MET
SEQRES 13 B 364 VAL GLN CYS VAL GLY THR LYS TYR LYS LEU ASP ALA ARG
SEQRES 14 B 364 ARG LEU PHE LEU GLY GLY ILE SER SER GLY GLY THR MET
SEQRES 15 B 364 THR ASN ARG ALA LEU LEU PHE ARG SER ASN PHE TRP ALA
SEQRES 16 B 364 GLY GLY LEU PRO ILE SER GLY GLU TRP TYR VAL THR SER
SEQRES 17 B 364 ASP ASP GLY THR PRO LEU SER PHE ASP ASP ALA ARG ALA
SEQRES 18 B 364 ALA VAL ALA ALA ALA PRO THR LYS ILE HIS GLN GLY ARG
SEQRES 19 B 364 VAL GLY PRO TYR PRO LEU PRO ALA LYS VAL GLY PRO LEU
SEQRES 20 B 364 ILE VAL MET THR VAL TRP GLY GLY GLU LYS ASP LEU TRP
SEQRES 21 B 364 ASN CYS THR ARG PRO ASP GLY SER ARG PHE LEU CYS ALA
SEQRES 22 B 364 ASP TYR ARG PRO SER THR GLN ALA GLY SER ASN PHE PHE
SEQRES 23 B 364 SER ALA GLN PRO ASP VAL VAL HIS VAL ALA CYS SER SER
SEQRES 24 B 364 THR HIS GLY HIS MET TRP PRO GLN LEU ASN THR GLN GLU
SEQRES 25 B 364 PHE ASN ARG TRP ALA LEU ASP THR LEU ALA SER HIS PRO
SEQRES 26 B 364 LYS GLY SER ASP PRO ARG SER PHE LYS LEU THR GLN PRO
SEQRES 27 B 364 PRO GLU GLY TYR THR CYS HIS VAL GLY PRO PHE THR GLY
SEQRES 28 B 364 LEU TYR ALA SER ALA TRP SER HIS PRO GLN PHE GLU LYS
HET CIT B 401 13
HETNAM CIT CITRIC ACID
FORMUL 3 CIT C6 H8 O7
FORMUL 4 HOH *1049(H2 O)
HELIX 1 1 CYS A 22 TYR A 26 5 5
HELIX 2 2 SER A 69 VAL A 76 1 8
HELIX 3 3 ALA A 77 GLY A 80 5 4
HELIX 4 4 ALA A 81 GLY A 89 5 9
HELIX 5 5 ARG A 97 ASN A 101 5 5
HELIX 6 6 ASP A 131 ASN A 139 5 9
HELIX 7 7 GLY A 142 GLY A 156 1 15
HELIX 8 8 SER A 172 ARG A 185 1 14
HELIX 9 9 SER A 210 ALA A 221 1 12
HELIX 10 10 TYR A 270 GLN A 284 1 15
HELIX 11 11 ASN A 304 SER A 318 1 15
HELIX 12 12 ASP A 324 PHE A 328 5 5
HELIX 13 13 SER B 69 VAL B 76 1 8
HELIX 14 14 ALA B 77 GLY B 80 5 4
HELIX 15 15 ALA B 81 GLY B 89 5 9
HELIX 16 16 ARG B 97 ASN B 101 5 5
HELIX 17 17 ASP B 131 ASN B 139 5 9
HELIX 18 18 GLY B 142 TYR B 159 1 18
HELIX 19 19 SER B 172 ARG B 185 1 14
HELIX 20 20 SER B 210 ALA B 221 1 12
HELIX 21 21 ASP B 269 GLN B 284 1 16
HELIX 22 22 ASN B 304 SER B 318 1 15
HELIX 23 23 ASP B 324 PHE B 328 5 5
SHEET 1 A 9 GLY A 31 HIS A 38 0
SHEET 2 A 9 MET A 41 TYR A 48 -1 O PHE A 45 N ASN A 33
SHEET 3 A 9 THR A 91 PRO A 95 -1 O VAL A 92 N TYR A 48
SHEET 4 A 9 ALA A 57 MET A 63 1 N PRO A 58 O THR A 91
SHEET 5 A 9 LEU A 161 ILE A 171 1 O ARG A 165 N VAL A 59
SHEET 6 A 9 GLY A 191 ILE A 195 1 O ILE A 195 N GLY A 170
SHEET 7 A 9 LEU A 242 TRP A 248 1 O MET A 245 N GLY A 192
SHEET 8 A 9 VAL A 287 SER A 293 1 O VAL A 290 N VAL A 244
SHEET 9 A 9 THR A 338 VAL A 341 -1 O HIS A 340 N ALA A 291
SHEET 1 B 2 LEU A 254 THR A 258 0
SHEET 2 B 2 ARG A 264 ASP A 269 -1 O CYS A 267 N TRP A 255
SHEET 1 C 9 GLY B 31 HIS B 38 0
SHEET 2 C 9 MET B 41 TYR B 48 -1 O ARG B 43 N PHE B 36
SHEET 3 C 9 THR B 91 PRO B 95 -1 O ALA B 94 N ILE B 46
SHEET 4 C 9 ALA B 57 MET B 63 1 N PRO B 58 O THR B 91
SHEET 5 C 9 LEU B 161 ILE B 171 1 O ASP B 162 N ALA B 57
SHEET 6 C 9 GLY B 191 ILE B 195 1 O ILE B 195 N GLY B 170
SHEET 7 C 9 LEU B 242 TRP B 248 1 O MET B 245 N GLY B 192
SHEET 8 C 9 VAL B 287 SER B 293 1 O VAL B 290 N VAL B 244
SHEET 9 C 9 THR B 338 VAL B 341 -1 O HIS B 340 N ALA B 291
SSBOND 1 CYS A 22 CYS A 154 1555 1555 2.08
SSBOND 2 CYS A 99 CYS A 111 1555 1555 2.07
SSBOND 3 CYS A 257 CYS A 267 1555 1555 2.06
SSBOND 4 CYS A 292 CYS A 339 1555 1555 2.05
SSBOND 5 CYS B 22 CYS B 154 1555 1555 2.07
SSBOND 6 CYS B 99 CYS B 111 1555 1555 2.08
SSBOND 7 CYS B 292 CYS B 339 1555 1555 2.06
CISPEP 1 TYR A 233 PRO A 234 0 -0.43
CISPEP 2 TYR B 233 PRO B 234 0 -0.43
SITE 1 AC1 9 SER B 66 VAL B 67 GLU B 68 ILE B 171
SITE 2 AC1 9 SER B 172 HIS B 298 HOH B 547 HOH B 909
SITE 3 AC1 9 HOH B1027
CRYST1 49.934 58.285 65.350 89.63 73.17 75.76 P 1 2
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 0.020026 -0.005082 -0.006428 0.00000
SCALE2 0.000000 0.017701 0.001239 0.00000
SCALE3 0.000000 0.000000 0.016026 0.00000
TER 2551 ALA A 351
TER 5004 SER B 350
MASTER 447 0 1 23 20 0 3 6 6064 2 27 56
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