| content |
HEADER HYDROLASE 08-NOV-13 3WL8
TITLE CRYSTAL STRUCTURE OF POPH S172A WITH OCTANOIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OXIDIZED POLYVINYL ALCOHOL HYDROLASE;
COMPND 3 CHAIN: A;
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;
COMPND 8 MUTATION: 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 3WL8 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 : 41325
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) : 0.148
REMARK 3 FREE R VALUE : 0.175
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2078
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) : 0.2240
REMARK 3 BIN FREE R VALUE : 0.2550
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 185
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 : 2576
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 687
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.73200
REMARK 3 B22 (A**2) : 1.27700
REMARK 3 B33 (A**2) : -3.00900
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 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) : 0.16
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.12
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.016
REMARK 3 BOND ANGLES (DEGREES) : 1.700
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) : 1.135 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.662 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.931 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.760 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 30.58
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 3WL8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-NOV-13.
REMARK 100 THE RCSB ID CODE IS RCSB096475.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-SEP-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 : 43062
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.5000
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 (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.50000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.500
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 (%): 39.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRI-SODIUM CITRATE, PH 5.6, 30%
REMARK 280 W/V POLYETHYLENE GLYCOL 4000, 6% 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 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 29.19600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.98600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.64750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.98600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.19600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.64750
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: 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 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 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 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 748 O HOH A 1096 1.95
REMARK 500 O HOH A 917 O HOH A 1137 1.99
REMARK 500 O HOH A 775 O HOH A 1161 2.02
REMARK 500 N VAL A 18 O HOH A 1187 2.06
REMARK 500 O HOH A 677 O HOH A 1094 2.07
REMARK 500 O HOH A 951 O HOH A 1069 2.09
REMARK 500 O HOH A 673 O HOH A 1184 2.10
REMARK 500 O HOH A 615 O HOH A 774 2.11
REMARK 500 O HOH A 1011 O HOH A 1172 2.13
REMARK 500 O HOH A 822 O HOH A 1164 2.17
REMARK 500 O HOH A 774 O HOH A 1106 2.17
REMARK 500 O HOH A 963 O HOH A 1026 2.18
REMARK 500 O HOH A 837 O HOH A 1166 2.18
REMARK 500 O HOH A 970 O HOH A 1145 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 1173 O HOH A 1184 4455 1.55
REMARK 500 O HOH A 1167 O HOH A 1179 4455 1.63
REMARK 500 O HOH A 1171 O HOH A 1175 4555 1.64
REMARK 500 O HOH A 909 O HOH A 1161 4555 2.18
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 58.18 35.59
REMARK 500 ARG A 107 -102.24 -103.68
REMARK 500 ARG A 110 16.79 59.09
REMARK 500 ALA A 172 -121.69 61.05
REMARK 500 TRP A 352 0.18 -62.96
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 TYR A 233 0.09 SIDE CHAIN
REMARK 500 TYR A 337 0.07 SIDE CHAIN
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 912 DISTANCE = 5.57 ANGSTROMS
REMARK 525 HOH A 935 DISTANCE = 7.01 ANGSTROMS
REMARK 525 HOH A 956 DISTANCE = 7.36 ANGSTROMS
REMARK 525 HOH A 980 DISTANCE = 7.69 ANGSTROMS
REMARK 525 HOH A 991 DISTANCE = 7.93 ANGSTROMS
REMARK 525 HOH A1017 DISTANCE = 5.43 ANGSTROMS
REMARK 525 HOH A1020 DISTANCE = 6.90 ANGSTROMS
REMARK 525 HOH A1031 DISTANCE = 8.06 ANGSTROMS
REMARK 525 HOH A1037 DISTANCE = 6.87 ANGSTROMS
REMARK 525 HOH A1040 DISTANCE = 8.01 ANGSTROMS
REMARK 525 HOH A1065 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A1078 DISTANCE = 6.78 ANGSTROMS
REMARK 525 HOH A1135 DISTANCE = 5.25 ANGSTROMS
REMARK 525 HOH A1174 DISTANCE = 6.30 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 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OCA A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WL5 RELATED DB: PDB
REMARK 900 RELATED ID: 3WL6 RELATED DB: PDB
REMARK 900 RELATED ID: 3WL7 RELATED DB: PDB
REMARK 900 RELATED ID: 3WLA RELATED DB: PDB
DBREF 3WL8 A -1 348 UNP Q9LCQ7 OPH_PSESP 30 379
SEQADV 3WL8 ALA A -4 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL8 GLY A -3 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL8 ALA A -2 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL8 ALA A 172 UNP Q9LCQ7 SER 203 ENGINEERED MUTATION
SEQADV 3WL8 ALA A 349 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL8 SER A 350 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL8 ALA A 351 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL8 TRP A 352 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL8 SER A 353 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL8 HIS A 354 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL8 PRO A 355 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL8 GLN A 356 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL8 PHE A 357 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL8 GLU A 358 UNP Q9LCQ7 EXPRESSION TAG
SEQADV 3WL8 LYS A 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 ALA 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
HET CIT A 401 13
HET OCA A 402 10
HETNAM CIT CITRIC ACID
HETNAM OCA OCTANOIC ACID (CAPRYLIC ACID)
FORMUL 2 CIT C6 H8 O7
FORMUL 3 OCA C8 H16 O2
FORMUL 4 HOH *687(H2 O)
HELIX 1 1 SER A 69 VAL A 76 1 8
HELIX 2 2 ALA A 77 GLY A 80 5 4
HELIX 3 3 ALA A 81 GLY A 89 5 9
HELIX 4 4 ARG A 97 ASN A 101 5 5
HELIX 5 5 ASP A 131 ASN A 139 5 9
HELIX 6 6 GLY A 142 GLY A 156 1 15
HELIX 7 7 ALA A 172 ARG A 185 1 14
HELIX 8 8 SER A 210 ALA A 221 1 12
HELIX 9 9 TYR A 270 GLN A 284 1 15
HELIX 10 10 ASN A 304 SER A 318 1 15
HELIX 11 11 ASP A 324 PHE A 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 ALA A 94 N ILE A 46
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 ASP A 162 N ALA A 57
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
SSBOND 1 CYS A 22 CYS A 154 1555 1555 2.08
SSBOND 2 CYS A 99 CYS A 111 1555 1555 2.04
SSBOND 3 CYS A 257 CYS A 267 1555 1555 2.05
SSBOND 4 CYS A 292 CYS A 339 1555 1555 2.05
CISPEP 1 TYR A 233 PRO A 234 0 -0.14
SITE 1 AC1 10 ARG A 110 ASN A 304 THR A 305 GLN A 306
SITE 2 AC1 10 GLU A 307 ARG A 310 HOH A 714 HOH A 734
SITE 3 AC1 10 HOH A 913 HOH A1134
SITE 1 AC2 8 SER A 66 TRP A 121 ALA A 172 SER A 173
SITE 2 AC2 8 TRP A 255 TYR A 270 HIS A 298 HOH A 617
CRYST1 58.392 65.295 83.972 90.00 90.00 90.00 P 21 21 21 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 0.017126 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015315 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011909 0.00000
TER 2577 SER A 353
MASTER 371 0 2 11 11 0 5 6 3286 1 31 28
END |