| content |
HEADER HYDROLASE 08-NOV-13 3WLA
TITLE CRYSTAL STRUCTURE OF SOPH NATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OXIDIZED POLYVINYL ALCOHOL HYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: OPH, OXIDIZED PVA HYDROLASE, BETA-DIKETONE HYDROLASE;
COMPND 5 EC: 3.7.1.7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPHINGOPYXIS;
SOURCE 3 ORGANISM_TAXID: 292913;
SOURCE 4 STRAIN: 113P3;
SOURCE 5 GENE: OPH;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: GS115;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPIC9K
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 3WLA 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. 1.90 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) : 1.90
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 : 88575
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) : 0.193
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4475
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.97
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2990
REMARK 3 BIN FREE R VALUE : 0.3350
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 405
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 : 7542
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 834
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.30100
REMARK 3 B22 (A**2) : -2.71900
REMARK 3 B33 (A**2) : 0.41800
REMARK 3 B12 (A**2) : 3.55300
REMARK 3 B13 (A**2) : 4.37800
REMARK 3 B23 (A**2) : 1.63100
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.26
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) : 0.29
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.31
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.019
REMARK 3 BOND ANGLES (DEGREES) : 1.840
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 60.88
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 3WLA 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 RCSB096477.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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 : 92945
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
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 (%) : 97.8
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 26.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.51000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.900
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 (%): 56.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LI2SO4, 0.1 M BIS-TRIS PH 6.5, 3%
REMARK 280 V/V POLYETHYLENE GLYCOL 500, 6% V/V POLYETHYLENE GLYCOL 600, 25%
REMARK 280 W/V POLYETHYLENE GLYCOL 3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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, 3
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 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 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 GLU A -5
REMARK 465 ALA A -4
REMARK 465 GLU A -3
REMARK 465 ALA A -2
REMARK 465 TYR A -1
REMARK 465 VAL A 0
REMARK 465 LYS A 1
REMARK 465 GLU B -5
REMARK 465 ALA B -4
REMARK 465 GLU B -3
REMARK 465 ALA B -2
REMARK 465 TYR B -1
REMARK 465 VAL B 0
REMARK 465 LYS B 1
REMARK 465 GLU C -5
REMARK 465 ALA C -4
REMARK 465 GLU C -3
REMARK 465 ALA C -2
REMARK 465 TYR C -1
REMARK 465 VAL C 0
REMARK 465 LYS C 1
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 C 602 O HOH C 670 2.15
REMARK 500 OD1 ASN C 285 O HOH C 668 2.17
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 SER A 37 68.63 -107.06
REMARK 500 ALA A 38 63.11 -39.61
REMARK 500 ALA A 92 -74.32 -109.54
REMARK 500 SER A 156 -122.35 57.31
REMARK 500 PRO A 194 163.62 -49.28
REMARK 500 SER B 37 67.10 -103.23
REMARK 500 ALA B 38 62.52 -39.23
REMARK 500 GLN B 86 17.05 55.90
REMARK 500 ALA B 92 -81.05 -121.07
REMARK 500 SER B 156 -123.30 55.20
REMARK 500 PHE B 172 -64.23 -93.85
REMARK 500 PRO B 282 123.05 -38.78
REMARK 500 ALA C 5 146.82 -176.70
REMARK 500 LYS C 35 -75.33 -38.48
REMARK 500 ASP C 36 -139.39 -103.60
REMARK 500 SER C 37 24.80 -159.33
REMARK 500 ALA C 38 79.53 -62.34
REMARK 500 ALA C 92 -72.68 -123.39
REMARK 500 SER C 156 -125.13 58.37
REMARK 500 PHE C 172 -61.45 -90.57
REMARK 500 PRO C 282 123.62 -38.32
REMARK 500 PRO C 315 171.53 -56.54
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 318 0.08 SIDE CHAIN
REMARK 500 TYR C 318 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASN C 106 23.7 L L OUTSIDE RANGE
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 A1179 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH A1193 DISTANCE = 5.35 ANGSTROMS
REMARK 525 HOH A1247 DISTANCE = 5.34 ANGSTROMS
REMARK 525 HOH A1267 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH A1281 DISTANCE = 7.36 ANGSTROMS
REMARK 525 HOH A1292 DISTANCE = 6.92 ANGSTROMS
REMARK 525 HOH A1295 DISTANCE = 7.92 ANGSTROMS
REMARK 525 HOH A1302 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH A1303 DISTANCE = 7.83 ANGSTROMS
REMARK 525 HOH A1304 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A1312 DISTANCE = 8.00 ANGSTROMS
REMARK 525 HOH B 685 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH B 748 DISTANCE = 7.25 ANGSTROMS
REMARK 525 HOH B 751 DISTANCE = 7.01 ANGSTROMS
REMARK 525 HOH B 752 DISTANCE = 7.93 ANGSTROMS
REMARK 525 HOH B 753 DISTANCE = 7.69 ANGSTROMS
REMARK 525 HOH B 756 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH C 501 DISTANCE = 8.02 ANGSTROMS
REMARK 525 HOH C 665 DISTANCE = 7.90 ANGSTROMS
REMARK 525 HOH C 674 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH C 679 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH C 699 DISTANCE = 7.01 ANGSTROMS
REMARK 525 HOH C 718 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH C 743 DISTANCE = 7.07 ANGSTROMS
REMARK 525 HOH C 747 DISTANCE = 5.21 ANGSTROMS
REMARK 525 HOH C 750 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH C 754 DISTANCE = 5.66 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 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: 3WL8 RELATED DB: PDB
DBREF 3WLA A 1 330 UNP Q588Z2 OPH_SPHS1 35 364
DBREF 3WLA B 1 330 UNP Q588Z2 OPH_SPHS1 35 364
DBREF 3WLA C 1 330 UNP Q588Z2 OPH_SPHS1 35 364
SEQADV 3WLA GLU A -5 UNP Q588Z2 EXPRESSION TAG
SEQADV 3WLA ALA A -4 UNP Q588Z2 EXPRESSION TAG
SEQADV 3WLA GLU A -3 UNP Q588Z2 EXPRESSION TAG
SEQADV 3WLA ALA A -2 UNP Q588Z2 EXPRESSION TAG
SEQADV 3WLA TYR A -1 UNP Q588Z2 EXPRESSION TAG
SEQADV 3WLA VAL A 0 UNP Q588Z2 EXPRESSION TAG
SEQADV 3WLA GLU B -5 UNP Q588Z2 EXPRESSION TAG
SEQADV 3WLA ALA B -4 UNP Q588Z2 EXPRESSION TAG
SEQADV 3WLA GLU B -3 UNP Q588Z2 EXPRESSION TAG
SEQADV 3WLA ALA B -2 UNP Q588Z2 EXPRESSION TAG
SEQADV 3WLA TYR B -1 UNP Q588Z2 EXPRESSION TAG
SEQADV 3WLA VAL B 0 UNP Q588Z2 EXPRESSION TAG
SEQADV 3WLA GLU C -5 UNP Q588Z2 EXPRESSION TAG
SEQADV 3WLA ALA C -4 UNP Q588Z2 EXPRESSION TAG
SEQADV 3WLA GLU C -3 UNP Q588Z2 EXPRESSION TAG
SEQADV 3WLA ALA C -2 UNP Q588Z2 EXPRESSION TAG
SEQADV 3WLA TYR C -1 UNP Q588Z2 EXPRESSION TAG
SEQADV 3WLA VAL C 0 UNP Q588Z2 EXPRESSION TAG
SEQRES 1 A 336 GLU ALA GLU ALA TYR VAL LYS SER GLU TRP ALA CYS PRO
SEQRES 2 A 336 GLU GLY PHE THR PRO LYS ALA GLY LEU ASN THR ASP PHE
SEQRES 3 A 336 PRO SER ASP GLY LYS LYS ARG ALA PHE VAL VAL VAL PRO
SEQRES 4 A 336 PRO LYS ASP SER ALA GLY GLY ALA PRO VAL TRP VAL PRO
SEQRES 5 A 336 MET VAL GLY THR VAL GLU ALA THR ASN TRP ASN LEU ASN
SEQRES 6 A 336 VAL PRO ARG SER GLY ASN ASN ALA LYS LEU ALA GLU HIS
SEQRES 7 A 336 GLY TYR MET VAL ILE SER PRO VAL ARG GLN CYS ALA GLU
SEQRES 8 A 336 GLN ASP PRO ASN LEU GLY ALA GLY ALA CYS ASN GLY VAL
SEQRES 9 A 336 GLY LYS ASP GLY TRP THR TRP ASN PRO TRP ASN ASP GLY
SEQRES 10 A 336 ARG ALA PRO ASP ALA SER GLY ASP LYS TYR LYS THR ASP
SEQRES 11 A 336 ALA GLY ASP ASP VAL ARG PHE LEU GLU ALA MET VAL ARG
SEQRES 12 A 336 CYS VAL GLY THR LYS TRP LYS LEU ASP ARG LYS ARG LEU
SEQRES 13 A 336 PHE LEU GLY GLY ILE SER ALA GLY GLY THR MET THR ASN
SEQRES 14 A 336 ARG ALA LEU LEU PHE ASP SER GLU PHE TRP ALA GLY GLY
SEQRES 15 A 336 MET PRO ILE SER GLY GLU TRP TYR SER THR LYS ASP ASP
SEQRES 16 A 336 GLY SER THR VAL PRO PHE GLN GLU THR ARG LYS MET VAL
SEQRES 17 A 336 ALA ALA ALA PRO ALA LYS ILE TRP GLN GLY ARG VAL GLY
SEQRES 18 A 336 PRO TYR PRO LEU PRO SER LYS LEU ASP PRO MET VAL VAL
SEQRES 19 A 336 ILE THR VAL TRP GLY GLY GLU LYS ASP LEU TRP ASP CYS
SEQRES 20 A 336 GLY PRO PRO LEU GLY LEU CYS SER ASP TYR ARG PRO THR
SEQRES 21 A 336 THR GLN ALA SER SER ASN TYR PHE SER SER ILE SER ASN
SEQRES 22 A 336 VAL VAL HIS VAL ALA CYS SER ALA THR HIS GLY HIS MET
SEQRES 23 A 336 TRP PRO GLN VAL ASN THR ASP ALA PHE ASN LEU TRP ALA
SEQRES 24 A 336 LEU ASN THR MET ALA SER HIS PRO LYS GLY SER SER PRO
SEQRES 25 A 336 LYS ASP PHE LYS LEU THR ALA PRO PRO GLU GLY TYR SER
SEQRES 26 A 336 CYS LYS ILE GLY ARG PHE THR ASP HIS TYR LYS
SEQRES 1 B 336 GLU ALA GLU ALA TYR VAL LYS SER GLU TRP ALA CYS PRO
SEQRES 2 B 336 GLU GLY PHE THR PRO LYS ALA GLY LEU ASN THR ASP PHE
SEQRES 3 B 336 PRO SER ASP GLY LYS LYS ARG ALA PHE VAL VAL VAL PRO
SEQRES 4 B 336 PRO LYS ASP SER ALA GLY GLY ALA PRO VAL TRP VAL PRO
SEQRES 5 B 336 MET VAL GLY THR VAL GLU ALA THR ASN TRP ASN LEU ASN
SEQRES 6 B 336 VAL PRO ARG SER GLY ASN ASN ALA LYS LEU ALA GLU HIS
SEQRES 7 B 336 GLY TYR MET VAL ILE SER PRO VAL ARG GLN CYS ALA GLU
SEQRES 8 B 336 GLN ASP PRO ASN LEU GLY ALA GLY ALA CYS ASN GLY VAL
SEQRES 9 B 336 GLY LYS ASP GLY TRP THR TRP ASN PRO TRP ASN ASP GLY
SEQRES 10 B 336 ARG ALA PRO ASP ALA SER GLY ASP LYS TYR LYS THR ASP
SEQRES 11 B 336 ALA GLY ASP ASP VAL ARG PHE LEU GLU ALA MET VAL ARG
SEQRES 12 B 336 CYS VAL GLY THR LYS TRP LYS LEU ASP ARG LYS ARG LEU
SEQRES 13 B 336 PHE LEU GLY GLY ILE SER ALA GLY GLY THR MET THR ASN
SEQRES 14 B 336 ARG ALA LEU LEU PHE ASP SER GLU PHE TRP ALA GLY GLY
SEQRES 15 B 336 MET PRO ILE SER GLY GLU TRP TYR SER THR LYS ASP ASP
SEQRES 16 B 336 GLY SER THR VAL PRO PHE GLN GLU THR ARG LYS MET VAL
SEQRES 17 B 336 ALA ALA ALA PRO ALA LYS ILE TRP GLN GLY ARG VAL GLY
SEQRES 18 B 336 PRO TYR PRO LEU PRO SER LYS LEU ASP PRO MET VAL VAL
SEQRES 19 B 336 ILE THR VAL TRP GLY GLY GLU LYS ASP LEU TRP ASP CYS
SEQRES 20 B 336 GLY PRO PRO LEU GLY LEU CYS SER ASP TYR ARG PRO THR
SEQRES 21 B 336 THR GLN ALA SER SER ASN TYR PHE SER SER ILE SER ASN
SEQRES 22 B 336 VAL VAL HIS VAL ALA CYS SER ALA THR HIS GLY HIS MET
SEQRES 23 B 336 TRP PRO GLN VAL ASN THR ASP ALA PHE ASN LEU TRP ALA
SEQRES 24 B 336 LEU ASN THR MET ALA SER HIS PRO LYS GLY SER SER PRO
SEQRES 25 B 336 LYS ASP PHE LYS LEU THR ALA PRO PRO GLU GLY TYR SER
SEQRES 26 B 336 CYS LYS ILE GLY ARG PHE THR ASP HIS TYR LYS
SEQRES 1 C 336 GLU ALA GLU ALA TYR VAL LYS SER GLU TRP ALA CYS PRO
SEQRES 2 C 336 GLU GLY PHE THR PRO LYS ALA GLY LEU ASN THR ASP PHE
SEQRES 3 C 336 PRO SER ASP GLY LYS LYS ARG ALA PHE VAL VAL VAL PRO
SEQRES 4 C 336 PRO LYS ASP SER ALA GLY GLY ALA PRO VAL TRP VAL PRO
SEQRES 5 C 336 MET VAL GLY THR VAL GLU ALA THR ASN TRP ASN LEU ASN
SEQRES 6 C 336 VAL PRO ARG SER GLY ASN ASN ALA LYS LEU ALA GLU HIS
SEQRES 7 C 336 GLY TYR MET VAL ILE SER PRO VAL ARG GLN CYS ALA GLU
SEQRES 8 C 336 GLN ASP PRO ASN LEU GLY ALA GLY ALA CYS ASN GLY VAL
SEQRES 9 C 336 GLY LYS ASP GLY TRP THR TRP ASN PRO TRP ASN ASP GLY
SEQRES 10 C 336 ARG ALA PRO ASP ALA SER GLY ASP LYS TYR LYS THR ASP
SEQRES 11 C 336 ALA GLY ASP ASP VAL ARG PHE LEU GLU ALA MET VAL ARG
SEQRES 12 C 336 CYS VAL GLY THR LYS TRP LYS LEU ASP ARG LYS ARG LEU
SEQRES 13 C 336 PHE LEU GLY GLY ILE SER ALA GLY GLY THR MET THR ASN
SEQRES 14 C 336 ARG ALA LEU LEU PHE ASP SER GLU PHE TRP ALA GLY GLY
SEQRES 15 C 336 MET PRO ILE SER GLY GLU TRP TYR SER THR LYS ASP ASP
SEQRES 16 C 336 GLY SER THR VAL PRO PHE GLN GLU THR ARG LYS MET VAL
SEQRES 17 C 336 ALA ALA ALA PRO ALA LYS ILE TRP GLN GLY ARG VAL GLY
SEQRES 18 C 336 PRO TYR PRO LEU PRO SER LYS LEU ASP PRO MET VAL VAL
SEQRES 19 C 336 ILE THR VAL TRP GLY GLY GLU LYS ASP LEU TRP ASP CYS
SEQRES 20 C 336 GLY PRO PRO LEU GLY LEU CYS SER ASP TYR ARG PRO THR
SEQRES 21 C 336 THR GLN ALA SER SER ASN TYR PHE SER SER ILE SER ASN
SEQRES 22 C 336 VAL VAL HIS VAL ALA CYS SER ALA THR HIS GLY HIS MET
SEQRES 23 C 336 TRP PRO GLN VAL ASN THR ASP ALA PHE ASN LEU TRP ALA
SEQRES 24 C 336 LEU ASN THR MET ALA SER HIS PRO LYS GLY SER SER PRO
SEQRES 25 C 336 LYS ASP PHE LYS LEU THR ALA PRO PRO GLU GLY TYR SER
SEQRES 26 C 336 CYS LYS ILE GLY ARG PHE THR ASP HIS TYR LYS
HET SO4 A 901 5
HET SO4 B 401 5
HET SO4 C 401 5
HET SO4 C 402 5
HETNAM SO4 SULFATE ION
FORMUL 4 SO4 4(O4 S 2-)
FORMUL 8 HOH *834(H2 O)
HELIX 1 1 ALA A 53 VAL A 60 1 8
HELIX 2 2 PRO A 61 GLY A 64 5 4
HELIX 3 3 ASN A 65 GLY A 73 5 9
HELIX 4 4 ARG A 81 GLU A 85 5 5
HELIX 5 5 ALA A 92 ASN A 96 5 5
HELIX 6 6 ASP A 115 THR A 123 5 9
HELIX 7 7 GLY A 126 GLY A 140 1 15
HELIX 8 8 SER A 156 ASP A 169 1 14
HELIX 9 9 PRO A 194 ALA A 205 1 12
HELIX 10 10 TYR A 251 SER A 264 1 14
HELIX 11 11 ASN A 285 SER A 299 1 15
HELIX 12 12 SER A 305 PHE A 309 5 5
HELIX 13 13 ALA B 53 VAL B 60 1 8
HELIX 14 14 PRO B 61 GLY B 64 5 4
HELIX 15 15 ASN B 65 GLY B 73 5 9
HELIX 16 16 ARG B 81 GLU B 85 5 5
HELIX 17 17 ALA B 92 ASN B 96 5 5
HELIX 18 18 ASP B 115 THR B 123 5 9
HELIX 19 19 GLY B 126 GLY B 140 1 15
HELIX 20 20 SER B 156 ASP B 169 1 14
HELIX 21 21 PRO B 194 ALA B 205 1 12
HELIX 22 22 TYR B 251 ILE B 265 1 15
HELIX 23 23 ASN B 285 SER B 299 1 15
HELIX 24 24 SER B 305 PHE B 309 5 5
HELIX 25 25 ALA C 53 VAL C 60 1 8
HELIX 26 26 PRO C 61 GLY C 64 5 4
HELIX 27 27 ASN C 65 GLY C 73 5 9
HELIX 28 28 ARG C 81 GLU C 85 5 5
HELIX 29 29 ALA C 92 ASN C 96 5 5
HELIX 30 30 ASP C 115 THR C 123 5 9
HELIX 31 31 GLY C 126 GLY C 140 1 15
HELIX 32 32 SER C 156 ASP C 169 1 14
HELIX 33 33 PRO C 194 ALA C 205 1 12
HELIX 34 34 TYR C 251 ILE C 265 1 15
HELIX 35 35 ASN C 285 SER C 299 1 15
HELIX 36 36 SER C 305 PHE C 309 5 5
SHEET 1 A 9 GLY A 15 SER A 22 0
SHEET 2 A 9 LYS A 25 VAL A 32 -1 O ARG A 27 N PHE A 20
SHEET 3 A 9 MET A 75 PRO A 79 -1 O SER A 78 N VAL A 30
SHEET 4 A 9 ALA A 41 MET A 47 1 N PRO A 42 O MET A 75
SHEET 5 A 9 LEU A 145 ILE A 155 1 O ARG A 149 N VAL A 43
SHEET 6 A 9 GLY A 175 ILE A 179 1 O ILE A 179 N GLY A 154
SHEET 7 A 9 MET A 226 TRP A 232 1 O ILE A 229 N GLY A 176
SHEET 8 A 9 VAL A 268 SER A 274 1 O VAL A 271 N VAL A 228
SHEET 9 A 9 SER A 319 ILE A 322 -1 O LYS A 321 N ALA A 272
SHEET 1 B 2 LEU A 238 ASP A 240 0
SHEET 2 B 2 LEU A 247 ASP A 250 -1 O SER A 249 N TRP A 239
SHEET 1 C 9 GLY B 15 SER B 22 0
SHEET 2 C 9 LYS B 25 VAL B 32 -1 O ARG B 27 N PHE B 20
SHEET 3 C 9 MET B 75 PRO B 79 -1 O VAL B 76 N VAL B 32
SHEET 4 C 9 ALA B 41 MET B 47 1 N TRP B 44 O MET B 75
SHEET 5 C 9 LEU B 145 ILE B 155 1 O ARG B 149 N VAL B 43
SHEET 6 C 9 GLY B 175 ILE B 179 1 O ILE B 179 N GLY B 154
SHEET 7 C 9 MET B 226 TRP B 232 1 O ILE B 229 N GLY B 176
SHEET 8 C 9 VAL B 268 SER B 274 1 O CYS B 273 N THR B 230
SHEET 9 C 9 SER B 319 ILE B 322 -1 O LYS B 321 N ALA B 272
SHEET 1 D 2 LEU B 238 ASP B 240 0
SHEET 2 D 2 LEU B 247 ASP B 250 -1 O CYS B 248 N TRP B 239
SHEET 1 E 9 GLY C 15 SER C 22 0
SHEET 2 E 9 LYS C 25 VAL C 32 -1 O ARG C 27 N PHE C 20
SHEET 3 E 9 MET C 75 PRO C 79 -1 O VAL C 76 N VAL C 32
SHEET 4 E 9 ALA C 41 MET C 47 1 N PRO C 42 O MET C 75
SHEET 5 E 9 LEU C 145 ILE C 155 1 O ARG C 149 N VAL C 43
SHEET 6 E 9 GLY C 175 ILE C 179 1 O ILE C 179 N GLY C 154
SHEET 7 E 9 MET C 226 TRP C 232 1 O ILE C 229 N GLY C 176
SHEET 8 E 9 VAL C 268 SER C 274 1 O VAL C 271 N VAL C 228
SHEET 9 E 9 SER C 319 ILE C 322 -1 O SER C 319 N SER C 274
SHEET 1 F 2 LEU C 238 ASP C 240 0
SHEET 2 F 2 LEU C 247 ASP C 250 -1 O SER C 249 N TRP C 239
SSBOND 1 CYS A 6 CYS A 138 1555 1555 2.12
SSBOND 2 CYS A 83 CYS A 95 1555 1555 2.07
SSBOND 3 CYS A 273 CYS A 320 1555 1555 2.06
SSBOND 4 CYS B 6 CYS B 138 1555 1555 2.10
SSBOND 5 CYS B 83 CYS B 95 1555 1555 2.07
SSBOND 6 CYS B 273 CYS B 320 1555 1555 2.07
SSBOND 7 CYS C 6 CYS C 138 1555 1555 2.10
SSBOND 8 CYS C 83 CYS C 95 1555 1555 2.06
SSBOND 9 CYS C 273 CYS C 320 1555 1555 2.09
CISPEP 1 TYR A 217 PRO A 218 0 -0.52
CISPEP 2 PRO A 243 PRO A 244 0 0.37
CISPEP 3 TYR B 217 PRO B 218 0 -0.84
CISPEP 4 PRO B 243 PRO B 244 0 -0.58
CISPEP 5 TYR C 217 PRO C 218 0 -0.14
CISPEP 6 PRO C 243 PRO C 244 0 0.49
SITE 1 AC1 7 THR A 50 VAL A 51 SER A 156 TRP A 239
SITE 2 AC1 7 HOH A1012 HOH A1029 ARG C 62
SITE 1 AC2 6 THR B 50 VAL B 51 SER B 156 TRP B 239
SITE 2 AC2 6 HIS B 279 HOH B 523
SITE 1 AC3 7 ARG A 62 THR C 50 VAL C 51 SER C 156
SITE 2 AC3 7 HOH C 502 HOH C 520 HOH C 604
SITE 1 AC4 10 GLY A 91 ALA A 92 GLY A 93 GLY C 91
SITE 2 AC4 10 ALA C 92 GLY C 93 HOH C 559 HOH C 610
SITE 3 AC4 10 HOH C 624 HOH C 642
CRYST1 58.340 75.742 75.980 74.04 88.67 74.01 P 1 3
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 0.017141 -0.004912 0.001015 0.00000
SCALE2 0.000000 0.013734 -0.003997 0.00000
SCALE3 0.000000 0.000000 0.013711 0.00000
TER 2515 LYS A 330
TER 5030 LYS B 330
TER 7545 LYS C 330
MASTER 387 0 4 36 33 0 9 6 8396 3 38 78
END |