HEADER HYDROLASE 02-APR-09 3GXG
TITLE CRYSTAL STRUCTURE OF PUTATIVE PHOSPHATASE (DUF442) (YP_001181608.1)
TITLE 2 FROM SHEWANELLA PUTREFACIENS CN-32 AT 1.60 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE PHOSPHATASE (DUF442);
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SHEWANELLA PUTREFACIENS;
SOURCE 3 ORGANISM_TAXID: 319224;
SOURCE 4 STRAIN: CN-32;
SOURCE 5 GENE: SPUTCN32_0073, YP_001181608.1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS YP_001181608.1, PUTATIVE PHOSPHATASE (DUF442), STRUCTURAL GENOMICS,
KEYWDS 2 JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE
KEYWDS 3 INITIATIVE, PSI-2, TYROSINE PHOSPHATASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 5 01-FEB-23 3GXG 1 REMARK SEQADV
REVDAT 4 24-JUL-19 3GXG 1 REMARK LINK
REVDAT 3 25-OCT-17 3GXG 1 REMARK
REVDAT 2 13-JUL-11 3GXG 1 VERSN
REVDAT 1 07-JUL-09 3GXG 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF PUTATIVE PHOSPHATASE (DUF442)
JRNL TITL 2 (YP_001181608.1) FROM SHEWANELLA PUTREFACIENS CN-32 AT 1.60
JRNL TITL 3 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0053
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.64
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 106820
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) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.180
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5324
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7485
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE SET COUNT : 394
REMARK 3 BIN FREE R VALUE : 0.2830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4934
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 115
REMARK 3 SOLVENT ATOMS : 937
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.76
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.33000
REMARK 3 B22 (A**2) : 0.33000
REMARK 3 B33 (A**2) : -0.66000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.070
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.072
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.048
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.384
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.960
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5334 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3494 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7269 ; 1.474 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8655 ; 0.944 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 684 ; 5.403 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 267 ;34.201 ;26.704
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 894 ;11.202 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;15.702 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 779 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5972 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 932 ; 0.001 ; 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): 3248 ; 1.603 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1284 ; 0.468 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5232 ; 2.505 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2086 ; 4.190 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2005 ; 6.157 ;11.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. A MET-INHIBITION PROTOCOL WAS USED FOR
REMARK 3 SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE
REMARK 3 OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO
REMARK 3 0.85 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 3. CL, SO4, EDO AND ACT MODELED IS PRESENT IN
REMARK 3 CRYTALLIZATION OR CRYO SOLUTION.
REMARK 4
REMARK 4 3GXG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-09.
REMARK 100 THE DEPOSITION ID IS D_1000052427.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97843
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(111) BENT
REMARK 200 MONOCHROMATOR (HORIZONTAL
REMARK 200 FOCUSING)
REMARK 200 OPTICS : FLAT MIRROR (VERTICAL FOCUSING)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 106820
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 42.640
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6000
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) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.55100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX, SHELXD, AUTOSHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.26M (NH4)2SO4, 0.20M NACL, 0.1M
REMARK 280 ACETATE PH 4.5, NANODROP, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4
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 -Y,X,Z
REMARK 290 4555 Y,-X,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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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 300 REMARK: ANALYTICAL SIZE EXCLUSION CHROMATOGRAPHY SUPPORTS THE
REMARK 300 ASSIGNMENT OF A MONOMER AS A SIGNIFICANT OLIGOMERIZATION STATE
REMARK 300 IN SOLUTION
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 30400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 48700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -648.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 BIOMT1 2 -1.000000 0.000000 0.000000 111.22300
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 111.22300
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 111.22300
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 111.22300
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 82 NZ
REMARK 470 GLU C 25 CD OE1 OE2
REMARK 470 GLU D 25 CD OE1 OE2
REMARK 470 LYS D 74 CD CE NZ
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 OD2 ASP D 75 O HOH D 949 2.17
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 MSE A 148 SE MSE A 148 CE -0.363
REMARK 500 MSE B 148 SE MSE B 148 CE -0.375
REMARK 500 MSE C 148 SE MSE C 148 CE -0.412
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 GLY C 0 O - C - N ANGL. DEV. = -11.8 DEGREES
REMARK 500 GLY D 0 CA - C - N ANGL. DEV. = 13.3 DEGREES
REMARK 500 GLY D 0 O - C - N ANGL. DEV. = -13.4 DEGREES
REMARK 500 ASN D 23 C - N - CA ANGL. DEV. = 18.6 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 ASP A 79 76.79 -152.15
REMARK 500 ASN A 100 66.66 -159.85
REMARK 500 CYS A 125 -137.53 -146.93
REMARK 500 ASN A 156 -120.30 35.53
REMARK 500 ASP B 79 75.50 -151.40
REMARK 500 ASN B 100 62.65 -159.67
REMARK 500 CYS B 125 -137.89 -146.00
REMARK 500 MSE B 152 31.17 -97.99
REMARK 500 ASN B 156 -123.65 38.59
REMARK 500 ASP C 79 78.80 -154.90
REMARK 500 ASN C 100 64.35 -159.14
REMARK 500 CYS C 125 -135.92 -145.57
REMARK 500 MSE C 152 32.39 -98.12
REMARK 500 ASN C 156 -122.30 38.74
REMARK 500 ASN D 100 62.00 -160.97
REMARK 500 CYS D 125 -135.92 -144.52
REMARK 500 MSE D 152 31.38 -98.50
REMARK 500 ASN D 156 -125.93 39.53
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 GLY A 0 14.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 208
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 209
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 214
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 217
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 221
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 379
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 380
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 212
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 213
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 216
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 379
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 380
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 215
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 218
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 220
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 379
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 380
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 219
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 222
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 379
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 380
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 381
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 396500 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT (RESIDUES 23-178) WAS EXPRESSED WITH A PURIFICATION
REMARK 999 TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE
REMARK 999 LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
DBREF 3GXG A 23 178 UNP A4Y1H6 A4Y1H6_SHEPC 23 178
DBREF 3GXG B 23 178 UNP A4Y1H6 A4Y1H6_SHEPC 23 178
DBREF 3GXG C 23 178 UNP A4Y1H6 A4Y1H6_SHEPC 23 178
DBREF 3GXG D 23 178 UNP A4Y1H6 A4Y1H6_SHEPC 23 178
SEQADV 3GXG GLY A 0 UNP A4Y1H6 EXPRESSION TAG
SEQADV 3GXG GLY B 0 UNP A4Y1H6 EXPRESSION TAG
SEQADV 3GXG GLY C 0 UNP A4Y1H6 EXPRESSION TAG
SEQADV 3GXG GLY D 0 UNP A4Y1H6 EXPRESSION TAG
SEQRES 1 A 157 GLY ASN ILE GLU SER ILE GLU ASN LEU GLN GLY ILE ARG
SEQRES 2 A 157 ALA LEU GLN GLN GLN ALA PRO GLN LEU LEU SER SER GLY
SEQRES 3 A 157 LEU PRO ASN GLU GLN GLN PHE SER LEU LEU LYS GLN ALA
SEQRES 4 A 157 GLY VAL ASP VAL VAL ILE ASN LEU MSE PRO ASP SER SER
SEQRES 5 A 157 LYS ASP ALA HIS PRO ASP GLU GLY LYS LEU VAL THR GLN
SEQRES 6 A 157 ALA GLY MSE ASP TYR VAL TYR ILE PRO VAL ASP TRP GLN
SEQRES 7 A 157 ASN PRO LYS VAL GLU ASP VAL GLU ALA PHE PHE ALA ALA
SEQRES 8 A 157 MSE ASP GLN HIS LYS GLY LYS ASP VAL LEU VAL HIS CYS
SEQRES 9 A 157 LEU ALA ASN TYR ARG ALA SER ALA PHE ALA TYR LEU TYR
SEQRES 10 A 157 GLN LEU LYS GLN GLY GLN ASN PRO ASN MSE ALA GLN THR
SEQRES 11 A 157 MSE THR PRO TRP ASN ASP GLU LEU ALA ILE TYR PRO LYS
SEQRES 12 A 157 TRP GLN ALA LEU LEU THR GLU VAL SER ALA LYS TYR GLY
SEQRES 13 A 157 HIS
SEQRES 1 B 157 GLY ASN ILE GLU SER ILE GLU ASN LEU GLN GLY ILE ARG
SEQRES 2 B 157 ALA LEU GLN GLN GLN ALA PRO GLN LEU LEU SER SER GLY
SEQRES 3 B 157 LEU PRO ASN GLU GLN GLN PHE SER LEU LEU LYS GLN ALA
SEQRES 4 B 157 GLY VAL ASP VAL VAL ILE ASN LEU MSE PRO ASP SER SER
SEQRES 5 B 157 LYS ASP ALA HIS PRO ASP GLU GLY LYS LEU VAL THR GLN
SEQRES 6 B 157 ALA GLY MSE ASP TYR VAL TYR ILE PRO VAL ASP TRP GLN
SEQRES 7 B 157 ASN PRO LYS VAL GLU ASP VAL GLU ALA PHE PHE ALA ALA
SEQRES 8 B 157 MSE ASP GLN HIS LYS GLY LYS ASP VAL LEU VAL HIS CYS
SEQRES 9 B 157 LEU ALA ASN TYR ARG ALA SER ALA PHE ALA TYR LEU TYR
SEQRES 10 B 157 GLN LEU LYS GLN GLY GLN ASN PRO ASN MSE ALA GLN THR
SEQRES 11 B 157 MSE THR PRO TRP ASN ASP GLU LEU ALA ILE TYR PRO LYS
SEQRES 12 B 157 TRP GLN ALA LEU LEU THR GLU VAL SER ALA LYS TYR GLY
SEQRES 13 B 157 HIS
SEQRES 1 C 157 GLY ASN ILE GLU SER ILE GLU ASN LEU GLN GLY ILE ARG
SEQRES 2 C 157 ALA LEU GLN GLN GLN ALA PRO GLN LEU LEU SER SER GLY
SEQRES 3 C 157 LEU PRO ASN GLU GLN GLN PHE SER LEU LEU LYS GLN ALA
SEQRES 4 C 157 GLY VAL ASP VAL VAL ILE ASN LEU MSE PRO ASP SER SER
SEQRES 5 C 157 LYS ASP ALA HIS PRO ASP GLU GLY LYS LEU VAL THR GLN
SEQRES 6 C 157 ALA GLY MSE ASP TYR VAL TYR ILE PRO VAL ASP TRP GLN
SEQRES 7 C 157 ASN PRO LYS VAL GLU ASP VAL GLU ALA PHE PHE ALA ALA
SEQRES 8 C 157 MSE ASP GLN HIS LYS GLY LYS ASP VAL LEU VAL HIS CYS
SEQRES 9 C 157 LEU ALA ASN TYR ARG ALA SER ALA PHE ALA TYR LEU TYR
SEQRES 10 C 157 GLN LEU LYS GLN GLY GLN ASN PRO ASN MSE ALA GLN THR
SEQRES 11 C 157 MSE THR PRO TRP ASN ASP GLU LEU ALA ILE TYR PRO LYS
SEQRES 12 C 157 TRP GLN ALA LEU LEU THR GLU VAL SER ALA LYS TYR GLY
SEQRES 13 C 157 HIS
SEQRES 1 D 157 GLY ASN ILE GLU SER ILE GLU ASN LEU GLN GLY ILE ARG
SEQRES 2 D 157 ALA LEU GLN GLN GLN ALA PRO GLN LEU LEU SER SER GLY
SEQRES 3 D 157 LEU PRO ASN GLU GLN GLN PHE SER LEU LEU LYS GLN ALA
SEQRES 4 D 157 GLY VAL ASP VAL VAL ILE ASN LEU MSE PRO ASP SER SER
SEQRES 5 D 157 LYS ASP ALA HIS PRO ASP GLU GLY LYS LEU VAL THR GLN
SEQRES 6 D 157 ALA GLY MSE ASP TYR VAL TYR ILE PRO VAL ASP TRP GLN
SEQRES 7 D 157 ASN PRO LYS VAL GLU ASP VAL GLU ALA PHE PHE ALA ALA
SEQRES 8 D 157 MSE ASP GLN HIS LYS GLY LYS ASP VAL LEU VAL HIS CYS
SEQRES 9 D 157 LEU ALA ASN TYR ARG ALA SER ALA PHE ALA TYR LEU TYR
SEQRES 10 D 157 GLN LEU LYS GLN GLY GLN ASN PRO ASN MSE ALA GLN THR
SEQRES 11 D 157 MSE THR PRO TRP ASN ASP GLU LEU ALA ILE TYR PRO LYS
SEQRES 12 D 157 TRP GLN ALA LEU LEU THR GLU VAL SER ALA LYS TYR GLY
SEQRES 13 D 157 HIS
MODRES 3GXG MSE A 69 MET SELENOMETHIONINE
MODRES 3GXG MSE A 89 MET SELENOMETHIONINE
MODRES 3GXG MSE A 113 MET SELENOMETHIONINE
MODRES 3GXG MSE A 148 MET SELENOMETHIONINE
MODRES 3GXG MSE A 152 MET SELENOMETHIONINE
MODRES 3GXG MSE B 69 MET SELENOMETHIONINE
MODRES 3GXG MSE B 89 MET SELENOMETHIONINE
MODRES 3GXG MSE B 113 MET SELENOMETHIONINE
MODRES 3GXG MSE B 148 MET SELENOMETHIONINE
MODRES 3GXG MSE B 152 MET SELENOMETHIONINE
MODRES 3GXG MSE C 69 MET SELENOMETHIONINE
MODRES 3GXG MSE C 89 MET SELENOMETHIONINE
MODRES 3GXG MSE C 113 MET SELENOMETHIONINE
MODRES 3GXG MSE C 148 MET SELENOMETHIONINE
MODRES 3GXG MSE C 152 MET SELENOMETHIONINE
MODRES 3GXG MSE D 69 MET SELENOMETHIONINE
MODRES 3GXG MSE D 89 MET SELENOMETHIONINE
MODRES 3GXG MSE D 113 MET SELENOMETHIONINE
MODRES 3GXG MSE D 148 MET SELENOMETHIONINE
MODRES 3GXG MSE D 152 MET SELENOMETHIONINE
HET MSE A 69 8
HET MSE A 89 8
HET MSE A 113 8
HET MSE A 148 8
HET MSE A 152 8
HET MSE B 69 8
HET MSE B 89 8
HET MSE B 113 8
HET MSE B 148 8
HET MSE B 152 8
HET MSE C 69 8
HET MSE C 89 8
HET MSE C 113 8
HET MSE C 148 8
HET MSE C 152 8
HET MSE D 69 8
HET MSE D 89 8
HET MSE D 113 8
HET MSE D 148 8
HET MSE D 152 8
HET SO4 A 201 5
HET SO4 A 208 5
HET SO4 A 209 5
HET CL A 210 1
HET CL A 211 1
HET CL A 214 1
HET EDO A 217 4
HET EDO A 221 8
HET EDO A 379 4
HET ACT A 380 4
HET SO4 B 202 5
HET SO4 B 207 5
HET CL B 212 1
HET CL B 213 1
HET EDO B 216 4
HET EDO B 379 4
HET ACT B 380 4
HET SO4 C 203 5
HET SO4 C 205 5
HET CL C 215 1
HET EDO C 218 4
HET EDO C 220 4
HET EDO C 379 4
HET ACT C 380 4
HET SO4 D 204 5
HET SO4 D 206 5
HET EDO D 219 4
HET EDO D 222 4
HET EDO D 379 4
HET EDO D 380 4
HET ACT D 381 4
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM ACT ACETATE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 20(C5 H11 N O2 SE)
FORMUL 5 SO4 9(O4 S 2-)
FORMUL 8 CL 6(CL 1-)
FORMUL 11 EDO 12(C2 H6 O2)
FORMUL 14 ACT 4(C2 H3 O2 1-)
FORMUL 36 HOH *937(H2 O)
HELIX 1 1 SER A 26 GLN A 31 5 6
HELIX 2 2 ASN A 50 ALA A 60 1 11
HELIX 3 3 ASP A 79 ALA A 87 1 9
HELIX 4 4 LYS A 102 GLN A 115 1 14
HELIX 5 5 ASN A 128 GLN A 142 1 15
HELIX 6 6 ASN A 147 MSE A 152 1 6
HELIX 7 7 THR A 153 ASN A 156 5 4
HELIX 8 8 GLU A 158 ILE A 161 5 4
HELIX 9 9 TYR A 162 LYS A 175 1 14
HELIX 10 10 SER B 26 GLN B 31 5 6
HELIX 11 11 GLN B 53 ALA B 60 1 8
HELIX 12 12 ASP B 79 ALA B 87 1 9
HELIX 13 13 LYS B 102 GLN B 115 1 14
HELIX 14 14 ASN B 128 GLN B 142 1 15
HELIX 15 15 ASN B 147 MSE B 152 1 6
HELIX 16 16 THR B 153 ASN B 156 5 4
HELIX 17 17 GLU B 158 ILE B 161 5 4
HELIX 18 18 TYR B 162 LYS B 175 1 14
HELIX 19 19 SER C 26 GLN C 31 5 6
HELIX 20 20 ASN C 50 ALA C 60 1 11
HELIX 21 21 ASP C 79 ALA C 87 1 9
HELIX 22 22 LYS C 102 GLN C 115 1 14
HELIX 23 23 ASN C 128 GLN C 142 1 15
HELIX 24 24 ASN C 147 MSE C 152 1 6
HELIX 25 25 THR C 153 ASN C 156 5 4
HELIX 26 26 GLU C 158 ILE C 161 5 4
HELIX 27 27 TYR C 162 ALA C 174 1 13
HELIX 28 28 SER D 26 GLN D 31 5 6
HELIX 29 29 ASN D 50 ALA D 60 1 11
HELIX 30 30 ASP D 79 ALA D 87 1 9
HELIX 31 31 LYS D 102 GLN D 115 1 14
HELIX 32 32 ASN D 128 GLN D 142 1 15
HELIX 33 33 ASN D 147 MSE D 152 1 6
HELIX 34 34 THR D 153 ASN D 156 5 4
HELIX 35 35 GLU D 158 ILE D 161 5 4
HELIX 36 36 TYR D 162 LYS D 175 1 14
SHEET 1 A 5 GLN A 37 ALA A 40 0
SHEET 2 A 5 LEU A 43 SER A 46 -1 O SER A 45 N GLN A 37
SHEET 3 A 5 VAL A 121 HIS A 124 1 O VAL A 121 N LEU A 44
SHEET 4 A 5 VAL A 64 ASN A 67 1 N ILE A 66 O LEU A 122
SHEET 5 A 5 ASP A 90 TYR A 93 1 O ASP A 90 N VAL A 65
SHEET 1 B 5 GLN B 37 ALA B 40 0
SHEET 2 B 5 LEU B 43 SER B 46 -1 O SER B 45 N GLN B 37
SHEET 3 B 5 VAL B 121 HIS B 124 1 O VAL B 121 N LEU B 44
SHEET 4 B 5 VAL B 64 ASN B 67 1 N ILE B 66 O LEU B 122
SHEET 5 B 5 ASP B 90 TYR B 93 1 O VAL B 92 N ASN B 67
SHEET 1 C 5 GLN C 37 ALA C 40 0
SHEET 2 C 5 LEU C 43 SER C 46 -1 O SER C 45 N GLN C 37
SHEET 3 C 5 VAL C 121 HIS C 124 1 O VAL C 121 N LEU C 44
SHEET 4 C 5 VAL C 64 ASN C 67 1 N ILE C 66 O LEU C 122
SHEET 5 C 5 ASP C 90 TYR C 93 1 O VAL C 92 N VAL C 65
SHEET 1 D 5 GLN D 37 ALA D 40 0
SHEET 2 D 5 LEU D 43 SER D 46 -1 O SER D 45 N GLN D 37
SHEET 3 D 5 VAL D 121 HIS D 124 1 O VAL D 121 N LEU D 44
SHEET 4 D 5 VAL D 64 ASN D 67 1 N ILE D 66 O LEU D 122
SHEET 5 D 5 ASP D 90 TYR D 93 1 O VAL D 92 N ASN D 67
LINK C LEU A 68 N MSE A 69 1555 1555 1.33
LINK C MSE A 69 N PRO A 70 1555 1555 1.35
LINK C GLY A 88 N MSE A 89 1555 1555 1.32
LINK C MSE A 89 N ASP A 90 1555 1555 1.32
LINK C ALA A 112 N MSE A 113 1555 1555 1.34
LINK C MSE A 113 N ASP A 114 1555 1555 1.33
LINK C ASN A 147 N MSE A 148 1555 1555 1.33
LINK C MSE A 148 N ALA A 149 1555 1555 1.32
LINK C THR A 151 N MSE A 152 1555 1555 1.34
LINK C MSE A 152 N THR A 153 1555 1555 1.33
LINK C LEU B 68 N MSE B 69 1555 1555 1.34
LINK C MSE B 69 N PRO B 70 1555 1555 1.35
LINK C GLY B 88 N MSE B 89 1555 1555 1.33
LINK C MSE B 89 N ASP B 90 1555 1555 1.32
LINK C ALA B 112 N MSE B 113 1555 1555 1.33
LINK C MSE B 113 N ASP B 114 1555 1555 1.33
LINK C ASN B 147 N MSE B 148 1555 1555 1.33
LINK C MSE B 148 N ALA B 149 1555 1555 1.33
LINK C THR B 151 N MSE B 152 1555 1555 1.34
LINK C MSE B 152 N THR B 153 1555 1555 1.33
LINK C LEU C 68 N MSE C 69 1555 1555 1.33
LINK C MSE C 69 N PRO C 70 1555 1555 1.34
LINK C GLY C 88 N MSE C 89 1555 1555 1.33
LINK C MSE C 89 N ASP C 90 1555 1555 1.32
LINK C ALA C 112 N MSE C 113 1555 1555 1.34
LINK C MSE C 113 N ASP C 114 1555 1555 1.33
LINK C ASN C 147 N MSE C 148 1555 1555 1.33
LINK C MSE C 148 N ALA C 149 1555 1555 1.34
LINK C THR C 151 N MSE C 152 1555 1555 1.33
LINK C MSE C 152 N THR C 153 1555 1555 1.33
LINK C LEU D 68 N MSE D 69 1555 1555 1.34
LINK C MSE D 69 N PRO D 70 1555 1555 1.35
LINK C GLY D 88 N MSE D 89 1555 1555 1.34
LINK C MSE D 89 N ASP D 90 1555 1555 1.32
LINK C ALA D 112 N MSE D 113 1555 1555 1.33
LINK C MSE D 113 N ASP D 114 1555 1555 1.33
LINK C ASN D 147 N MSE D 148 1555 1555 1.32
LINK C MSE D 148 N ALA D 149 1555 1555 1.32
LINK C THR D 151 N MSE D 152 1555 1555 1.33
LINK C MSE D 152 N THR D 153 1555 1555 1.34
SITE 1 AC1 8 CYS A 125 LEU A 126 ALA A 127 ASN A 128
SITE 2 AC1 8 TYR A 129 ARG A 130 HOH A 414 HOH A 418
SITE 1 AC2 6 ARG A 34 ALA A 35 ALA A 127 ASN A 145
SITE 2 AC2 6 HOH A 618 HOH A1092
SITE 1 AC3 8 ASN A 23 PRO A 41 HOH A 821 HOH A 892
SITE 2 AC3 8 HOH A 897 ASN B 23 PRO B 41 HOH B 481
SITE 1 AC4 2 GLN A 53 HOH B 453
SITE 1 AC5 3 ASN A 147 THR A 151 HOH A 943
SITE 1 AC6 3 LYS A 164 ALA A 174 HOH A 518
SITE 1 AC7 7 PRO A 70 ASP A 71 SER A 72 TYR A 93
SITE 2 AC7 7 HOH A 789 HOH A 957 HOH A 981
SITE 1 AC8 6 ASN A 50 GLU A 51 HIS A 77 HOH A 647
SITE 2 AC8 6 HOH A1086 LYS C 58
SITE 1 AC9 7 PRO A 101 GLU A 171 HOH A 388 HOH A 399
SITE 2 AC9 7 HOH A 403 ALA B 174 HOH B1157
SITE 1 BC1 7 ALA A 149 MSE A 152 ASP A 157 HOH A 401
SITE 2 BC1 7 HOH A 638 HOH A1018 HOH A1109
SITE 1 BC2 8 CYS B 125 LEU B 126 ALA B 127 ASN B 128
SITE 2 BC2 8 TYR B 129 ARG B 130 HOH B 420 HOH B 421
SITE 1 BC3 5 ARG B 34 ALA B 127 ASN B 145 HOH B 551
SITE 2 BC3 5 HOH B1035
SITE 1 BC4 2 ASN B 50 GLU B 51
SITE 1 BC5 2 ASN B 147 THR B 151
SITE 1 BC6 5 ASP B 71 SER B 72 TYR B 93 HOH B 719
SITE 2 BC6 5 HOH B 806
SITE 1 BC7 9 ALA A 174 HOH A 507 HOH A1159 PRO B 101
SITE 2 BC7 9 LYS B 102 GLU B 171 HOH B 396 HOH B 406
SITE 3 BC7 9 HOH B 422
SITE 1 BC8 5 MSE B 152 ASP B 157 HOH B 432 HOH B 698
SITE 2 BC8 5 HOH B 711
SITE 1 BC9 8 CYS C 125 LEU C 126 ALA C 127 ASN C 128
SITE 2 BC9 8 TYR C 129 ARG C 130 HOH C 386 HOH C 419
SITE 1 CC1 7 ARG C 34 ALA C 35 ALA C 127 ASN C 145
SITE 2 CC1 7 HOH C 515 HOH C 740 HOH C 985
SITE 1 CC2 3 LYS C 164 ALA C 174 HOH C 411
SITE 1 CC3 5 ASP C 71 SER C 72 TYR C 93 HOH C 695
SITE 2 CC3 5 HOH C 798
SITE 1 CC4 7 PRO C 101 LYS C 102 GLU C 171 HOH C 382
SITE 2 CC4 7 HOH C 387 HOH C 459 ALA D 174
SITE 1 CC5 5 ASN C 147 GLN C 150 THR C 151 HOH C 598
SITE 2 CC5 5 HOH C 962
SITE 1 CC6 5 ALA C 149 MSE C 152 ASP C 157 HOH C 414
SITE 2 CC6 5 HOH C 750
SITE 1 CC7 8 CYS D 125 LEU D 126 ALA D 127 ASN D 128
SITE 2 CC7 8 TYR D 129 ARG D 130 HOH D 426 HOH D 428
SITE 1 CC8 6 ARG D 34 ALA D 35 ALA D 127 ASN D 145
SITE 2 CC8 6 HOH D 600 HOH D1101
SITE 1 CC9 5 ASP D 71 SER D 72 TYR D 93 HOH D 633
SITE 2 CC9 5 HOH D 960
SITE 1 DC1 6 ASN D 50 GLU D 51 HIS D 77 HOH D 457
SITE 2 DC1 6 HOH D1051 HOH D1141
SITE 1 DC2 6 ALA C 174 PRO D 101 LEU D 168 GLU D 171
SITE 2 DC2 6 HOH D 390 HOH D 463
SITE 1 DC3 5 GLN D 37 GLN D 38 GLN D 39 HOH D 706
SITE 2 DC3 5 HOH D 886
SITE 1 DC4 5 ALA D 149 MSE D 152 ASP D 157 HOH D 415
SITE 2 DC4 5 HOH D1017
CRYST1 111.223 111.223 66.380 90.00 90.00 90.00 P 4 16
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 0.008991 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008991 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015065 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
