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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 28-MAR-07 2PBL
TITLE CRYSTAL STRUCTURE OF PUTATIVE THIOESTERASE (YP_614486.1)
TITLE 2 FROM SILICIBACTER SP. TM1040 AT 1.79 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ESTERASE/LIPASE/THIOESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SILICIBACTER SP. TM1040;
SOURCE 3 ORGANISM_TAXID: 292414;
SOURCE 4 STRAIN: TM1040;
SOURCE 5 GENE: YP_614486.1, TM1040_2492;
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_614486.1, PUTATIVE THIOESTERASE, STRUCTURAL GENOMICS,
KEYWDS 2 JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN
KEYWDS 3 STRUCTURE INITIATIVE, PSI-2, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 2 24-FEB-09 2PBL 1 VERSN
REVDAT 1 17-APR-07 2PBL 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF PUTATIVE THIOESTERASE
JRNL TITL 2 (YP_614486.1) FROM SILICIBACTER SP. TM1040 AT 1.79
JRNL TITL 3 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.79 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.79
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 93699
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) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4700
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) : 1.79
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.84
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6562
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94
REMARK 3 BIN R VALUE (WORKING SET) : 0.3490
REMARK 3 BIN FREE R VALUE SET COUNT : 333
REMARK 3 BIN FREE R VALUE : 0.4210
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8131
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 51
REMARK 3 SOLVENT ATOMS : 1310
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.53
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.35000
REMARK 3 B22 (A**2) : -1.40000
REMARK 3 B33 (A**2) : 0.79000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.33000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.174
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.161
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.120
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.928
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8402 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 7547 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11482 ; 1.710 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 17460 ; 1.014 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1066 ; 4.279 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 376 ;35.609 ;23.777
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1249 ;10.280 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 53 ;16.333 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1245 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9609 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1744 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1891 ; 0.212 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 8188 ; 0.176 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4253 ; 0.180 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): 4656 ; 0.088 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1650 ; 0.229 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.031 ; 0.500
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.156 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 11 ; 0.203 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 78 ; 0.241 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 44 ; 0.257 ; 0.500
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): 5440 ; 1.997 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2134 ; 0.789 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8494 ; 2.793 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3454 ; 5.298 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2988 ; 6.855 ;11.000
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 0 A 5 3
REMARK 3 1 B 0 B 5 3
REMARK 3 1 C 0 C 5 3
REMARK 3 1 D 0 D 5 3
REMARK 3 2 A 6 A 261 5
REMARK 3 2 B 6 B 261 5
REMARK 3 2 C 6 C 261 5
REMARK 3 2 D 6 D 261 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 34 ; 0.030 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 B (A): 34 ; 0.030 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 C (A): 34 ; 0.030 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 D (A): 34 ; 0.040 ; 0.050
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1485 ; 0.170 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 B (A): 1485 ; 0.170 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 C (A): 1485 ; 0.190 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 D (A): 1485 ; 0.170 ; 0.500
REMARK 3 LOOSE POSITIONAL 1 A (A): 2287 ; 0.360 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 B (A): 2287 ; 0.360 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 C (A): 2287 ; 0.480 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 D (A): 2287 ; 0.370 ; 5.000
REMARK 3 TIGHT THERMAL 1 A (A**2): 34 ; 0.150 ; 0.500
REMARK 3 TIGHT THERMAL 1 B (A**2): 34 ; 0.100 ; 0.500
REMARK 3 TIGHT THERMAL 1 C (A**2): 34 ; 0.100 ; 0.500
REMARK 3 TIGHT THERMAL 1 D (A**2): 34 ; 0.120 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1485 ; 1.200 ; 2.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 1485 ; 1.140 ; 2.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 1485 ; 1.180 ; 2.000
REMARK 3 MEDIUM THERMAL 1 D (A**2): 1485 ; 1.150 ; 2.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 2287 ; 2.170 ;10.000
REMARK 3 LOOSE THERMAL 1 B (A**2): 2287 ; 2.260 ;10.000
REMARK 3 LOOSE THERMAL 1 C (A**2): 2287 ; 2.210 ;10.000
REMARK 3 LOOSE THERMAL 1 D (A**2): 2287 ; 2.270 ;10.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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. ATOM RECORD CONTAINS RESIDUAL B FACTORS
REMARK 3 ONLY. 3. 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 0.75 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO
REMARK 3 PARTIAL S-MET INCORPORATION. 4. ONE MG ATOM AND FOUR CHLORIDE
REMARK 3 IONS FROM CRYSTALLIZATION WERE MODELED INTO THE STRUCTURE. 5.
REMARK 3 ONE P-NITROBENZENE-LIKE UNKNOWN LIGAND IS MODELED NEAR TO HIS
REMARK 3 135 IN EACH SUBUNIT. 6. PHOSPHATE IONS ARE MODELED IN THE
REMARK 3 UNKNOWN ELECTRON DENSITY NEAR GLU 149 IN EACH SUBUNIT.
REMARK 4
REMARK 4 2PBL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-07.
REMARK 100 THE RCSB ID CODE IS RCSB042195.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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) : 0.97937, 0.91837, 0.97910
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(111) BENT
REMARK 200 (HORIZONTAL FOCUSING)
REMARK 200 OPTICS : FLAT MIRROR (VERTICAL
REMARK 200 FOCUSING)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93727
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.790
REMARK 200 RESOLUTION RANGE LOW (A) : 29.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.10800
REMARK 200 R SYM (I) : 0.10800
REMARK 200 FOR THE DATA SET : 4.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.65300
REMARK 200 R SYM FOR SHELL (I) : 0.65300
REMARK 200 FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXD, AUTOSHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NANODROP, 0.2M MGCL2, 30.0% PEG
REMARK 280 4000, 0.1M TRIS-HCL PH 8.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 37.21900
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 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 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 MSE A 1 CG SE CE
REMARK 470 GLU A 2 CD OE1 OE2
REMARK 470 ASP A 36 CG OD1 OD2
REMARK 470 MSE B 1 CG SE CE
REMARK 470 GLU B 28 OE1 OE2
REMARK 470 GLU B 153 CD OE1 OE2
REMARK 470 MSE C 1 CG SE CE
REMARK 470 GLU C 14 CG CD OE1 OE2
REMARK 470 ASP C 36 CG OD1 OD2
REMARK 470 GLU C 58 CD OE1 OE2
REMARK 470 GLU C 246 CD OE1 OE2
REMARK 470 MSE D 1 CG SE CE
REMARK 470 GLU D 28 CD OE1 OE2
REMARK 470 GLN D 35 CG CD OE1 NE2
REMARK 470 GLU D 58 CG CD OE1 OE2
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 ASP D 203 O HOH D 269 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 144 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 144 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG C 201 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG D 37 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG D 49 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN A 35 -133.01 56.25
REMARK 500 PHE A 76 163.35 70.82
REMARK 500 SER A 136 -119.06 67.10
REMARK 500 GLU A 238 16.44 57.14
REMARK 500 GLN B 35 -130.93 57.88
REMARK 500 PHE B 76 171.76 68.48
REMARK 500 SER B 136 -110.46 65.78
REMARK 500 ALA B 204 147.24 -179.44
REMARK 500 PHE B 237 117.37 -38.72
REMARK 500 GLU B 238 15.10 56.34
REMARK 500 GLN C 35 -105.55 54.85
REMARK 500 PHE C 76 172.85 73.27
REMARK 500 SER C 136 -117.36 69.10
REMARK 500 ASP C 203 27.00 -79.90
REMARK 500 GLN D 35 -120.21 47.21
REMARK 500 PHE D 76 165.51 70.53
REMARK 500 SER D 136 -116.63 65.96
REMARK 500 ALA D 204 147.80 -176.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 262 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 322 O
REMARK 620 2 HOH D 267 O 80.1
REMARK 620 3 HOH D 275 O 97.4 144.4
REMARK 620 4 HOH B 327 O 101.2 100.0 115.2
REMARK 620 5 HOH D 264 O 75.5 74.3 70.8 173.7
REMARK 620 6 HOH D 269 O 149.5 79.0 87.0 104.2 77.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 262
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 262
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 262
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 263
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 262
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 264
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 263
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL A 263
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL B 265
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL C 264
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL D 263
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 371276 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE
REMARK 999 LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
DBREF 2PBL A 1 261 UNP Q1GDP2 Q1GDP2_SILST 1 261
DBREF 2PBL B 1 261 UNP Q1GDP2 Q1GDP2_SILST 1 261
DBREF 2PBL C 1 261 UNP Q1GDP2 Q1GDP2_SILST 1 261
DBREF 2PBL D 1 261 UNP Q1GDP2 Q1GDP2_SILST 1 261
SEQADV 2PBL GLY A 0 UNP Q1GDP2 LEADER SEQUENCE
SEQADV 2PBL MSE A 1 UNP Q1GDP2 MET 1 MODIFIED RESIDUE
SEQADV 2PBL MSE A 74 UNP Q1GDP2 MET 74 MODIFIED RESIDUE
SEQADV 2PBL MSE A 97 UNP Q1GDP2 MET 97 MODIFIED RESIDUE
SEQADV 2PBL MSE A 145 UNP Q1GDP2 MET 145 MODIFIED RESIDUE
SEQADV 2PBL MSE A 179 UNP Q1GDP2 MET 179 MODIFIED RESIDUE
SEQADV 2PBL MSE A 185 UNP Q1GDP2 MET 185 MODIFIED RESIDUE
SEQADV 2PBL MSE A 198 UNP Q1GDP2 MET 198 MODIFIED RESIDUE
SEQADV 2PBL GLY B 0 UNP Q1GDP2 LEADER SEQUENCE
SEQADV 2PBL MSE B 1 UNP Q1GDP2 MET 1 MODIFIED RESIDUE
SEQADV 2PBL MSE B 74 UNP Q1GDP2 MET 74 MODIFIED RESIDUE
SEQADV 2PBL MSE B 97 UNP Q1GDP2 MET 97 MODIFIED RESIDUE
SEQADV 2PBL MSE B 145 UNP Q1GDP2 MET 145 MODIFIED RESIDUE
SEQADV 2PBL MSE B 179 UNP Q1GDP2 MET 179 MODIFIED RESIDUE
SEQADV 2PBL MSE B 185 UNP Q1GDP2 MET 185 MODIFIED RESIDUE
SEQADV 2PBL MSE B 198 UNP Q1GDP2 MET 198 MODIFIED RESIDUE
SEQADV 2PBL GLY C 0 UNP Q1GDP2 LEADER SEQUENCE
SEQADV 2PBL MSE C 1 UNP Q1GDP2 MET 1 MODIFIED RESIDUE
SEQADV 2PBL MSE C 74 UNP Q1GDP2 MET 74 MODIFIED RESIDUE
SEQADV 2PBL MSE C 97 UNP Q1GDP2 MET 97 MODIFIED RESIDUE
SEQADV 2PBL MSE C 145 UNP Q1GDP2 MET 145 MODIFIED RESIDUE
SEQADV 2PBL MSE C 179 UNP Q1GDP2 MET 179 MODIFIED RESIDUE
SEQADV 2PBL MSE C 185 UNP Q1GDP2 MET 185 MODIFIED RESIDUE
SEQADV 2PBL MSE C 198 UNP Q1GDP2 MET 198 MODIFIED RESIDUE
SEQADV 2PBL GLY D 0 UNP Q1GDP2 LEADER SEQUENCE
SEQADV 2PBL MSE D 1 UNP Q1GDP2 MET 1 MODIFIED RESIDUE
SEQADV 2PBL MSE D 74 UNP Q1GDP2 MET 74 MODIFIED RESIDUE
SEQADV 2PBL MSE D 97 UNP Q1GDP2 MET 97 MODIFIED RESIDUE
SEQADV 2PBL MSE D 145 UNP Q1GDP2 MET 145 MODIFIED RESIDUE
SEQADV 2PBL MSE D 179 UNP Q1GDP2 MET 179 MODIFIED RESIDUE
SEQADV 2PBL MSE D 185 UNP Q1GDP2 MET 185 MODIFIED RESIDUE
SEQADV 2PBL MSE D 198 UNP Q1GDP2 MET 198 MODIFIED RESIDUE
SEQRES 1 A 262 GLY MSE GLU LEU ASP ASP ALA TYR ALA ASN GLY ALA TYR
SEQRES 2 A 262 ILE GLU GLY ALA ALA ASP TYR PRO PRO ARG TRP ALA ALA
SEQRES 3 A 262 SER ALA GLU ASP PHE ARG ASN SER LEU GLN ASP ARG ALA
SEQRES 4 A 262 ARG LEU ASN LEU SER TYR GLY GLU GLY ASP ARG HIS LYS
SEQRES 5 A 262 PHE ASP LEU PHE LEU PRO GLU GLY THR PRO VAL GLY LEU
SEQRES 6 A 262 PHE VAL PHE VAL HIS GLY GLY TYR TRP MSE ALA PHE ASP
SEQRES 7 A 262 LYS SER SER TRP SER HIS LEU ALA VAL GLY ALA LEU SER
SEQRES 8 A 262 LYS GLY TRP ALA VAL ALA MSE PRO SER TYR GLU LEU CYS
SEQRES 9 A 262 PRO GLU VAL ARG ILE SER GLU ILE THR GLN GLN ILE SER
SEQRES 10 A 262 GLN ALA VAL THR ALA ALA ALA LYS GLU ILE ASP GLY PRO
SEQRES 11 A 262 ILE VAL LEU ALA GLY HIS SER ALA GLY GLY HIS LEU VAL
SEQRES 12 A 262 ALA ARG MSE LEU ASP PRO GLU VAL LEU PRO GLU ALA VAL
SEQRES 13 A 262 GLY ALA ARG ILE ARG ASN VAL VAL PRO ILE SER PRO LEU
SEQRES 14 A 262 SER ASP LEU ARG PRO LEU LEU ARG THR SER MSE ASN GLU
SEQRES 15 A 262 LYS PHE LYS MSE ASP ALA ASP ALA ALA ILE ALA GLU SER
SEQRES 16 A 262 PRO VAL GLU MSE GLN ASN ARG TYR ASP ALA LYS VAL THR
SEQRES 17 A 262 VAL TRP VAL GLY GLY ALA GLU ARG PRO ALA PHE LEU ASP
SEQRES 18 A 262 GLN ALA ILE TRP LEU VAL GLU ALA TRP ASP ALA ASP HIS
SEQRES 19 A 262 VAL ILE ALA PHE GLU LYS HIS HIS PHE ASN VAL ILE GLU
SEQRES 20 A 262 PRO LEU ALA ASP PRO GLU SER ASP LEU VAL ALA VAL ILE
SEQRES 21 A 262 THR ALA
SEQRES 1 B 262 GLY MSE GLU LEU ASP ASP ALA TYR ALA ASN GLY ALA TYR
SEQRES 2 B 262 ILE GLU GLY ALA ALA ASP TYR PRO PRO ARG TRP ALA ALA
SEQRES 3 B 262 SER ALA GLU ASP PHE ARG ASN SER LEU GLN ASP ARG ALA
SEQRES 4 B 262 ARG LEU ASN LEU SER TYR GLY GLU GLY ASP ARG HIS LYS
SEQRES 5 B 262 PHE ASP LEU PHE LEU PRO GLU GLY THR PRO VAL GLY LEU
SEQRES 6 B 262 PHE VAL PHE VAL HIS GLY GLY TYR TRP MSE ALA PHE ASP
SEQRES 7 B 262 LYS SER SER TRP SER HIS LEU ALA VAL GLY ALA LEU SER
SEQRES 8 B 262 LYS GLY TRP ALA VAL ALA MSE PRO SER TYR GLU LEU CYS
SEQRES 9 B 262 PRO GLU VAL ARG ILE SER GLU ILE THR GLN GLN ILE SER
SEQRES 10 B 262 GLN ALA VAL THR ALA ALA ALA LYS GLU ILE ASP GLY PRO
SEQRES 11 B 262 ILE VAL LEU ALA GLY HIS SER ALA GLY GLY HIS LEU VAL
SEQRES 12 B 262 ALA ARG MSE LEU ASP PRO GLU VAL LEU PRO GLU ALA VAL
SEQRES 13 B 262 GLY ALA ARG ILE ARG ASN VAL VAL PRO ILE SER PRO LEU
SEQRES 14 B 262 SER ASP LEU ARG PRO LEU LEU ARG THR SER MSE ASN GLU
SEQRES 15 B 262 LYS PHE LYS MSE ASP ALA ASP ALA ALA ILE ALA GLU SER
SEQRES 16 B 262 PRO VAL GLU MSE GLN ASN ARG TYR ASP ALA LYS VAL THR
SEQRES 17 B 262 VAL TRP VAL GLY GLY ALA GLU ARG PRO ALA PHE LEU ASP
SEQRES 18 B 262 GLN ALA ILE TRP LEU VAL GLU ALA TRP ASP ALA ASP HIS
SEQRES 19 B 262 VAL ILE ALA PHE GLU LYS HIS HIS PHE ASN VAL ILE GLU
SEQRES 20 B 262 PRO LEU ALA ASP PRO GLU SER ASP LEU VAL ALA VAL ILE
SEQRES 21 B 262 THR ALA
SEQRES 1 C 262 GLY MSE GLU LEU ASP ASP ALA TYR ALA ASN GLY ALA TYR
SEQRES 2 C 262 ILE GLU GLY ALA ALA ASP TYR PRO PRO ARG TRP ALA ALA
SEQRES 3 C 262 SER ALA GLU ASP PHE ARG ASN SER LEU GLN ASP ARG ALA
SEQRES 4 C 262 ARG LEU ASN LEU SER TYR GLY GLU GLY ASP ARG HIS LYS
SEQRES 5 C 262 PHE ASP LEU PHE LEU PRO GLU GLY THR PRO VAL GLY LEU
SEQRES 6 C 262 PHE VAL PHE VAL HIS GLY GLY TYR TRP MSE ALA PHE ASP
SEQRES 7 C 262 LYS SER SER TRP SER HIS LEU ALA VAL GLY ALA LEU SER
SEQRES 8 C 262 LYS GLY TRP ALA VAL ALA MSE PRO SER TYR GLU LEU CYS
SEQRES 9 C 262 PRO GLU VAL ARG ILE SER GLU ILE THR GLN GLN ILE SER
SEQRES 10 C 262 GLN ALA VAL THR ALA ALA ALA LYS GLU ILE ASP GLY PRO
SEQRES 11 C 262 ILE VAL LEU ALA GLY HIS SER ALA GLY GLY HIS LEU VAL
SEQRES 12 C 262 ALA ARG MSE LEU ASP PRO GLU VAL LEU PRO GLU ALA VAL
SEQRES 13 C 262 GLY ALA ARG ILE ARG ASN VAL VAL PRO ILE SER PRO LEU
SEQRES 14 C 262 SER ASP LEU ARG PRO LEU LEU ARG THR SER MSE ASN GLU
SEQRES 15 C 262 LYS PHE LYS MSE ASP ALA ASP ALA ALA ILE ALA GLU SER
SEQRES 16 C 262 PRO VAL GLU MSE GLN ASN ARG TYR ASP ALA LYS VAL THR
SEQRES 17 C 262 VAL TRP VAL GLY GLY ALA GLU ARG PRO ALA PHE LEU ASP
SEQRES 18 C 262 GLN ALA ILE TRP LEU VAL GLU ALA TRP ASP ALA ASP HIS
SEQRES 19 C 262 VAL ILE ALA PHE GLU LYS HIS HIS PHE ASN VAL ILE GLU
SEQRES 20 C 262 PRO LEU ALA ASP PRO GLU SER ASP LEU VAL ALA VAL ILE
SEQRES 21 C 262 THR ALA
SEQRES 1 D 262 GLY MSE GLU LEU ASP ASP ALA TYR ALA ASN GLY ALA TYR
SEQRES 2 D 262 ILE GLU GLY ALA ALA ASP TYR PRO PRO ARG TRP ALA ALA
SEQRES 3 D 262 SER ALA GLU ASP PHE ARG ASN SER LEU GLN ASP ARG ALA
SEQRES 4 D 262 ARG LEU ASN LEU SER TYR GLY GLU GLY ASP ARG HIS LYS
SEQRES 5 D 262 PHE ASP LEU PHE LEU PRO GLU GLY THR PRO VAL GLY LEU
SEQRES 6 D 262 PHE VAL PHE VAL HIS GLY GLY TYR TRP MSE ALA PHE ASP
SEQRES 7 D 262 LYS SER SER TRP SER HIS LEU ALA VAL GLY ALA LEU SER
SEQRES 8 D 262 LYS GLY TRP ALA VAL ALA MSE PRO SER TYR GLU LEU CYS
SEQRES 9 D 262 PRO GLU VAL ARG ILE SER GLU ILE THR GLN GLN ILE SER
SEQRES 10 D 262 GLN ALA VAL THR ALA ALA ALA LYS GLU ILE ASP GLY PRO
SEQRES 11 D 262 ILE VAL LEU ALA GLY HIS SER ALA GLY GLY HIS LEU VAL
SEQRES 12 D 262 ALA ARG MSE LEU ASP PRO GLU VAL LEU PRO GLU ALA VAL
SEQRES 13 D 262 GLY ALA ARG ILE ARG ASN VAL VAL PRO ILE SER PRO LEU
SEQRES 14 D 262 SER ASP LEU ARG PRO LEU LEU ARG THR SER MSE ASN GLU
SEQRES 15 D 262 LYS PHE LYS MSE ASP ALA ASP ALA ALA ILE ALA GLU SER
SEQRES 16 D 262 PRO VAL GLU MSE GLN ASN ARG TYR ASP ALA LYS VAL THR
SEQRES 17 D 262 VAL TRP VAL GLY GLY ALA GLU ARG PRO ALA PHE LEU ASP
SEQRES 18 D 262 GLN ALA ILE TRP LEU VAL GLU ALA TRP ASP ALA ASP HIS
SEQRES 19 D 262 VAL ILE ALA PHE GLU LYS HIS HIS PHE ASN VAL ILE GLU
SEQRES 20 D 262 PRO LEU ALA ASP PRO GLU SER ASP LEU VAL ALA VAL ILE
SEQRES 21 D 262 THR ALA
MODRES 2PBL MSE A 1 MET SELENOMETHIONINE
MODRES 2PBL MSE A 74 MET SELENOMETHIONINE
MODRES 2PBL MSE A 97 MET SELENOMETHIONINE
MODRES 2PBL MSE A 145 MET SELENOMETHIONINE
MODRES 2PBL MSE A 179 MET SELENOMETHIONINE
MODRES 2PBL MSE A 185 MET SELENOMETHIONINE
MODRES 2PBL MSE A 198 MET SELENOMETHIONINE
MODRES 2PBL MSE B 1 MET SELENOMETHIONINE
MODRES 2PBL MSE B 74 MET SELENOMETHIONINE
MODRES 2PBL MSE B 97 MET SELENOMETHIONINE
MODRES 2PBL MSE B 145 MET SELENOMETHIONINE
MODRES 2PBL MSE B 179 MET SELENOMETHIONINE
MODRES 2PBL MSE B 185 MET SELENOMETHIONINE
MODRES 2PBL MSE B 198 MET SELENOMETHIONINE
MODRES 2PBL MSE C 1 MET SELENOMETHIONINE
MODRES 2PBL MSE C 74 MET SELENOMETHIONINE
MODRES 2PBL MSE C 97 MET SELENOMETHIONINE
MODRES 2PBL MSE C 145 MET SELENOMETHIONINE
MODRES 2PBL MSE C 179 MET SELENOMETHIONINE
MODRES 2PBL MSE C 185 MET SELENOMETHIONINE
MODRES 2PBL MSE C 198 MET SELENOMETHIONINE
MODRES 2PBL MSE D 1 MET SELENOMETHIONINE
MODRES 2PBL MSE D 74 MET SELENOMETHIONINE
MODRES 2PBL MSE D 97 MET SELENOMETHIONINE
MODRES 2PBL MSE D 145 MET SELENOMETHIONINE
MODRES 2PBL MSE D 179 MET SELENOMETHIONINE
MODRES 2PBL MSE D 185 MET SELENOMETHIONINE
MODRES 2PBL MSE D 198 MET SELENOMETHIONINE
HET MSE A 1 5
HET MSE A 74 8
HET MSE A 97 8
HET MSE A 145 8
HET MSE A 179 8
HET MSE A 185 8
HET MSE A 198 8
HET MSE B 1 5
HET MSE B 74 8
HET MSE B 97 8
HET MSE B 145 8
HET MSE B 179 8
HET MSE B 185 8
HET MSE B 198 8
HET MSE C 1 5
HET MSE C 74 8
HET MSE C 97 8
HET MSE C 145 8
HET MSE C 179 8
HET MSE C 185 8
HET MSE C 198 8
HET MSE D 1 5
HET MSE D 74 8
HET MSE D 97 8
HET MSE D 145 8
HET MSE D 179 8
HET MSE D 185 8
HET MSE D 198 8
HET MG B 262 1
HET CL A 262 1
HET CL C 262 1
HET CL B 263 1
HET CL D 262 1
HET PO4 B 264 5
HET PO4 C 263 5
HET UNL A 263 9
HET UNL B 265 9
HET UNL C 264 9
HET UNL D 263 9
HETNAM MSE SELENOMETHIONINE
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM PO4 PHOSPHATE ION
HETNAM UNL UNKNOWN LIGAND
FORMUL 1 MSE 28(C5 H11 N O2 SE)
FORMUL 5 MG MG 2+
FORMUL 6 CL 4(CL 1-)
FORMUL 10 PO4 2(O4 P 3-)
FORMUL 16 HOH *1310(H2 O)
HELIX 1 1 ASN A 9 ILE A 13 5 5
HELIX 2 2 GLY A 15 ALA A 17 5 3
HELIX 3 3 ASP A 18 GLN A 35 1 18
HELIX 4 4 ASP A 77 LEU A 84 5 8
HELIX 5 5 ALA A 85 LYS A 91 1 7
HELIX 6 6 ARG A 107 ILE A 126 1 20
HELIX 7 7 SER A 136 MSE A 145 1 10
HELIX 8 8 PRO A 152 ALA A 157 1 6
HELIX 9 9 LEU A 171 SER A 178 5 8
HELIX 10 10 MSE A 179 LYS A 184 1 6
HELIX 11 11 ASP A 186 GLU A 193 1 8
HELIX 12 12 SER A 194 MSE A 198 5 5
HELIX 13 13 ARG A 215 ASP A 230 1 16
HELIX 14 14 ILE A 245 ASP A 250 5 6
HELIX 15 15 SER A 253 ALA A 261 1 9
HELIX 16 16 ASN B 9 ILE B 13 5 5
HELIX 17 17 GLY B 15 ALA B 17 5 3
HELIX 18 18 ASP B 18 GLN B 35 1 18
HELIX 19 19 ASP B 77 LEU B 84 5 8
HELIX 20 20 ALA B 85 LYS B 91 1 7
HELIX 21 21 ARG B 107 ILE B 126 1 20
HELIX 22 22 SER B 136 MSE B 145 1 10
HELIX 23 23 PRO B 152 ALA B 157 1 6
HELIX 24 24 LEU B 171 SER B 178 5 8
HELIX 25 25 MSE B 179 LYS B 184 1 6
HELIX 26 26 ASP B 186 GLU B 193 1 8
HELIX 27 27 SER B 194 MSE B 198 5 5
HELIX 28 28 ARG B 215 ASP B 230 1 16
HELIX 29 29 ILE B 245 ASP B 250 5 6
HELIX 30 30 SER B 253 ALA B 261 1 9
HELIX 31 31 ASP C 4 ALA C 8 5 5
HELIX 32 32 GLY C 15 ALA C 17 5 3
HELIX 33 33 ASP C 18 GLN C 35 1 18
HELIX 34 34 ASP C 77 LEU C 84 5 8
HELIX 35 35 ALA C 85 SER C 90 1 6
HELIX 36 36 ARG C 107 ILE C 126 1 20
HELIX 37 37 SER C 136 MSE C 145 1 10
HELIX 38 38 PRO C 152 ALA C 157 1 6
HELIX 39 39 LEU C 171 SER C 178 5 8
HELIX 40 40 MSE C 179 LYS C 184 1 6
HELIX 41 41 ASP C 186 GLU C 193 1 8
HELIX 42 42 SER C 194 MSE C 198 5 5
HELIX 43 43 ARG C 215 ASP C 230 1 16
HELIX 44 44 ILE C 245 ASP C 250 5 6
HELIX 45 45 SER C 253 ALA C 261 1 9
HELIX 46 46 GLY D 15 ALA D 17 5 3
HELIX 47 47 ASP D 18 GLN D 35 1 18
HELIX 48 48 ASP D 77 LEU D 84 5 8
HELIX 49 49 ALA D 85 LYS D 91 1 7
HELIX 50 50 ARG D 107 ILE D 126 1 20
HELIX 51 51 SER D 136 MSE D 145 1 10
HELIX 52 52 PRO D 152 ALA D 157 1 6
HELIX 53 53 LEU D 171 SER D 178 5 8
HELIX 54 54 MSE D 179 LYS D 184 1 6
HELIX 55 55 ASP D 186 GLU D 193 1 8
HELIX 56 56 SER D 194 MSE D 198 5 5
HELIX 57 57 ARG D 215 ASP D 230 1 16
HELIX 58 58 ILE D 245 ASP D 250 5 6
HELIX 59 59 SER D 253 THR D 260 1 8
SHEET 1 A 8 ALA A 38 SER A 43 0
SHEET 2 A 8 LYS A 51 PHE A 55 -1 O LEU A 54 N ARG A 39
SHEET 3 A 8 TRP A 93 PRO A 98 -1 O VAL A 95 N PHE A 55
SHEET 4 A 8 GLY A 63 VAL A 68 1 N GLY A 63 O ALA A 94
SHEET 5 A 8 ILE A 130 HIS A 135 1 O VAL A 131 N VAL A 66
SHEET 6 A 8 ILE A 159 ILE A 165 1 O ILE A 165 N GLY A 134
SHEET 7 A 8 LYS A 205 GLY A 211 1 O LYS A 205 N VAL A 162
SHEET 8 A 8 ASP A 232 ALA A 236 1 O VAL A 234 N VAL A 208
SHEET 1 B 8 ALA B 38 SER B 43 0
SHEET 2 B 8 LYS B 51 PHE B 55 -1 O LEU B 54 N ARG B 39
SHEET 3 B 8 ALA B 94 PRO B 98 -1 O VAL B 95 N PHE B 55
SHEET 4 B 8 LEU B 64 VAL B 68 1 N PHE B 65 O ALA B 94
SHEET 5 B 8 ILE B 130 HIS B 135 1 O VAL B 131 N VAL B 66
SHEET 6 B 8 ILE B 159 ILE B 165 1 O ARG B 160 N ILE B 130
SHEET 7 B 8 LYS B 205 GLY B 211 1 O TRP B 209 N PRO B 164
SHEET 8 B 8 ASP B 232 ALA B 236 1 O ASP B 232 N VAL B 206
SHEET 1 C 8 ALA C 38 SER C 43 0
SHEET 2 C 8 LYS C 51 PHE C 55 -1 O LEU C 54 N ARG C 39
SHEET 3 C 8 ALA C 94 PRO C 98 -1 O VAL C 95 N PHE C 55
SHEET 4 C 8 LEU C 64 VAL C 68 1 N PHE C 65 O ALA C 96
SHEET 5 C 8 ILE C 130 HIS C 135 1 O VAL C 131 N LEU C 64
SHEET 6 C 8 ILE C 159 ILE C 165 1 O ILE C 165 N GLY C 134
SHEET 7 C 8 LYS C 205 GLY C 211 1 O TRP C 209 N PRO C 164
SHEET 8 C 8 ASP C 232 ALA C 236 1 O ASP C 232 N VAL C 208
SHEET 1 D 8 ALA D 38 SER D 43 0
SHEET 2 D 8 LYS D 51 PHE D 55 -1 O LEU D 54 N ARG D 39
SHEET 3 D 8 ALA D 94 PRO D 98 -1 O VAL D 95 N PHE D 55
SHEET 4 D 8 LEU D 64 VAL D 68 1 N PHE D 65 O ALA D 96
SHEET 5 D 8 ILE D 130 HIS D 135 1 O VAL D 131 N LEU D 64
SHEET 6 D 8 ILE D 159 ILE D 165 1 O ILE D 165 N GLY D 134
SHEET 7 D 8 LYS D 205 GLY D 211 1 O LYS D 205 N VAL D 162
SHEET 8 D 8 ASP D 232 ALA D 236 1 O ASP D 232 N VAL D 208
LINK C GLY A 0 N MSE A 1 1555 1555 1.34
LINK C MSE A 1 N GLU A 2 1555 1555 1.32
LINK C TRP A 73 N MSE A 74 1555 1555 1.34
LINK C MSE A 74 N ALA A 75 1555 1555 1.34
LINK C ALA A 96 N MSE A 97 1555 1555 1.33
LINK C MSE A 97 N PRO A 98 1555 1555 1.34
LINK C ARG A 144 N MSE A 145 1555 1555 1.35
LINK C MSE A 145 N LEU A 146 1555 1555 1.34
LINK C SER A 178 N MSE A 179 1555 1555 1.34
LINK C MSE A 179 N ASN A 180 1555 1555 1.33
LINK C LYS A 184 N MSE A 185 1555 1555 1.33
LINK C MSE A 185 N ASP A 186 1555 1555 1.33
LINK C GLU A 197 N MSE A 198 1555 1555 1.33
LINK C MSE A 198 N GLN A 199 1555 1555 1.32
LINK C GLY B 0 N MSE B 1 1555 1555 1.34
LINK C MSE B 1 N GLU B 2 1555 1555 1.33
LINK C TRP B 73 N MSE B 74 1555 1555 1.33
LINK C MSE B 74 N ALA B 75 1555 1555 1.33
LINK C ALA B 96 N MSE B 97 1555 1555 1.33
LINK C MSE B 97 N PRO B 98 1555 1555 1.34
LINK C ARG B 144 N MSE B 145 1555 1555 1.34
LINK C MSE B 145 N LEU B 146 1555 1555 1.34
LINK C SER B 178 N MSE B 179 1555 1555 1.33
LINK C MSE B 179 N ASN B 180 1555 1555 1.33
LINK C LYS B 184 N MSE B 185 1555 1555 1.33
LINK C MSE B 185 N ASP B 186 1555 1555 1.33
LINK C GLU B 197 N MSE B 198 1555 1555 1.34
LINK C MSE B 198 N GLN B 199 1555 1555 1.33
LINK MG MG B 262 O HOH B 322 1555 1555 2.11
LINK MG MG B 262 O HOH D 267 1555 1555 2.16
LINK MG MG B 262 O HOH D 275 1555 1555 2.15
LINK MG MG B 262 O HOH B 327 1555 1555 2.02
LINK MG MG B 262 O HOH D 264 1555 1555 1.77
LINK MG MG B 262 O HOH D 269 1555 1555 1.97
LINK C GLY C 0 N MSE C 1 1555 1555 1.34
LINK C MSE C 1 N GLU C 2 1555 1555 1.33
LINK C TRP C 73 N MSE C 74 1555 1555 1.33
LINK C MSE C 74 N ALA C 75 1555 1555 1.33
LINK C ALA C 96 N MSE C 97 1555 1555 1.33
LINK C MSE C 97 N PRO C 98 1555 1555 1.34
LINK C ARG C 144 N MSE C 145 1555 1555 1.32
LINK C MSE C 145 N LEU C 146 1555 1555 1.34
LINK C SER C 178 N MSE C 179 1555 1555 1.34
LINK C MSE C 179 N ASN C 180 1555 1555 1.32
LINK C LYS C 184 N MSE C 185 1555 1555 1.33
LINK C MSE C 185 N ASP C 186 1555 1555 1.31
LINK C GLU C 197 N MSE C 198 1555 1555 1.32
LINK C MSE C 198 N GLN C 199 1555 1555 1.34
LINK C GLY D 0 N MSE D 1 1555 1555 1.34
LINK C MSE D 1 N GLU D 2 1555 1555 1.33
LINK C TRP D 73 N MSE D 74 1555 1555 1.33
LINK C MSE D 74 N ALA D 75 1555 1555 1.33
LINK C ALA D 96 N MSE D 97 1555 1555 1.34
LINK C MSE D 97 N PRO D 98 1555 1555 1.33
LINK C ARG D 144 N MSE D 145 1555 1555 1.32
LINK C MSE D 145 N LEU D 146 1555 1555 1.32
LINK C SER D 178 N MSE D 179 1555 1555 1.34
LINK C MSE D 179 N ASN D 180 1555 1555 1.33
LINK C LYS D 184 N MSE D 185 1555 1555 1.34
LINK C MSE D 185 N ASP D 186 1555 1555 1.32
LINK C GLU D 197 N MSE D 198 1555 1555 1.32
LINK C MSE D 198 N GLN D 199 1555 1555 1.34
CISPEP 1 CYS A 103 PRO A 104 0 4.57
CISPEP 2 CYS B 103 PRO B 104 0 3.06
CISPEP 3 CYS C 103 PRO C 104 0 2.47
CISPEP 4 CYS D 103 PRO D 104 0 1.85
SITE 1 AC1 7 HOH B 322 HOH B 327 ASP D 203 HOH D 264
SITE 2 AC1 7 HOH D 267 HOH D 269 HOH D 275
SITE 1 AC2 3 ARG A 107 SER A 109 HOH A 364
SITE 1 AC3 2 ARG C 107 SER C 109
SITE 1 AC4 4 ARG B 107 SER B 109 HOH B 330 HOH B 446
SITE 1 AC5 3 ARG D 107 SER D 109 HOH D 290
SITE 1 AC6 11 PRO A 148 GLU A 149 VAL A 150 LEU A 151
SITE 2 AC6 11 PRO A 152 PRO B 148 GLU B 149 VAL B 150
SITE 3 AC6 11 LEU B 151 PRO B 152 HOH B 319
SITE 1 AC7 10 PRO C 148 GLU C 149 VAL C 150 LEU C 151
SITE 2 AC7 10 PRO C 152 PRO D 148 GLU D 149 VAL D 150
SITE 3 AC7 10 LEU D 151 PRO D 152
SITE 1 AC8 8 ASN A 9 GLY A 71 TYR A 72 PHE A 76
SITE 2 AC8 8 HIS A 135 SER A 136 HIS A 241 HOH A 449
SITE 1 AC9 8 ASN B 9 GLY B 71 TYR B 72 HIS B 135
SITE 2 AC9 8 HIS B 241 PHE B 242 HOH B 419 HOH B 484
SITE 1 BC1 8 ASN C 9 GLY C 71 TYR C 72 PHE C 76
SITE 2 BC1 8 HIS C 135 HIS C 241 HOH C 311 HOH C 472
SITE 1 BC2 9 ASN D 9 GLY D 71 TYR D 72 PHE D 76
SITE 2 BC2 9 HIS D 135 SER D 136 HIS D 241 HOH D 330
SITE 3 BC2 9 HOH D 516
CRYST1 77.197 74.438 95.727 90.00 113.39 90.00 P 1 21 1 8
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 0.012950 0.000000 0.005600 0.00000
SCALE2 0.000000 0.013430 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011380 0.00000
TER 2029 ALA A 261
TER 4074 ALA B 261
TER 6109 ALA C 261
TER 8135 ALA D 261
MASTER 439 0 39 59 32 0 21 6 9492 4 286 84
END |