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HEADER HYDROLASE 21-AUG-07 2R11
TITLE CRYSTAL STRUCTURE OF PUTATIVE HYDROLASE (2632844) FROM
TITLE 2 BACILLUS SUBTILIS AT 1.96 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE NP;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: RESIDUES 1-294;
COMPND 5 SYNONYM: CARBOXYLESTERASE NA;
COMPND 6 EC: 3.1.1.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: 168;
SOURCE 5 GENE: 2632844, NAP, BSU05440;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS 2632844, PUTATIVE HYDROLASE, STRUCTURAL GENOMICS, JOINT
KEYWDS 2 CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE
KEYWDS 3 INITIATIVE, PSI-2, STRUCTURAL GENOMICS, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 1 04-SEP-07 2R11 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF PUTATIVE HYDROLASE (2632844)
JRNL TITL 2 FROM BACILLUS SUBTILIS AT 1.96 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.96 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.96
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 3 NUMBER OF REFLECTIONS : 85485
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4284
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.96
REMARK 3 BIN RESOLUTION RANGE LOW : 2.01
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6423
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.57
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE SET COUNT : 328
REMARK 3 BIN FREE R VALUE : 0.3190
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 10230
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.86
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.73000
REMARK 3 B22 (A**2) : -0.62000
REMARK 3 B33 (A**2) : -0.25000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.22000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.186
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.174
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.128
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.475
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9535 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 6366 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13012 ; 1.359 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): 15479 ; 0.901 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1180 ; 4.370 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 452 ;33.019 ;23.606
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1494 ;12.820 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;13.436 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1401 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10695 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2037 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2110 ; 0.203 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 6684 ; 0.193 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4709 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 4565 ; 0.085 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 786 ; 0.168 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.027 ; 0.200
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.091 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 28 ; 0.138 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 96 ; 0.256 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 38 ; 0.177 ; 0.200
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): 5988 ; 1.626 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2303 ; 0.628 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9377 ; 2.419 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4154 ; 4.393 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3616 ; 5.632 ;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 : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 13 A 293 5
REMARK 3 1 B 13 B 293 5
REMARK 3 1 C 13 C 293 5
REMARK 3 1 D 13 D 293 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1616 ; 0.190 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 B (A): 1616 ; 0.190 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 C (A): 1616 ; 0.180 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 D (A): 1616 ; 0.190 ; 0.500
REMARK 3 LOOSE POSITIONAL 1 A (A): 1997 ; 0.450 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 B (A): 1997 ; 0.370 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 C (A): 1997 ; 0.330 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 D (A): 1997 ; 0.390 ; 5.000
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1616 ; 1.110 ; 2.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 1616 ; 1.120 ; 2.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 1616 ; 1.070 ; 2.000
REMARK 3 MEDIUM THERMAL 1 D (A**2): 1616 ; 1.090 ; 2.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 1997 ; 2.500 ;10.000
REMARK 3 LOOSE THERMAL 1 B (A**2): 1997 ; 2.580 ;10.000
REMARK 3 LOOSE THERMAL 1 C (A**2): 1997 ; 2.440 ;10.000
REMARK 3 LOOSE THERMAL 1 D (A**2): 1997 ; 2.580 ;10.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
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. 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. 3. EDO, MG, CL AND PGE IN THE
REMARK 3 MODEL ARE PRESENT BASED ON CRYO/CRYSTALLIZATION CONDITIONS. 4.
REMARK 3 DUE TO PRESENCE OF ICE RINGS, THE DATA FROM THE FOLLOWING
REMARK 3 RESOLUTION RANGES ARE EXCLUDED: 2.29-2.23, 3.70-3.64. 5. THE
REMARK 3 ACTIVE SITE TRIAD CONSISTS OF S130-H274-D245.
REMARK 4
REMARK 4 2R11 COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB044292.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-APR-2006
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 9.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91837, 0.97934
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : FLAT COLLIMATING MIRROR,
REMARK 200 TOROID FOCUSING MIRROR
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 : 85536
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960
REMARK 200 RESOLUTION RANGE LOW (A) : 48.795
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : 0.09400
REMARK 200 FOR THE DATA SET : 6.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.46400
REMARK 200 R SYM FOR SHELL (I) : 0.46400
REMARK 200 FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELX, AUTOSHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NANODROP, 14.0% PEG 8000, 0.2M
REMARK 280 MGCL2, 0.1M CHES PH 9.0, 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,1/2+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 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 48.77500
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
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND 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. AUTHORS STATE THAT CRYSTAL PACKING
REMARK 300 ANALYSIS SUPPORTS THE ASSIGNMENT OF A DIMER AS A
REMARK 300 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE.
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: DIMER
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 2640 ANGSTROM**2
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMER
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 2750 ANGSTROM**2
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 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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 MSE A -11
REMARK 465 GLY A -10
REMARK 465 SER A -9
REMARK 465 ASP A -8
REMARK 465 LYS A -7
REMARK 465 ILE A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MSE A 1
REMARK 465 SER A 2
REMARK 465 ASN A 3
REMARK 465 HIS A 4
REMARK 465 SER A 5
REMARK 465 SER A 6
REMARK 465 SER A 7
REMARK 465 ILE A 8
REMARK 465 PRO A 9
REMARK 465 GLU A 10
REMARK 465 ALA A 294
REMARK 465 MSE B -11
REMARK 465 GLY B -10
REMARK 465 SER B -9
REMARK 465 ASP B -8
REMARK 465 LYS B -7
REMARK 465 ILE B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MSE B 1
REMARK 465 SER B 2
REMARK 465 ASN B 3
REMARK 465 HIS B 4
REMARK 465 SER B 5
REMARK 465 SER B 6
REMARK 465 SER B 7
REMARK 465 MSE C -11
REMARK 465 GLY C -10
REMARK 465 SER C -9
REMARK 465 ASP C -8
REMARK 465 LYS C -7
REMARK 465 ILE C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 HIS C 0
REMARK 465 MSE C 1
REMARK 465 SER C 2
REMARK 465 ASN C 3
REMARK 465 HIS C 4
REMARK 465 SER C 5
REMARK 465 SER C 6
REMARK 465 SER C 7
REMARK 465 ILE C 8
REMARK 465 PRO C 9
REMARK 465 MSE D -11
REMARK 465 GLY D -10
REMARK 465 SER D -9
REMARK 465 ASP D -8
REMARK 465 LYS D -7
REMARK 465 ILE D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 HIS D -1
REMARK 465 HIS D 0
REMARK 465 MSE D 1
REMARK 465 SER D 2
REMARK 465 ASN D 3
REMARK 465 HIS D 4
REMARK 465 SER D 5
REMARK 465 SER D 6
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 ASP A 54 CG OD1 OD2
REMARK 470 GLU A 180 CG CD OE1 OE2
REMARK 470 ARG A 212 CZ NH1 NH2
REMARK 470 LYS A 270 CG CD CE NZ
REMARK 470 ILE B 8 CG1 CG2 CD1
REMARK 470 GLU B 10 CG CD OE1 OE2
REMARK 470 GLU B 53 OE1 OE2
REMARK 470 GLU B 180 CD OE1 OE2
REMARK 470 LYS B 270 CG CD CE NZ
REMARK 470 GLU C 10 CG CD OE1 OE2
REMARK 470 GLU C 180 CD OE1 OE2
REMARK 470 LYS C 202 CD CE NZ
REMARK 470 ARG C 212 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 270 CG CD CE NZ
REMARK 470 SER D 7 OG
REMARK 470 LYS D 270 CG CD CE NZ
REMARK 470 ASN D 293 CG OD1 ND2
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
REMARK 500 OE2 GLU C 122 O HOH C 406 2.13
REMARK 500 OG SER C 102 OD2 ASP C 107 2.14
REMARK 500 O LEU D 28 O HOH D 414 2.17
REMARK 500 OG SER A 102 OD2 ASP A 107 2.18
REMARK 500 O HOH B 313 O HOH B 373 2.19
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 LEU A 65 -6.49 66.60
REMARK 500 SER A 67 168.36 68.74
REMARK 500 ASN A 94 -157.45 -176.15
REMARK 500 GLU A 122 -77.12 -86.69
REMARK 500 SER A 130 -120.65 52.95
REMARK 500 GLU A 157 -114.20 43.55
REMARK 500 THR A 158 -63.70 74.95
REMARK 500 THR A 174 56.01 -90.84
REMARK 500 LEU B 65 -4.98 68.95
REMARK 500 SER B 67 172.35 72.71
REMARK 500 ASN B 94 -163.83 -170.87
REMARK 500 GLU B 122 -72.81 -90.87
REMARK 500 SER B 130 -120.65 56.32
REMARK 500 GLU B 145 -8.62 -59.93
REMARK 500 LYS B 148 -78.99 -78.03
REMARK 500 GLU B 157 -115.36 44.83
REMARK 500 THR B 158 -59.48 72.47
REMARK 500 TYR B 248 172.54 179.89
REMARK 500 LEU C 65 -8.74 63.53
REMARK 500 SER C 67 172.46 69.75
REMARK 500 LYS C 93 99.26 -69.17
REMARK 500 ASN C 94 -160.18 -171.12
REMARK 500 GLU C 122 -72.03 -88.21
REMARK 500 SER C 130 -119.41 56.48
REMARK 500 GLU C 157 -110.36 42.67
REMARK 500 THR C 158 -65.12 70.13
REMARK 500 THR C 174 52.59 -100.68
REMARK 500 LEU D 65 -2.95 66.90
REMARK 500 SER D 67 173.19 68.20
REMARK 500 ASN D 94 -162.39 -170.92
REMARK 500 SER D 130 -124.92 59.80
REMARK 500 GLU D 157 -113.06 41.10
REMARK 500 THR D 158 -64.53 74.47
REMARK 500 ASN D 191 75.14 -108.78
REMARK 500 VAL D 275 59.93 -97.72
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 295 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 294 OXT
REMARK 620 2 HOH B 318 O 91.5
REMARK 620 3 HOH B 333 O 93.6 91.3
REMARK 620 4 HOH B 389 O 175.3 91.2 90.2
REMARK 620 5 HOH B 376 O 87.4 85.9 177.1 88.9
REMARK 620 6 HOH B 316 O 90.0 171.7 96.7 86.9 86.0
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 360559 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT CONSISTS OF RESIDUES 1-294 OF THE FULL LENGTH
REMARK 999 PROTEIN (1-300). IT WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHH.
DBREF 2R11 A 1 294 UNP P96688 P96688_BACSU 1 294
DBREF 2R11 B 1 294 UNP P96688 P96688_BACSU 1 294
DBREF 2R11 C 1 294 UNP P96688 P96688_BACSU 1 294
DBREF 2R11 D 1 294 UNP P96688 P96688_BACSU 1 294
SEQADV 2R11 MSE A -11 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 GLY A -10 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 SER A -9 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 ASP A -8 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 LYS A -7 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 ILE A -6 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS A -5 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS A -4 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS A -3 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS A -2 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS A -1 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS A 0 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 MSE B -11 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 GLY B -10 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 SER B -9 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 ASP B -8 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 LYS B -7 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 ILE B -6 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS B -5 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS B -4 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS B -3 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS B -2 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS B -1 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS B 0 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 MSE C -11 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 GLY C -10 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 SER C -9 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 ASP C -8 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 LYS C -7 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 ILE C -6 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS C -5 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS C -4 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS C -3 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS C -2 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS C -1 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS C 0 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 MSE D -11 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 GLY D -10 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 SER D -9 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 ASP D -8 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 LYS D -7 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 ILE D -6 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS D -5 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS D -4 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS D -3 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS D -2 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS D -1 UNP P96688 LEADER SEQUENCE
SEQADV 2R11 HIS D 0 UNP P96688 LEADER SEQUENCE
SEQRES 1 A 306 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 A 306 SER ASN HIS SER SER SER ILE PRO GLU LEU SER ASP ASN
SEQRES 3 A 306 GLY ILE ARG TYR TYR GLN THR TYR ASN GLU SER LEU SER
SEQRES 4 A 306 LEU TRP PRO VAL ARG CYS LYS SER PHE TYR ILE SER THR
SEQRES 5 A 306 ARG PHE GLY GLN THR HIS VAL ILE ALA SER GLY PRO GLU
SEQRES 6 A 306 ASP ALA PRO PRO LEU VAL LEU LEU HIS GLY ALA LEU PHE
SEQRES 7 A 306 SER SER THR MSE TRP TYR PRO ASN ILE ALA ASP TRP SER
SEQRES 8 A 306 SER LYS TYR ARG THR TYR ALA VAL ASP ILE ILE GLY ASP
SEQRES 9 A 306 LYS ASN LYS SER ILE PRO GLU ASN VAL SER GLY THR ARG
SEQRES 10 A 306 THR ASP TYR ALA ASN TRP LEU LEU ASP VAL PHE ASP ASN
SEQRES 11 A 306 LEU GLY ILE GLU LYS SER HIS MSE ILE GLY LEU SER LEU
SEQRES 12 A 306 GLY GLY LEU HIS THR MSE ASN PHE LEU LEU ARG MSE PRO
SEQRES 13 A 306 GLU ARG VAL LYS SER ALA ALA ILE LEU SER PRO ALA GLU
SEQRES 14 A 306 THR PHE LEU PRO PHE HIS HIS ASP PHE TYR LYS TYR ALA
SEQRES 15 A 306 LEU GLY LEU THR ALA SER ASN GLY VAL GLU THR PHE LEU
SEQRES 16 A 306 ASN TRP MSE MSE ASN ASP GLN ASN VAL LEU HIS PRO ILE
SEQRES 17 A 306 PHE VAL LYS GLN PHE LYS ALA GLY VAL MSE TRP GLN ASP
SEQRES 18 A 306 GLY SER ARG ASN PRO ASN PRO ASN ALA ASP GLY PHE PRO
SEQRES 19 A 306 TYR VAL PHE THR ASP GLU GLU LEU ARG SER ALA ARG VAL
SEQRES 20 A 306 PRO ILE LEU LEU LEU LEU GLY GLU HIS GLU VAL ILE TYR
SEQRES 21 A 306 ASP PRO HIS SER ALA LEU HIS ARG ALA SER SER PHE VAL
SEQRES 22 A 306 PRO ASP ILE GLU ALA GLU VAL ILE LYS ASN ALA GLY HIS
SEQRES 23 A 306 VAL LEU SER MSE GLU GLN PRO THR TYR VAL ASN GLU ARG
SEQRES 24 A 306 VAL MSE ARG PHE PHE ASN ALA
SEQRES 1 B 306 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 B 306 SER ASN HIS SER SER SER ILE PRO GLU LEU SER ASP ASN
SEQRES 3 B 306 GLY ILE ARG TYR TYR GLN THR TYR ASN GLU SER LEU SER
SEQRES 4 B 306 LEU TRP PRO VAL ARG CYS LYS SER PHE TYR ILE SER THR
SEQRES 5 B 306 ARG PHE GLY GLN THR HIS VAL ILE ALA SER GLY PRO GLU
SEQRES 6 B 306 ASP ALA PRO PRO LEU VAL LEU LEU HIS GLY ALA LEU PHE
SEQRES 7 B 306 SER SER THR MSE TRP TYR PRO ASN ILE ALA ASP TRP SER
SEQRES 8 B 306 SER LYS TYR ARG THR TYR ALA VAL ASP ILE ILE GLY ASP
SEQRES 9 B 306 LYS ASN LYS SER ILE PRO GLU ASN VAL SER GLY THR ARG
SEQRES 10 B 306 THR ASP TYR ALA ASN TRP LEU LEU ASP VAL PHE ASP ASN
SEQRES 11 B 306 LEU GLY ILE GLU LYS SER HIS MSE ILE GLY LEU SER LEU
SEQRES 12 B 306 GLY GLY LEU HIS THR MSE ASN PHE LEU LEU ARG MSE PRO
SEQRES 13 B 306 GLU ARG VAL LYS SER ALA ALA ILE LEU SER PRO ALA GLU
SEQRES 14 B 306 THR PHE LEU PRO PHE HIS HIS ASP PHE TYR LYS TYR ALA
SEQRES 15 B 306 LEU GLY LEU THR ALA SER ASN GLY VAL GLU THR PHE LEU
SEQRES 16 B 306 ASN TRP MSE MSE ASN ASP GLN ASN VAL LEU HIS PRO ILE
SEQRES 17 B 306 PHE VAL LYS GLN PHE LYS ALA GLY VAL MSE TRP GLN ASP
SEQRES 18 B 306 GLY SER ARG ASN PRO ASN PRO ASN ALA ASP GLY PHE PRO
SEQRES 19 B 306 TYR VAL PHE THR ASP GLU GLU LEU ARG SER ALA ARG VAL
SEQRES 20 B 306 PRO ILE LEU LEU LEU LEU GLY GLU HIS GLU VAL ILE TYR
SEQRES 21 B 306 ASP PRO HIS SER ALA LEU HIS ARG ALA SER SER PHE VAL
SEQRES 22 B 306 PRO ASP ILE GLU ALA GLU VAL ILE LYS ASN ALA GLY HIS
SEQRES 23 B 306 VAL LEU SER MSE GLU GLN PRO THR TYR VAL ASN GLU ARG
SEQRES 24 B 306 VAL MSE ARG PHE PHE ASN ALA
SEQRES 1 C 306 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 C 306 SER ASN HIS SER SER SER ILE PRO GLU LEU SER ASP ASN
SEQRES 3 C 306 GLY ILE ARG TYR TYR GLN THR TYR ASN GLU SER LEU SER
SEQRES 4 C 306 LEU TRP PRO VAL ARG CYS LYS SER PHE TYR ILE SER THR
SEQRES 5 C 306 ARG PHE GLY GLN THR HIS VAL ILE ALA SER GLY PRO GLU
SEQRES 6 C 306 ASP ALA PRO PRO LEU VAL LEU LEU HIS GLY ALA LEU PHE
SEQRES 7 C 306 SER SER THR MSE TRP TYR PRO ASN ILE ALA ASP TRP SER
SEQRES 8 C 306 SER LYS TYR ARG THR TYR ALA VAL ASP ILE ILE GLY ASP
SEQRES 9 C 306 LYS ASN LYS SER ILE PRO GLU ASN VAL SER GLY THR ARG
SEQRES 10 C 306 THR ASP TYR ALA ASN TRP LEU LEU ASP VAL PHE ASP ASN
SEQRES 11 C 306 LEU GLY ILE GLU LYS SER HIS MSE ILE GLY LEU SER LEU
SEQRES 12 C 306 GLY GLY LEU HIS THR MSE ASN PHE LEU LEU ARG MSE PRO
SEQRES 13 C 306 GLU ARG VAL LYS SER ALA ALA ILE LEU SER PRO ALA GLU
SEQRES 14 C 306 THR PHE LEU PRO PHE HIS HIS ASP PHE TYR LYS TYR ALA
SEQRES 15 C 306 LEU GLY LEU THR ALA SER ASN GLY VAL GLU THR PHE LEU
SEQRES 16 C 306 ASN TRP MSE MSE ASN ASP GLN ASN VAL LEU HIS PRO ILE
SEQRES 17 C 306 PHE VAL LYS GLN PHE LYS ALA GLY VAL MSE TRP GLN ASP
SEQRES 18 C 306 GLY SER ARG ASN PRO ASN PRO ASN ALA ASP GLY PHE PRO
SEQRES 19 C 306 TYR VAL PHE THR ASP GLU GLU LEU ARG SER ALA ARG VAL
SEQRES 20 C 306 PRO ILE LEU LEU LEU LEU GLY GLU HIS GLU VAL ILE TYR
SEQRES 21 C 306 ASP PRO HIS SER ALA LEU HIS ARG ALA SER SER PHE VAL
SEQRES 22 C 306 PRO ASP ILE GLU ALA GLU VAL ILE LYS ASN ALA GLY HIS
SEQRES 23 C 306 VAL LEU SER MSE GLU GLN PRO THR TYR VAL ASN GLU ARG
SEQRES 24 C 306 VAL MSE ARG PHE PHE ASN ALA
SEQRES 1 D 306 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 D 306 SER ASN HIS SER SER SER ILE PRO GLU LEU SER ASP ASN
SEQRES 3 D 306 GLY ILE ARG TYR TYR GLN THR TYR ASN GLU SER LEU SER
SEQRES 4 D 306 LEU TRP PRO VAL ARG CYS LYS SER PHE TYR ILE SER THR
SEQRES 5 D 306 ARG PHE GLY GLN THR HIS VAL ILE ALA SER GLY PRO GLU
SEQRES 6 D 306 ASP ALA PRO PRO LEU VAL LEU LEU HIS GLY ALA LEU PHE
SEQRES 7 D 306 SER SER THR MSE TRP TYR PRO ASN ILE ALA ASP TRP SER
SEQRES 8 D 306 SER LYS TYR ARG THR TYR ALA VAL ASP ILE ILE GLY ASP
SEQRES 9 D 306 LYS ASN LYS SER ILE PRO GLU ASN VAL SER GLY THR ARG
SEQRES 10 D 306 THR ASP TYR ALA ASN TRP LEU LEU ASP VAL PHE ASP ASN
SEQRES 11 D 306 LEU GLY ILE GLU LYS SER HIS MSE ILE GLY LEU SER LEU
SEQRES 12 D 306 GLY GLY LEU HIS THR MSE ASN PHE LEU LEU ARG MSE PRO
SEQRES 13 D 306 GLU ARG VAL LYS SER ALA ALA ILE LEU SER PRO ALA GLU
SEQRES 14 D 306 THR PHE LEU PRO PHE HIS HIS ASP PHE TYR LYS TYR ALA
SEQRES 15 D 306 LEU GLY LEU THR ALA SER ASN GLY VAL GLU THR PHE LEU
SEQRES 16 D 306 ASN TRP MSE MSE ASN ASP GLN ASN VAL LEU HIS PRO ILE
SEQRES 17 D 306 PHE VAL LYS GLN PHE LYS ALA GLY VAL MSE TRP GLN ASP
SEQRES 18 D 306 GLY SER ARG ASN PRO ASN PRO ASN ALA ASP GLY PHE PRO
SEQRES 19 D 306 TYR VAL PHE THR ASP GLU GLU LEU ARG SER ALA ARG VAL
SEQRES 20 D 306 PRO ILE LEU LEU LEU LEU GLY GLU HIS GLU VAL ILE TYR
SEQRES 21 D 306 ASP PRO HIS SER ALA LEU HIS ARG ALA SER SER PHE VAL
SEQRES 22 D 306 PRO ASP ILE GLU ALA GLU VAL ILE LYS ASN ALA GLY HIS
SEQRES 23 D 306 VAL LEU SER MSE GLU GLN PRO THR TYR VAL ASN GLU ARG
SEQRES 24 D 306 VAL MSE ARG PHE PHE ASN ALA
MODRES 2R11 MSE A 70 MET SELENOMETHIONINE
MODRES 2R11 MSE A 126 MET SELENOMETHIONINE
MODRES 2R11 MSE A 137 MET SELENOMETHIONINE
MODRES 2R11 MSE A 143 MET SELENOMETHIONINE
MODRES 2R11 MSE A 186 MET SELENOMETHIONINE
MODRES 2R11 MSE A 187 MET SELENOMETHIONINE
MODRES 2R11 MSE A 206 MET SELENOMETHIONINE
MODRES 2R11 MSE A 278 MET SELENOMETHIONINE
MODRES 2R11 MSE A 289 MET SELENOMETHIONINE
MODRES 2R11 MSE B 70 MET SELENOMETHIONINE
MODRES 2R11 MSE B 126 MET SELENOMETHIONINE
MODRES 2R11 MSE B 137 MET SELENOMETHIONINE
MODRES 2R11 MSE B 143 MET SELENOMETHIONINE
MODRES 2R11 MSE B 186 MET SELENOMETHIONINE
MODRES 2R11 MSE B 187 MET SELENOMETHIONINE
MODRES 2R11 MSE B 206 MET SELENOMETHIONINE
MODRES 2R11 MSE B 278 MET SELENOMETHIONINE
MODRES 2R11 MSE B 289 MET SELENOMETHIONINE
MODRES 2R11 MSE C 70 MET SELENOMETHIONINE
MODRES 2R11 MSE C 126 MET SELENOMETHIONINE
MODRES 2R11 MSE C 137 MET SELENOMETHIONINE
MODRES 2R11 MSE C 143 MET SELENOMETHIONINE
MODRES 2R11 MSE C 186 MET SELENOMETHIONINE
MODRES 2R11 MSE C 187 MET SELENOMETHIONINE
MODRES 2R11 MSE C 206 MET SELENOMETHIONINE
MODRES 2R11 MSE C 278 MET SELENOMETHIONINE
MODRES 2R11 MSE C 289 MET SELENOMETHIONINE
MODRES 2R11 MSE D 70 MET SELENOMETHIONINE
MODRES 2R11 MSE D 126 MET SELENOMETHIONINE
MODRES 2R11 MSE D 137 MET SELENOMETHIONINE
MODRES 2R11 MSE D 143 MET SELENOMETHIONINE
MODRES 2R11 MSE D 186 MET SELENOMETHIONINE
MODRES 2R11 MSE D 187 MET SELENOMETHIONINE
MODRES 2R11 MSE D 206 MET SELENOMETHIONINE
MODRES 2R11 MSE D 278 MET SELENOMETHIONINE
MODRES 2R11 MSE D 289 MET SELENOMETHIONINE
HET MSE A 70 8
HET MSE A 126 8
HET MSE A 137 8
HET MSE A 143 8
HET MSE A 186 8
HET MSE A 187 8
HET MSE A 206 8
HET MSE A 278 8
HET MSE A 289 13
HET MSE B 70 8
HET MSE B 126 8
HET MSE B 137 8
HET MSE B 143 8
HET MSE B 186 8
HET MSE B 187 8
HET MSE B 206 13
HET MSE B 278 8
HET MSE B 289 13
HET MSE C 70 8
HET MSE C 126 8
HET MSE C 137 8
HET MSE C 143 8
HET MSE C 186 8
HET MSE C 187 8
HET MSE C 206 13
HET MSE C 278 8
HET MSE C 289 13
HET MSE D 70 8
HET MSE D 126 8
HET MSE D 137 8
HET MSE D 143 13
HET MSE D 186 8
HET MSE D 187 8
HET MSE D 206 8
HET MSE D 278 8
HET MSE D 289 13
HET MG B 295 1
HET CL A 295 1
HET EDO D 295 4
HET EDO B 296 4
HET PGE C 295 10
HETNAM MSE SELENOMETHIONINE
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PGE TRIETHYLENE GLYCOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 36(C5 H11 N O2 SE)
FORMUL 5 MG MG 2+
FORMUL 6 CL CL 1-
FORMUL 7 EDO 2(C2 H6 O2)
FORMUL 9 PGE C6 H14 O4
FORMUL 10 HOH *985(H2 O)
HELIX 1 1 SER A 12 SER A 27 1 16
HELIX 2 2 SER A 67 TYR A 72 5 6
HELIX 3 3 ASN A 74 TYR A 82 1 9
HELIX 4 4 THR A 104 LEU A 119 1 16
HELIX 5 5 SER A 130 MSE A 143 1 14
HELIX 6 6 HIS A 163 GLY A 172 1 10
HELIX 7 7 ASN A 177 MSE A 187 1 11
HELIX 8 8 HIS A 194 TRP A 207 1 14
HELIX 9 9 THR A 226 SER A 232 1 7
HELIX 10 10 ASP A 249 VAL A 261 1 13
HELIX 11 11 VAL A 275 GLN A 280 1 6
HELIX 12 12 GLN A 280 ASN A 293 1 14
HELIX 13 13 SER B 12 SER B 27 1 16
HELIX 14 14 SER B 67 TYR B 72 5 6
HELIX 15 15 ASN B 74 TYR B 82 1 9
HELIX 16 16 THR B 104 GLY B 120 1 17
HELIX 17 17 SER B 130 MSE B 143 1 14
HELIX 18 18 HIS B 163 GLY B 172 1 10
HELIX 19 19 ASN B 177 MSE B 187 1 11
HELIX 20 20 HIS B 194 MSE B 206 1 13
HELIX 21 21 THR B 226 SER B 232 1 7
HELIX 22 22 ASP B 249 VAL B 261 1 13
HELIX 23 23 VAL B 275 GLN B 280 1 6
HELIX 24 24 GLN B 280 ALA B 294 1 15
HELIX 25 25 SER C 12 LEU C 26 1 15
HELIX 26 26 SER C 27 TRP C 29 5 3
HELIX 27 27 SER C 67 TYR C 72 5 6
HELIX 28 28 ASN C 74 TYR C 82 1 9
HELIX 29 29 THR C 104 GLY C 120 1 17
HELIX 30 30 SER C 130 MSE C 143 1 14
HELIX 31 31 HIS C 163 GLY C 172 1 10
HELIX 32 32 LEU C 173 ALA C 175 5 3
HELIX 33 33 ASN C 177 MSE C 187 1 11
HELIX 34 34 HIS C 194 TRP C 207 1 14
HELIX 35 35 THR C 226 SER C 232 1 7
HELIX 36 36 ASP C 249 VAL C 261 1 13
HELIX 37 37 VAL C 275 GLN C 280 1 6
HELIX 38 38 GLN C 280 ALA C 294 1 15
HELIX 39 39 SER D 12 LEU D 26 1 15
HELIX 40 40 SER D 27 TRP D 29 5 3
HELIX 41 41 SER D 67 TYR D 72 5 6
HELIX 42 42 ASN D 74 SER D 79 1 6
HELIX 43 43 THR D 104 GLY D 120 1 17
HELIX 44 44 SER D 130 MSE D 143 1 14
HELIX 45 45 HIS D 163 GLY D 172 1 10
HELIX 46 46 ASN D 177 MSE D 187 1 11
HELIX 47 47 HIS D 194 TRP D 207 1 14
HELIX 48 48 THR D 226 SER D 232 1 7
HELIX 49 49 ASP D 249 VAL D 261 1 13
HELIX 50 50 VAL D 275 GLN D 280 1 6
HELIX 51 51 GLN D 280 ALA D 294 1 15
SHEET 1 A 3 LYS A 34 ILE A 38 0
SHEET 2 A 3 GLY A 43 SER A 50 -1 O THR A 45 N ILE A 38
SHEET 3 A 3 ILE A 97 PRO A 98 -1 O ILE A 97 N GLN A 44
SHEET 1 B 8 LYS A 34 ILE A 38 0
SHEET 2 B 8 GLY A 43 SER A 50 -1 O THR A 45 N ILE A 38
SHEET 3 B 8 ARG A 83 VAL A 87 -1 O ALA A 86 N ILE A 48
SHEET 4 B 8 PRO A 57 LEU A 61 1 N LEU A 58 O TYR A 85
SHEET 5 B 8 SER A 124 LEU A 129 1 O ILE A 127 N LEU A 61
SHEET 6 B 8 VAL A 147 LEU A 153 1 O ALA A 151 N MSE A 126
SHEET 7 B 8 ILE A 237 GLY A 242 1 O LEU A 238 N ILE A 152
SHEET 8 B 8 GLU A 265 ILE A 269 1 O ILE A 269 N LEU A 241
SHEET 1 C 3 LYS B 34 THR B 40 0
SHEET 2 C 3 GLY B 43 SER B 50 -1 O THR B 45 N ILE B 38
SHEET 3 C 3 ILE B 97 PRO B 98 -1 O ILE B 97 N GLN B 44
SHEET 1 D 8 LYS B 34 THR B 40 0
SHEET 2 D 8 GLY B 43 SER B 50 -1 O THR B 45 N ILE B 38
SHEET 3 D 8 ARG B 83 VAL B 87 -1 O ALA B 86 N ILE B 48
SHEET 4 D 8 PRO B 57 LEU B 61 1 N LEU B 58 O TYR B 85
SHEET 5 D 8 SER B 124 LEU B 129 1 O ILE B 127 N LEU B 61
SHEET 6 D 8 VAL B 147 LEU B 153 1 O LEU B 153 N GLY B 128
SHEET 7 D 8 ILE B 237 GLY B 242 1 O LEU B 238 N ILE B 152
SHEET 8 D 8 GLU B 265 ILE B 269 1 O ILE B 269 N LEU B 241
SHEET 1 E 3 LYS C 34 ILE C 38 0
SHEET 2 E 3 GLY C 43 SER C 50 -1 O THR C 45 N ILE C 38
SHEET 3 E 3 ILE C 97 PRO C 98 -1 O ILE C 97 N GLN C 44
SHEET 1 F 8 LYS C 34 ILE C 38 0
SHEET 2 F 8 GLY C 43 SER C 50 -1 O THR C 45 N ILE C 38
SHEET 3 F 8 ARG C 83 VAL C 87 -1 O THR C 84 N SER C 50
SHEET 4 F 8 PRO C 57 LEU C 61 1 N LEU C 58 O TYR C 85
SHEET 5 F 8 SER C 124 LEU C 129 1 O ILE C 127 N LEU C 61
SHEET 6 F 8 VAL C 147 LEU C 153 1 O LEU C 153 N GLY C 128
SHEET 7 F 8 ILE C 237 GLY C 242 1 O LEU C 238 N ILE C 152
SHEET 8 F 8 GLU C 265 ILE C 269 1 O ILE C 269 N LEU C 241
SHEET 1 G 3 CYS D 33 THR D 40 0
SHEET 2 G 3 GLY D 43 SER D 50 -1 O THR D 45 N ILE D 38
SHEET 3 G 3 ILE D 97 PRO D 98 -1 O ILE D 97 N GLN D 44
SHEET 1 H 8 CYS D 33 THR D 40 0
SHEET 2 H 8 GLY D 43 SER D 50 -1 O THR D 45 N ILE D 38
SHEET 3 H 8 ARG D 83 VAL D 87 -1 O ALA D 86 N ILE D 48
SHEET 4 H 8 PRO D 57 LEU D 61 1 N LEU D 58 O TYR D 85
SHEET 5 H 8 SER D 124 LEU D 129 1 O ILE D 127 N VAL D 59
SHEET 6 H 8 VAL D 147 LEU D 153 1 O LEU D 153 N GLY D 128
SHEET 7 H 8 ILE D 237 GLY D 242 1 O LEU D 238 N ILE D 152
SHEET 8 H 8 GLU D 265 ILE D 269 1 O ILE D 269 N LEU D 241
LINK OXT ALA B 294 MG MG B 295 1555 1555 1.86
LINK MG MG B 295 O HOH B 318 1555 1555 2.04
LINK MG MG B 295 O HOH B 333 1555 1555 2.10
LINK MG MG B 295 O HOH B 389 1555 1555 1.98
LINK MG MG B 295 O HOH B 376 1555 1555 2.05
LINK MG MG B 295 O HOH B 316 1555 1555 2.15
CISPEP 1 PHE A 221 PRO A 222 0 -1.03
CISPEP 2 PHE B 221 PRO B 222 0 1.03
CISPEP 3 PHE C 221 PRO C 222 0 -3.85
CISPEP 4 PHE D 221 PRO D 222 0 0.51
CRYST1 80.590 97.550 88.270 90.00 110.01 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 0.012410 0.000000 0.004520 0.00000
SCALE2 0.000000 0.010250 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012060 0.00000
TER 2268 ASN A 293
TER 4574 ALA B 294
TER 6868 ALA C 294
TER 9229 ALA D 294
MASTER 469 0 41 51 44 0 0 610230 4 349 96
END |