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HEADER HYDROLASE 17-SEP-07 2RAU
TITLE CRYSTAL STRUCTURE OF A PUTATIVE LIPASE (NP_343859.1) FROM
TITLE 2 SULFOLOBUS SOLFATARICUS AT 1.85 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS P2;
SOURCE 3 ORGANISM_COMMON: ARCHAEA;
SOURCE 4 STRAIN: P2, DSM 1617, JCM 11322;
SOURCE 5 ATCC: 35092;
SOURCE 6 GENE: NP_343859.1, SSO2518;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS NP_343859.1, PUTATIVE LIPASE, STRUCTURAL GENOMICS, JOINT
KEYWDS 2 CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE
KEYWDS 3 INITIATIVE, PSI-2, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 1 09-OCT-07 2RAU 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF A PUTATIVE LIPASE
JRNL TITL 2 (NP_343859.1) FROM SULFOLOBUS SOLFATARICUS AT 1.85
JRNL TITL 3 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.85 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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 48690
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) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2458
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3380
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE SET COUNT : 176
REMARK 3 BIN FREE R VALUE : 0.2900
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 3243
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.94000
REMARK 3 B22 (A**2) : 0.94000
REMARK 3 B33 (A**2) : -1.41000
REMARK 3 B12 (A**2) : 0.47000
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): 0.093
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.094
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.072
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.584
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2991 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2049 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4067 ; 1.686 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4995 ; 1.019 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 366 ; 5.621 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 127 ;36.898 ;23.937
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 459 ;12.128 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;22.289 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 431 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3314 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 616 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 573 ; 0.215 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2133 ; 0.193 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1457 ; 0.187 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): 1473 ; 0.091 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 432 ; 0.205 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.104 ; 0.500
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.291 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 9 ; 0.200 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 27 ; 0.208 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 32 ; 0.248 ; 0.500
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 1 ; 0.066 ; 0.500
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): 1872 ; 2.059 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 721 ; 0.526 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2921 ; 2.974 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1359 ; 4.449 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1146 ; 6.341 ;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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 353
REMARK 3 ORIGIN FOR THE GROUP (A): 44.7960 32.7220 14.4800
REMARK 3 T TENSOR
REMARK 3 T11: -0.0599 T22: -0.0226
REMARK 3 T33: -0.1573 T12: -0.0186
REMARK 3 T13: 0.0070 T23: -0.0243
REMARK 3 L TENSOR
REMARK 3 L11: 0.5262 L22: 0.4994
REMARK 3 L33: 1.6878 L12: 0.0195
REMARK 3 L13: 0.0106 L23: 0.3130
REMARK 3 S TENSOR
REMARK 3 S11: -0.0165 S12: 0.0573 S13: -0.0276
REMARK 3 S21: 0.0063 S22: -0.0706 S23: 0.1382
REMARK 3 S31: 0.1543 S32: -0.2635 S33: 0.0871
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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. CALCIUM IONS, UNKNOWN LIGAND,
REMARK 3 POLYETHYLENE GLYCOL AND ETHYLENE GLYCOL MOLECULES ARE MODELED
REMARK 3 IN THE STRUCTURE. 5. RESIDUES 0, 1, 186 AND 187 ARE DISORDERED
REMARK 3 AND NOT MODELED IN THE STRUCTURE.
REMARK 4
REMARK 4 2RAU 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 RCSB044636.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUL-2007
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
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) : 0.91837, 0.97937, 0.97916
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 : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48739
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 28.548
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : 0.10500
REMARK 200 FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.89600
REMARK 200 R SYM FOR SHELL (I) : 0.89600
REMARK 200 FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NANODROP, 0.2M CACL2, 28.0% PEG
REMARK 280 400, 0.1M HEPES PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,1/3+Z
REMARK 290 3555 -X+Y,-X,2/3+Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,2/3-Z
REMARK 290 6555 -X,-X+Y,1/3-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.67733
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 93.35467
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 93.35467
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 46.67733
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.
REMARK 300 SIZE EXCLUSION CHROMATOGRAPHY SUPPORTS THE ASSIGNMENT
REMARK 300 OF A MONOMER AS A 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: MONOMER
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 2010 ANGSTROM**2
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 BIOMT1 2 -0.500000 -0.866025 0.000000 124.99950
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 72.16849
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 46.67733
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 374 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 443 LIES ON A SPECIAL POSITION.
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 GLY A 0
REMARK 465 MSE A 1
REMARK 465 PRO A 186
REMARK 465 LYS A 187
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 TYR A 2 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 3 CD OE1 OE2
REMARK 470 GLU A 4 CD OE1 OE2
REMARK 470 LYS A 110 CD CE NZ
REMARK 470 HIS A 182 CG ND1 CD2 CE1 NE2
REMARK 470 ILE A 184 CG1 CG2 CD1
REMARK 470 ARG A 185 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 197 CG CD OE1 OE2
REMARK 470 LYS A 233 CE NZ
REMARK 470 ASP A 284 CG OD1 OD2
REMARK 470 LYS A 286 CG CD CE NZ
REMARK 470 GLU A 290 CG CD OE1 OE2
REMARK 470 GLN A 307 OE1 NE2
REMARK 470 SER A 311 OG
REMARK 470 LYS A 312 CG CD CE NZ
REMARK 470 ILE A 313 CG1 CG2 CD1
REMARK 470 SER A 316 OG
REMARK 470 LYS A 324 CD CE NZ
REMARK 470 LYS A 347 CE NZ
REMARK 470 ARG A 353 CG CD NE CZ NH1 NH2
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 GLU A 3 -39.24 -37.63
REMARK 500 ARG A 29 -168.15 -117.91
REMARK 500 ASP A 50 -156.20 65.42
REMARK 500 ASP A 111 -122.62 53.47
REMARK 500 SER A 151 -123.35 60.48
REMARK 500 TYR A 258 61.51 63.27
REMARK 500 GLU A 282 33.31 -95.17
REMARK 500 PHE A 304 -58.69 -147.07
REMARK 500 VAL A 341 -61.36 -120.03
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 CA A 355 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 141 O
REMARK 620 2 GLU A 143 OE1 102.9
REMARK 620 3 GLU A 143 OE2 98.2 51.8
REMARK 620 4 HOH A 445 O 157.6 78.8 100.1
REMARK 620 5 HOH A 486 O 82.9 125.2 73.4 114.7
REMARK 620 N 1 2 3 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 375699 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 2RAU A 1 353 UNP Q97VU1 Q97VU1_SULSO 1 353
SEQADV 2RAU GLY A 0 UNP Q97VU1 LEADER SEQUENCE
SEQRES 1 A 354 GLY MSE TYR GLU GLU TRP LYS ILE VAL LYS ARG GLU ALA
SEQRES 2 A 354 PRO ILE LEU GLY ASN ASP GLN LEU ILE GLU ASN ILE TRP
SEQRES 3 A 354 LYS MSE LYS ARG GLU ASP SER PRO TYR ASP ILE ILE SER
SEQRES 4 A 354 LEU HIS LYS VAL ASN LEU ILE GLY GLY GLY ASN ASP ALA
SEQRES 5 A 354 VAL LEU ILE LEU PRO GLY THR TRP SER SER GLY GLU GLN
SEQRES 6 A 354 LEU VAL THR ILE SER TRP ASN GLY VAL HIS TYR THR ILE
SEQRES 7 A 354 PRO ASP TYR ARG LYS SER ILE VAL LEU TYR LEU ALA ARG
SEQRES 8 A 354 ASN GLY PHE ASN VAL TYR THR ILE ASP TYR ARG THR HIS
SEQRES 9 A 354 TYR VAL PRO PRO PHE LEU LYS ASP ARG GLN LEU SER PHE
SEQRES 10 A 354 THR ALA ASN TRP GLY TRP SER THR TRP ILE SER ASP ILE
SEQRES 11 A 354 LYS GLU VAL VAL SER PHE ILE LYS ARG ASP SER GLY GLN
SEQRES 12 A 354 GLU ARG ILE TYR LEU ALA GLY GLU SER PHE GLY GLY ILE
SEQRES 13 A 354 ALA ALA LEU ASN TYR SER SER LEU TYR TRP LYS ASN ASP
SEQRES 14 A 354 ILE LYS GLY LEU ILE LEU LEU ASP GLY GLY PRO THR LYS
SEQRES 15 A 354 HIS GLY ILE ARG PRO LYS PHE TYR THR PRO GLU VAL ASN
SEQRES 16 A 354 SER ILE GLU GLU MSE GLU ALA LYS GLY ILE TYR VAL ILE
SEQRES 17 A 354 PRO SER ARG GLY GLY PRO ASN ASN PRO ILE TRP SER TYR
SEQRES 18 A 354 ALA LEU ALA ASN PRO ASP MSE PRO SER PRO ASP PRO LYS
SEQRES 19 A 354 TYR LYS SER ILE SER ASP PHE LEU MSE ASP SER LEU TYR
SEQRES 20 A 354 VAL THR GLY SER ALA ASN PRO TYR ASP TYR PRO TYR SER
SEQRES 21 A 354 LYS LYS GLU ASP MSE PHE PRO ILE LEU ALA SER PHE ASP
SEQRES 22 A 354 PRO TYR TRP PRO TYR ARG LEU SER LEU GLU ARG ASP LEU
SEQRES 23 A 354 LYS PHE ASP TYR GLU GLY ILE LEU VAL PRO THR ILE ALA
SEQRES 24 A 354 PHE VAL SER GLU ARG PHE GLY ILE GLN ILE PHE ASP SER
SEQRES 25 A 354 LYS ILE LEU PRO SER ASN SER GLU ILE ILE LEU LEU LYS
SEQRES 26 A 354 GLY TYR GLY HIS LEU ASP VAL TYR THR GLY GLU ASN SER
SEQRES 27 A 354 GLU LYS ASP VAL ASN SER VAL VAL LEU LYS TRP LEU SER
SEQRES 28 A 354 GLN GLN ARG
MODRES 2RAU MSE A 27 MET SELENOMETHIONINE
MODRES 2RAU MSE A 199 MET SELENOMETHIONINE
MODRES 2RAU MSE A 227 MET SELENOMETHIONINE
MODRES 2RAU MSE A 242 MET SELENOMETHIONINE
MODRES 2RAU MSE A 264 MET SELENOMETHIONINE
HET MSE A 27 8
HET MSE A 199 8
HET MSE A 227 8
HET MSE A 242 8
HET MSE A 264 8
HET CA A 354 1
HET CA A 355 1
HET CA A 356 1
HET EDO A 357 4
HET PG4 A 358 13
HET UNL A 359 20
HET PEG A 360 7
HET PEG A 361 7
HET PEG A 362 7
HET PEG A 363 7
HETNAM MSE SELENOMETHIONINE
HETNAM CA CALCIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM UNL UNKNOWN LIGAND
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 5(C5 H11 N O2 SE)
FORMUL 2 CA 3(CA 2+)
FORMUL 5 EDO C2 H6 O2
FORMUL 6 PG4 C8 H18 O5
FORMUL 8 PEG 4(C4 H10 O3)
FORMUL 12 HOH *333(H2 O)
HELIX 1 1 SER A 61 ILE A 68 1 8
HELIX 2 2 ASP A 79 LYS A 82 5 4
HELIX 3 3 SER A 83 ASN A 91 1 9
HELIX 4 4 TYR A 100 VAL A 105 5 6
HELIX 5 5 LYS A 110 ALA A 118 5 9
HELIX 6 6 GLY A 121 GLY A 141 1 21
HELIX 7 7 SER A 151 ASP A 168 1 18
HELIX 8 8 SER A 195 GLY A 203 1 9
HELIX 9 9 PRO A 216 ASN A 224 1 9
HELIX 10 10 SER A 236 THR A 248 1 13
HELIX 11 11 LYS A 260 SER A 270 1 11
HELIX 12 12 TYR A 277 GLU A 282 1 6
HELIX 13 13 PHE A 304 PHE A 309 1 6
HELIX 14 14 ASP A 310 LEU A 314 5 5
HELIX 15 15 GLY A 327 TYR A 332 5 6
HELIX 16 16 ASN A 336 VAL A 341 1 6
HELIX 17 17 VAL A 341 ARG A 353 1 13
SHEET 1 A 9 LYS A 6 ILE A 14 0
SHEET 2 A 9 ASN A 17 LYS A 28 -1 O ILE A 24 N VAL A 8
SHEET 3 A 9 ILE A 36 LEU A 44 -1 O ASN A 43 N ILE A 21
SHEET 4 A 9 PHE A 93 ASP A 99 -1 O VAL A 95 N VAL A 42
SHEET 5 A 9 ASN A 49 LEU A 55 1 N VAL A 52 O TYR A 96
SHEET 6 A 9 ILE A 145 GLU A 150 1 O ALA A 148 N LEU A 53
SHEET 7 A 9 ILE A 169 LEU A 175 1 O LEU A 175 N GLY A 149
SHEET 8 A 9 THR A 296 SER A 301 1 O PHE A 299 N LEU A 174
SHEET 9 A 9 GLU A 319 LEU A 323 1 O ILE A 321 N ALA A 298
SHEET 1 B 2 SER A 69 TRP A 70 0
SHEET 2 B 2 VAL A 73 HIS A 74 -1 O VAL A 73 N TRP A 70
SHEET 1 C 2 VAL A 206 PRO A 208 0
SHEET 2 C 2 TYR A 274 PRO A 276 -1 O TRP A 275 N ILE A 207
LINK O GLY A 141 CA CA A 355 1555 1555 2.38
LINK OE1 GLU A 143 CA CA A 355 1555 1555 2.66
LINK OE2 GLU A 143 CA CA A 355 1555 1555 2.19
LINK CA CA A 355 O HOH A 445 1555 1555 2.51
LINK CA CA A 355 O HOH A 486 1555 1555 2.66
CISPEP 1 GLU A 30 ASP A 31 0 2.08
CISPEP 2 TYR A 256 PRO A 257 0 6.71
CRYST1 83.333 83.333 140.032 90.00 90.00 120.00 P 31 2 1 6
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 0.012000 0.006928 0.000000 0.00000
SCALE2 0.000000 0.013856 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007141 0.00000
TER 2843 ARG A 353
MASTER 373 0 15 17 13 0 0 6 3243 1 92 28
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