HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 05-FEB-04 1S9U
TITLE ATOMIC STRUCTURE OF A PUTATIVE ANAEROBIC DEHYDROGENASE COMPONENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE COMPONENT OF ANAEROBIC DEHYDROGENASES;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 99287;
SOURCE 4 STRAIN: LT2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, ANAEROBIC DEHYDROGENASES COMPONENT, PSI, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG,
KEYWDS 3 UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.QIU,R.ZHANG,V.TERESHKO,Y.KIM,F.COLLART,A.JOACHIMIAK,A.KOSSIAKOFF,
AUTHOR 2 MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 6 13-JUL-11 1S9U 1 VERSN
REVDAT 5 07-JUL-09 1S9U 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1S9U 1 VERSN
REVDAT 3 22-JUL-08 1S9U 1 JRNL
REVDAT 2 18-JAN-05 1S9U 1 AUTHOR KEYWDS REMARK
REVDAT 1 08-JUN-04 1S9U 0
JRNL AUTH Y.QIU,R.ZHANG,T.A.BINKOWSKI,V.TERESHKO,A.JOACHIMIAK,
JRNL AUTH 2 A.KOSSIAKOFF
JRNL TITL THE 1.38 A CRYSTAL STRUCTURE OF DMSD PROTEIN FROM SALMONELLA
JRNL TITL 2 TYPHIMURIUM, A PROOFREADING CHAPERONE ON THE TAT PATHWAY.
JRNL REF PROTEINS V. 71 525 2008
JRNL REFN ISSN 0887-3585
JRNL PMID 18175314
JRNL DOI 10.1002/PROT.21828
REMARK 2
REMARK 2 RESOLUTION. 1.38 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.38
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.0
REMARK 3 NUMBER OF REFLECTIONS : 45922
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) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2481
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) : 1.38
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.42
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1704
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2990
REMARK 3 BIN FREE R VALUE SET COUNT : 112
REMARK 3 BIN FREE R VALUE : 0.3100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1633
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 264
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.74000
REMARK 3 B22 (A**2) : -0.35000
REMARK 3 B33 (A**2) : -0.23000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.19000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.053
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.056
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.034
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.848
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1741 ; 0.013 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1541 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2369 ; 1.396 ; 1.937
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3586 ; 1.230 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 199 ; 5.591 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 247 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1899 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 369 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 389 ; 0.258 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1705 ; 0.243 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 937 ; 0.088 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 165 ; 0.219 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 9 ; 0.089 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 58 ; 0.293 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 0.241 ; 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): 1012 ; 0.856 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1625 ; 1.584 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 729 ; 2.375 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 743 ; 3.777 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 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 204
REMARK 3 ORIGIN FOR THE GROUP (A): 21.9164 6.9277 5.2914
REMARK 3 T TENSOR
REMARK 3 T11: 0.0013 T22: 0.0071
REMARK 3 T33: 0.0077 T12: 0.0019
REMARK 3 T13: -0.0007 T23: 0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 0.3292 L22: 0.3301
REMARK 3 L33: 0.4930 L12: -0.0861
REMARK 3 L13: -0.0301 L23: -0.0788
REMARK 3 S TENSOR
REMARK 3 S11: 0.0072 S12: 0.0280 S13: 0.0201
REMARK 3 S21: -0.0014 S22: -0.0100 S23: -0.0119
REMARK 3 S31: -0.0064 S32: -0.0349 S33: 0.0027
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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1S9U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-04.
REMARK 100 THE RCSB ID CODE IS RCSB021547.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97945, 0.97929
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC-2
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85983
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 32.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.29000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.560
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 (%): 55.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 300, AMMONIUM SULFATE, IMIDAZOLE,
REMARK 280 GLYCEROL, PH 8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 42.70050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.67750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 42.70050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 39.67750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). THE BIOLOGICAL UNIT IS
REMARK 300 UNKNOWN.
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 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 622 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; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 PHE A 117
REMARK 465 GLU A 118
REMARK 465 MSE A 119
REMARK 465 GLN A 120
REMARK 465 GLN A 121
REMARK 465 ASN A 122
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 599 O HOH A 815 1.59
REMARK 500 OD1 ASP A 101 O HOH A 831 1.83
REMARK 500 O HOH A 581 O HOH A 914 2.10
REMARK 500 O HOH A 592 O HOH A 814 2.18
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 THR A 2 CA - CB - CG2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 ASP A 93 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG A 107 NE - CZ - NH2 ANGL. DEV. = -4.5 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 PRO A 86 41.83 -81.96
REMARK 500 ARG A 143 61.74 -103.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 678 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH A 771 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH A 932 DISTANCE = 5.37 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 307
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC23398 RELATED DB: TARGETDB
DBREF 1S9U A 1 204 UNP Q8ZPK0 DMSD_SALTY 1 204
SEQADV 1S9U SER A -2 UNP Q8ZPK0 CLONING ARTIFACT
SEQADV 1S9U ASP A -1 UNP Q8ZPK0 CLONING ARTIFACT
SEQADV 1S9U ALA A 0 UNP Q8ZPK0 CLONING ARTIFACT
SEQADV 1S9U GLU A 9 UNP Q8ZPK0 ASP 9 CONFLICT
SEQRES 1 A 207 SER ASP ALA MSE THR THR PHE LEU GLN ARG ASP GLU PHE
SEQRES 2 A 207 ALA VAL THR ALA ARG VAL LEU GLY ALA LEU PHE TYR TYR
SEQRES 3 A 207 SER PRO GLU SER HIS GLU THR ALA PRO LEU VAL GLN ALA
SEQRES 4 A 207 LEU LEU ASN ASP ASP TRP GLN ALA GLN TRP PRO LEU ASP
SEQRES 5 A 207 ALA GLU ALA LEU ALA PRO VAL ALA ALA MSE PHE LYS THR
SEQRES 6 A 207 HIS SER GLU GLU SER LEU PRO GLN ALA TRP GLN ARG LEU
SEQRES 7 A 207 PHE ILE GLY PRO TYR ALA LEU PRO SER PRO PRO TRP GLY
SEQRES 8 A 207 SER VAL TRP LEU ASP ARG GLU SER VAL LEU PHE GLY ASP
SEQRES 9 A 207 SER THR LEU ALA LEU ARG GLN TRP MSE ARG GLU ASN GLY
SEQRES 10 A 207 ILE GLN PHE GLU MSE GLN GLN ASN GLU PRO GLU ASP HIS
SEQRES 11 A 207 PHE GLY SER LEU LEU LEU LEU ALA ALA TRP LEU ALA GLU
SEQRES 12 A 207 ASN ASP ARG HIS HIS GLU CYS GLU GLN LEU LEU ALA TRP
SEQRES 13 A 207 HIS LEU PHE PRO TRP SER SER ARG PHE LEU ASP VAL PHE
SEQRES 14 A 207 ILE ASP HIS ALA GLY HIS PRO PHE TYR GLN ALA LEU GLY
SEQRES 15 A 207 GLN LEU ALA ARG LEU THR LEU ALA GLN TRP GLN ALA GLN
SEQRES 16 A 207 LEU ILE ILE PRO VAL ALA VAL LYS PRO LEU PHE ARG
MODRES 1S9U MSE A 1 MET SELENOMETHIONINE
MODRES 1S9U MSE A 59 MET SELENOMETHIONINE
MODRES 1S9U MSE A 110 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 59 8
HET MSE A 110 8
HET SO4 A 999 5
HET SO4 A1000 5
HET PEG A 303 7
HET PEG A 304 7
HET PEG A 305 7
HET PEG A 306 7
HET PEG A 307 7
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 1 MSE 3(C5 H11 N O2 SE)
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 PEG 5(C4 H10 O3)
FORMUL 9 HOH *264(H2 O)
HELIX 1 1 ASP A -1 GLN A 6 1 8
HELIX 2 2 ASP A 8 TYR A 23 1 16
HELIX 3 3 THR A 30 ASP A 40 1 11
HELIX 4 4 TRP A 42 TRP A 46 5 5
HELIX 5 5 ASP A 49 LYS A 61 1 13
HELIX 6 6 SER A 67 ILE A 77 1 11
HELIX 7 7 TRP A 87 ASP A 93 1 7
HELIX 8 8 GLY A 100 ASN A 113 1 14
HELIX 9 9 HIS A 127 ASN A 141 1 15
HELIX 10 10 ARG A 143 LEU A 155 1 13
HELIX 11 11 LEU A 155 ALA A 170 1 16
HELIX 12 12 HIS A 172 LEU A 193 1 22
LINK C ALA A 0 N MSE A 1 1555 1555 1.32
LINK C MSE A 1 N THR A 2 1555 1555 1.33
LINK C ALA A 58 N MSE A 59 1555 1555 1.32
LINK C MSE A 59 N PHE A 60 1555 1555 1.33
LINK C TRP A 109 N MSE A 110 1555 1555 1.33
LINK C MSE A 110 N ARG A 111 1555 1555 1.33
CISPEP 1 GLY A 78 PRO A 79 0 9.00
SITE 1 AC1 6 ASP A -1 SER A -2 ASP A 41 HOH A 627
SITE 2 AC1 6 HOH A 677 SO4 A1000
SITE 1 AC2 2 ASP A 41 SO4 A 999
SITE 1 AC3 4 ILE A 77 PRO A 79 ALA A 81 HOH A 843
SITE 1 AC4 6 HIS A 144 CYS A 147 GLU A 148 TRP A 189
SITE 2 AC4 6 HOH A 659 HOH A 742
SITE 1 AC5 3 LEU A 134 HOH A 879 HOH A 907
SITE 1 AC6 5 HOH A 546 HOH A 626 HOH A 684 HOH A 701
SITE 2 AC6 5 HOH A 817
SITE 1 AC7 4 GLU A 29 LEU A 33 HOH A 605 HOH A 773
CRYST1 85.401 79.355 43.470 90.00 115.14 90.00 C 1 2 1 4
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 0.011709 0.000000 0.005496 0.00000
SCALE2 0.000000 0.012602 0.000000 0.00000
SCALE3 0.000000 0.000000 0.025412 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
