HEADER OXIDOREDUCTASE 07-OCT-08 3ETF
TITLE CRYSTAL STRUCTURE OF A PUTATIVE SUCCINATE-SEMIALDEHYDE DEHYDROGENASE
TITLE 2 FROM SALMONELLA TYPHIMURIUM LT2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE SUCCINATE-SEMIALDEHYDE DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 1.2.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 602;
SOURCE 4 STRAIN: LT2;
SOURCE 5 GENE: YNEI, STM1524;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PMCSG7
KEYWDS PUTATIVE SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS OF INFECTIOUS DISEASES, OXIDOREDUCTASE, CSGID
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.BRUNZELLE,E.EVDOKIMOVA,M.KUDRITSKA,Z.WAWRZAK,W.F.ANDERSON,
AUTHOR 2 A.SAVCHENK,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
AUTHOR 3 (CSGID)
REVDAT 11 27-DEC-23 3ETF 1 REMARK LINK
REVDAT 10 24-JAN-18 3ETF 1 AUTHOR
REVDAT 9 25-OCT-17 3ETF 1 REMARK
REVDAT 8 12-JUN-13 3ETF 1 JRNL
REVDAT 7 19-DEC-12 3ETF 1 JRNL
REVDAT 6 13-JUL-11 3ETF 1 VERSN
REVDAT 5 09-JUN-09 3ETF 1 REVDAT
REVDAT 4 24-FEB-09 3ETF 1 VERSN
REVDAT 3 16-DEC-08 3ETF 1 TITLE
REVDAT 2 11-NOV-08 3ETF 1 REMARK
REVDAT 1 04-NOV-08 3ETF 0
JRNL AUTH H.ZHENG,A.BELIAVSKY,A.TCHIGVINTSEV,J.S.BRUNZELLE,G.BROWN,
JRNL AUTH 2 R.FLICK,E.EVDOKIMOVA,Z.WAWRZAK,R.MAHADEVAN,W.F.ANDERSON,
JRNL AUTH 3 A.SAVCHENKO,A.F.YAKUNIN
JRNL TITL STRUCTURE AND ACTIVITY OF THE NAD(P)(+) -DEPENDENT SUCCINATE
JRNL TITL 2 SEMIALDEHYDE DEHYDROGENASE YNEI FROM SALMONELLA TYPHIMURIUM.
JRNL REF PROTEINS V. 81 1031 2013
JRNL REFN ISSN 0887-3585
JRNL PMID 23229889
JRNL DOI 10.1002/PROT.24227
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 206465
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 10912
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 15035
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.03
REMARK 3 BIN R VALUE (WORKING SET) : 0.1940
REMARK 3 BIN FREE R VALUE SET COUNT : 787
REMARK 3 BIN FREE R VALUE : 0.2380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13556
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 1985
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.42000
REMARK 3 B22 (A**2) : -0.42000
REMARK 3 B33 (A**2) : 0.63000
REMARK 3 B12 (A**2) : -0.21000
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): 0.105
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.102
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.064
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.060
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 14181 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 19341 ; 1.404 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1906 ; 4.624 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 603 ;32.088 ;24.660
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2235 ;11.292 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 83 ;16.108 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2188 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10983 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 6882 ; 0.199 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 10003 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1587 ; 0.156 ; 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): 80 ; 0.236 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 54 ; 0.281 ; 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): 9578 ; 1.024 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14789 ; 1.342 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5267 ; 2.599 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4552 ; 3.972 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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: NULL
REMARK 4
REMARK 4 3ETF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-08.
REMARK 100 THE DEPOSITION ID IS D_1000049744.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9787
REMARK 200 MONOCHROMATOR : DIAMOND 111
REMARK 200 OPTICS : BE LENS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 206465
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.30
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.6500
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 : 11.42
REMARK 200 R MERGE FOR SHELL (I) : 0.46900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.970
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M NA FORMATE, 0.1M NA ACETATE, PH
REMARK 280 4.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 164.68533
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 82.34267
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 82.34267
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 164.68533
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 MSE A 1
REMARK 465 THR A 2
REMARK 465 MSE A 3
REMARK 465 MSE A 4
REMARK 465 THR A 5
REMARK 465 MSE B 1
REMARK 465 THR B 2
REMARK 465 MSE B 3
REMARK 465 MSE B 4
REMARK 465 THR B 5
REMARK 465 ALA B 6
REMARK 465 MSE C 1
REMARK 465 THR C 2
REMARK 465 MSE C 3
REMARK 465 MSE C 4
REMARK 465 THR C 5
REMARK 465 ALA C 6
REMARK 465 THR C 7
REMARK 465 MSE D 1
REMARK 465 THR D 2
REMARK 465 MSE D 3
REMARK 465 MSE D 4
REMARK 465 THR D 5
REMARK 465 ALA D 6
REMARK 465 THR D 7
REMARK 465 GLN D 8
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 THR B 7 OG1 CG2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 215 CG CD NE CZ NH1 NH2
REMARK 480 GLU A 303 OE1 OE2
REMARK 480 LYS A 377 CD CE NZ
REMARK 480 ARG B 215 CG CD NE CZ NH1 NH2
REMARK 480 LYS B 377 CE NZ
REMARK 480 ARG C 215 CG CD NE CZ NH1 NH2
REMARK 480 ARG D 215 CG CD NE CZ NH1 NH2
REMARK 480 GLU D 278 CG CD OE1 OE2
REMARK 480 LYS D 377 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD2 ASP A 317 OD2 ASP C 317 1.69
REMARK 500 O HOH B 988 O HOH C 1321 2.00
REMARK 500 O HOH A 960 O HOH C 960 2.05
REMARK 500 O HOH B 1136 O HOH B 1245 2.10
REMARK 500 O HOH B 1179 O HOH B 1347 2.12
REMARK 500 O HOH C 1111 O HOH C 1169 2.15
REMARK 500 O HOH C 920 O HOH C 1324 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU A 303 O HOH C 979 5665 1.88
REMARK 500 O HOH A 598 O HOH C 979 5665 1.91
REMARK 500 O HOH A 837 O HOH B 974 5665 1.99
REMARK 500 O HOH C 1198 O HOH D 763 5565 2.08
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 235 -162.83 -108.65
REMARK 500 ASN A 345 53.80 -113.00
REMARK 500 LYS A 435 -139.13 55.82
REMARK 500 LEU A 443 176.04 71.38
REMARK 500 SER A 444 -148.15 47.38
REMARK 500 LEU B 235 -159.86 -109.74
REMARK 500 ASN B 345 53.09 -111.32
REMARK 500 LEU B 393 -70.29 -90.78
REMARK 500 LYS B 435 -136.12 52.48
REMARK 500 LEU B 443 175.74 74.87
REMARK 500 SER B 444 -144.24 43.26
REMARK 500 LEU C 235 -165.26 -109.67
REMARK 500 LEU C 235 -165.26 -113.22
REMARK 500 ASN C 345 49.85 -105.72
REMARK 500 LEU C 393 -67.36 -91.13
REMARK 500 LYS C 435 -138.29 53.42
REMARK 500 LEU C 443 177.00 72.00
REMARK 500 SER C 444 -145.71 45.50
REMARK 500 LEU D 235 -159.30 -107.85
REMARK 500 ASP D 299 116.89 -33.70
REMARK 500 ASN D 345 53.99 -109.50
REMARK 500 LYS D 435 -137.66 53.34
REMARK 500 LEU D 443 175.25 73.20
REMARK 500 SER D 444 -146.13 47.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EFV RELATED DB: PDB
REMARK 900 RELATED ID: IDP01530 RELATED DB: TARGETDB
DBREF 3ETF A 1 462 UNP Q8ZPI3 Q8ZPI3_SALTY 1 462
DBREF 3ETF B 1 462 UNP Q8ZPI3 Q8ZPI3_SALTY 1 462
DBREF 3ETF C 1 462 UNP Q8ZPI3 Q8ZPI3_SALTY 1 462
DBREF 3ETF D 1 462 UNP Q8ZPI3 Q8ZPI3_SALTY 1 462
SEQRES 1 A 462 MSE THR MSE MSE THR ALA THR GLN ALA LEU SER VAL ASN
SEQRES 2 A 462 PRO ALA THR GLY GLN THR LEU ALA ALA MSE PRO TRP ALA
SEQRES 3 A 462 ASN ALA GLN GLU ILE GLU HIS ALA LEU SER LEU ALA ALA
SEQRES 4 A 462 SER GLY PHE LYS LYS TRP LYS MSE THR SER VAL ALA GLN
SEQRES 5 A 462 ARG ALA GLN THR LEU ARG ASP ILE GLY GLN ALA LEU ARG
SEQRES 6 A 462 ALA HIS ALA GLU GLU MSE ALA GLN CYS ILE THR ARG GLU
SEQRES 7 A 462 MSE GLY LYS PRO ILE LYS GLN ALA ARG ALA GLU VAL THR
SEQRES 8 A 462 LYS SER ALA ALA LEU CYS ASP TRP TYR ALA GLU HIS GLY
SEQRES 9 A 462 PRO ALA MSE LEU ASN PRO GLU PRO THR LEU VAL GLU ASN
SEQRES 10 A 462 GLN GLN ALA VAL ILE GLU TYR ARG PRO LEU GLY VAL ILE
SEQRES 11 A 462 LEU ALA ILE MSE PRO TRP ASN PHE PRO LEU TRP GLN VAL
SEQRES 12 A 462 LEU ARG GLY ALA VAL PRO ILE LEU LEU ALA GLY ASN SER
SEQRES 13 A 462 TYR LEU LEU LYS HIS ALA PRO ASN VAL THR GLY CYS ALA
SEQRES 14 A 462 GLN MSE ILE ALA ARG ILE LEU ALA GLU ALA GLY THR PRO
SEQRES 15 A 462 ALA GLY VAL TYR GLY TRP VAL ASN ALA ASN ASN GLU GLY
SEQRES 16 A 462 VAL SER GLN MSE ILE ASN ASP PRO ARG ILE ALA ALA VAL
SEQRES 17 A 462 THR VAL THR GLY SER VAL ARG ALA GLY ALA ALA ILE GLY
SEQRES 18 A 462 ALA GLN ALA GLY ALA ALA LEU LYS LYS CYS VAL LEU GLU
SEQRES 19 A 462 LEU GLY GLY SER ASP PRO PHE ILE VAL LEU ASN ASP ALA
SEQRES 20 A 462 ASP LEU GLU LEU ALA VAL LYS ALA ALA VAL ALA GLY ARG
SEQRES 21 A 462 TYR GLN ASN THR GLY GLN VAL CYS ALA ALA ALA LYS ARG
SEQRES 22 A 462 PHE ILE VAL GLU GLU GLY ILE ALA GLN ALA PHE THR ASP
SEQRES 23 A 462 ARG PHE VAL ALA ALA ALA ALA ALA LEU LYS MSE GLY ASP
SEQRES 24 A 462 PRO LEU VAL GLU GLU ASN ASP LEU GLY PRO MSE ALA ARG
SEQRES 25 A 462 PHE ASP LEU ARG ASP GLU LEU HIS GLN GLN VAL GLN ALA
SEQRES 26 A 462 SER VAL ALA GLU GLY ALA ARG LEU LEU LEU GLY GLY GLU
SEQRES 27 A 462 LYS ILE ALA GLY GLU GLY ASN TYR TYR ALA ALA THR VAL
SEQRES 28 A 462 LEU ALA ASP VAL THR PRO ASP MSE THR ALA PHE ARG GLN
SEQRES 29 A 462 GLU LEU PHE GLY PRO VAL ALA ALA ILE THR VAL ALA LYS
SEQRES 30 A 462 ASP ALA ALA HIS ALA LEU ALA LEU ALA ASN ASP SER GLU
SEQRES 31 A 462 PHE GLY LEU SER ALA THR ILE PHE THR ALA ASP ASP THR
SEQRES 32 A 462 LEU ALA ALA GLU MSE ALA ALA ARG LEU GLU CYS GLY GLY
SEQRES 33 A 462 VAL PHE ILE ASN GLY TYR SER ALA SER ASP ALA ARG VAL
SEQRES 34 A 462 ALA PHE GLY GLY VAL LYS LYS SER GLY PHE GLY ARG GLU
SEQRES 35 A 462 LEU SER HIS PHE GLY LEU HIS GLU PHE CYS ASN VAL GLN
SEQRES 36 A 462 THR VAL TRP LYS ASN ARG VAL
SEQRES 1 B 462 MSE THR MSE MSE THR ALA THR GLN ALA LEU SER VAL ASN
SEQRES 2 B 462 PRO ALA THR GLY GLN THR LEU ALA ALA MSE PRO TRP ALA
SEQRES 3 B 462 ASN ALA GLN GLU ILE GLU HIS ALA LEU SER LEU ALA ALA
SEQRES 4 B 462 SER GLY PHE LYS LYS TRP LYS MSE THR SER VAL ALA GLN
SEQRES 5 B 462 ARG ALA GLN THR LEU ARG ASP ILE GLY GLN ALA LEU ARG
SEQRES 6 B 462 ALA HIS ALA GLU GLU MSE ALA GLN CYS ILE THR ARG GLU
SEQRES 7 B 462 MSE GLY LYS PRO ILE LYS GLN ALA ARG ALA GLU VAL THR
SEQRES 8 B 462 LYS SER ALA ALA LEU CYS ASP TRP TYR ALA GLU HIS GLY
SEQRES 9 B 462 PRO ALA MSE LEU ASN PRO GLU PRO THR LEU VAL GLU ASN
SEQRES 10 B 462 GLN GLN ALA VAL ILE GLU TYR ARG PRO LEU GLY VAL ILE
SEQRES 11 B 462 LEU ALA ILE MSE PRO TRP ASN PHE PRO LEU TRP GLN VAL
SEQRES 12 B 462 LEU ARG GLY ALA VAL PRO ILE LEU LEU ALA GLY ASN SER
SEQRES 13 B 462 TYR LEU LEU LYS HIS ALA PRO ASN VAL THR GLY CYS ALA
SEQRES 14 B 462 GLN MSE ILE ALA ARG ILE LEU ALA GLU ALA GLY THR PRO
SEQRES 15 B 462 ALA GLY VAL TYR GLY TRP VAL ASN ALA ASN ASN GLU GLY
SEQRES 16 B 462 VAL SER GLN MSE ILE ASN ASP PRO ARG ILE ALA ALA VAL
SEQRES 17 B 462 THR VAL THR GLY SER VAL ARG ALA GLY ALA ALA ILE GLY
SEQRES 18 B 462 ALA GLN ALA GLY ALA ALA LEU LYS LYS CYS VAL LEU GLU
SEQRES 19 B 462 LEU GLY GLY SER ASP PRO PHE ILE VAL LEU ASN ASP ALA
SEQRES 20 B 462 ASP LEU GLU LEU ALA VAL LYS ALA ALA VAL ALA GLY ARG
SEQRES 21 B 462 TYR GLN ASN THR GLY GLN VAL CYS ALA ALA ALA LYS ARG
SEQRES 22 B 462 PHE ILE VAL GLU GLU GLY ILE ALA GLN ALA PHE THR ASP
SEQRES 23 B 462 ARG PHE VAL ALA ALA ALA ALA ALA LEU LYS MSE GLY ASP
SEQRES 24 B 462 PRO LEU VAL GLU GLU ASN ASP LEU GLY PRO MSE ALA ARG
SEQRES 25 B 462 PHE ASP LEU ARG ASP GLU LEU HIS GLN GLN VAL GLN ALA
SEQRES 26 B 462 SER VAL ALA GLU GLY ALA ARG LEU LEU LEU GLY GLY GLU
SEQRES 27 B 462 LYS ILE ALA GLY GLU GLY ASN TYR TYR ALA ALA THR VAL
SEQRES 28 B 462 LEU ALA ASP VAL THR PRO ASP MSE THR ALA PHE ARG GLN
SEQRES 29 B 462 GLU LEU PHE GLY PRO VAL ALA ALA ILE THR VAL ALA LYS
SEQRES 30 B 462 ASP ALA ALA HIS ALA LEU ALA LEU ALA ASN ASP SER GLU
SEQRES 31 B 462 PHE GLY LEU SER ALA THR ILE PHE THR ALA ASP ASP THR
SEQRES 32 B 462 LEU ALA ALA GLU MSE ALA ALA ARG LEU GLU CYS GLY GLY
SEQRES 33 B 462 VAL PHE ILE ASN GLY TYR SER ALA SER ASP ALA ARG VAL
SEQRES 34 B 462 ALA PHE GLY GLY VAL LYS LYS SER GLY PHE GLY ARG GLU
SEQRES 35 B 462 LEU SER HIS PHE GLY LEU HIS GLU PHE CYS ASN VAL GLN
SEQRES 36 B 462 THR VAL TRP LYS ASN ARG VAL
SEQRES 1 C 462 MSE THR MSE MSE THR ALA THR GLN ALA LEU SER VAL ASN
SEQRES 2 C 462 PRO ALA THR GLY GLN THR LEU ALA ALA MSE PRO TRP ALA
SEQRES 3 C 462 ASN ALA GLN GLU ILE GLU HIS ALA LEU SER LEU ALA ALA
SEQRES 4 C 462 SER GLY PHE LYS LYS TRP LYS MSE THR SER VAL ALA GLN
SEQRES 5 C 462 ARG ALA GLN THR LEU ARG ASP ILE GLY GLN ALA LEU ARG
SEQRES 6 C 462 ALA HIS ALA GLU GLU MSE ALA GLN CYS ILE THR ARG GLU
SEQRES 7 C 462 MSE GLY LYS PRO ILE LYS GLN ALA ARG ALA GLU VAL THR
SEQRES 8 C 462 LYS SER ALA ALA LEU CYS ASP TRP TYR ALA GLU HIS GLY
SEQRES 9 C 462 PRO ALA MSE LEU ASN PRO GLU PRO THR LEU VAL GLU ASN
SEQRES 10 C 462 GLN GLN ALA VAL ILE GLU TYR ARG PRO LEU GLY VAL ILE
SEQRES 11 C 462 LEU ALA ILE MSE PRO TRP ASN PHE PRO LEU TRP GLN VAL
SEQRES 12 C 462 LEU ARG GLY ALA VAL PRO ILE LEU LEU ALA GLY ASN SER
SEQRES 13 C 462 TYR LEU LEU LYS HIS ALA PRO ASN VAL THR GLY CYS ALA
SEQRES 14 C 462 GLN MSE ILE ALA ARG ILE LEU ALA GLU ALA GLY THR PRO
SEQRES 15 C 462 ALA GLY VAL TYR GLY TRP VAL ASN ALA ASN ASN GLU GLY
SEQRES 16 C 462 VAL SER GLN MSE ILE ASN ASP PRO ARG ILE ALA ALA VAL
SEQRES 17 C 462 THR VAL THR GLY SER VAL ARG ALA GLY ALA ALA ILE GLY
SEQRES 18 C 462 ALA GLN ALA GLY ALA ALA LEU LYS LYS CYS VAL LEU GLU
SEQRES 19 C 462 LEU GLY GLY SER ASP PRO PHE ILE VAL LEU ASN ASP ALA
SEQRES 20 C 462 ASP LEU GLU LEU ALA VAL LYS ALA ALA VAL ALA GLY ARG
SEQRES 21 C 462 TYR GLN ASN THR GLY GLN VAL CYS ALA ALA ALA LYS ARG
SEQRES 22 C 462 PHE ILE VAL GLU GLU GLY ILE ALA GLN ALA PHE THR ASP
SEQRES 23 C 462 ARG PHE VAL ALA ALA ALA ALA ALA LEU LYS MSE GLY ASP
SEQRES 24 C 462 PRO LEU VAL GLU GLU ASN ASP LEU GLY PRO MSE ALA ARG
SEQRES 25 C 462 PHE ASP LEU ARG ASP GLU LEU HIS GLN GLN VAL GLN ALA
SEQRES 26 C 462 SER VAL ALA GLU GLY ALA ARG LEU LEU LEU GLY GLY GLU
SEQRES 27 C 462 LYS ILE ALA GLY GLU GLY ASN TYR TYR ALA ALA THR VAL
SEQRES 28 C 462 LEU ALA ASP VAL THR PRO ASP MSE THR ALA PHE ARG GLN
SEQRES 29 C 462 GLU LEU PHE GLY PRO VAL ALA ALA ILE THR VAL ALA LYS
SEQRES 30 C 462 ASP ALA ALA HIS ALA LEU ALA LEU ALA ASN ASP SER GLU
SEQRES 31 C 462 PHE GLY LEU SER ALA THR ILE PHE THR ALA ASP ASP THR
SEQRES 32 C 462 LEU ALA ALA GLU MSE ALA ALA ARG LEU GLU CYS GLY GLY
SEQRES 33 C 462 VAL PHE ILE ASN GLY TYR SER ALA SER ASP ALA ARG VAL
SEQRES 34 C 462 ALA PHE GLY GLY VAL LYS LYS SER GLY PHE GLY ARG GLU
SEQRES 35 C 462 LEU SER HIS PHE GLY LEU HIS GLU PHE CYS ASN VAL GLN
SEQRES 36 C 462 THR VAL TRP LYS ASN ARG VAL
SEQRES 1 D 462 MSE THR MSE MSE THR ALA THR GLN ALA LEU SER VAL ASN
SEQRES 2 D 462 PRO ALA THR GLY GLN THR LEU ALA ALA MSE PRO TRP ALA
SEQRES 3 D 462 ASN ALA GLN GLU ILE GLU HIS ALA LEU SER LEU ALA ALA
SEQRES 4 D 462 SER GLY PHE LYS LYS TRP LYS MSE THR SER VAL ALA GLN
SEQRES 5 D 462 ARG ALA GLN THR LEU ARG ASP ILE GLY GLN ALA LEU ARG
SEQRES 6 D 462 ALA HIS ALA GLU GLU MSE ALA GLN CYS ILE THR ARG GLU
SEQRES 7 D 462 MSE GLY LYS PRO ILE LYS GLN ALA ARG ALA GLU VAL THR
SEQRES 8 D 462 LYS SER ALA ALA LEU CYS ASP TRP TYR ALA GLU HIS GLY
SEQRES 9 D 462 PRO ALA MSE LEU ASN PRO GLU PRO THR LEU VAL GLU ASN
SEQRES 10 D 462 GLN GLN ALA VAL ILE GLU TYR ARG PRO LEU GLY VAL ILE
SEQRES 11 D 462 LEU ALA ILE MSE PRO TRP ASN PHE PRO LEU TRP GLN VAL
SEQRES 12 D 462 LEU ARG GLY ALA VAL PRO ILE LEU LEU ALA GLY ASN SER
SEQRES 13 D 462 TYR LEU LEU LYS HIS ALA PRO ASN VAL THR GLY CYS ALA
SEQRES 14 D 462 GLN MSE ILE ALA ARG ILE LEU ALA GLU ALA GLY THR PRO
SEQRES 15 D 462 ALA GLY VAL TYR GLY TRP VAL ASN ALA ASN ASN GLU GLY
SEQRES 16 D 462 VAL SER GLN MSE ILE ASN ASP PRO ARG ILE ALA ALA VAL
SEQRES 17 D 462 THR VAL THR GLY SER VAL ARG ALA GLY ALA ALA ILE GLY
SEQRES 18 D 462 ALA GLN ALA GLY ALA ALA LEU LYS LYS CYS VAL LEU GLU
SEQRES 19 D 462 LEU GLY GLY SER ASP PRO PHE ILE VAL LEU ASN ASP ALA
SEQRES 20 D 462 ASP LEU GLU LEU ALA VAL LYS ALA ALA VAL ALA GLY ARG
SEQRES 21 D 462 TYR GLN ASN THR GLY GLN VAL CYS ALA ALA ALA LYS ARG
SEQRES 22 D 462 PHE ILE VAL GLU GLU GLY ILE ALA GLN ALA PHE THR ASP
SEQRES 23 D 462 ARG PHE VAL ALA ALA ALA ALA ALA LEU LYS MSE GLY ASP
SEQRES 24 D 462 PRO LEU VAL GLU GLU ASN ASP LEU GLY PRO MSE ALA ARG
SEQRES 25 D 462 PHE ASP LEU ARG ASP GLU LEU HIS GLN GLN VAL GLN ALA
SEQRES 26 D 462 SER VAL ALA GLU GLY ALA ARG LEU LEU LEU GLY GLY GLU
SEQRES 27 D 462 LYS ILE ALA GLY GLU GLY ASN TYR TYR ALA ALA THR VAL
SEQRES 28 D 462 LEU ALA ASP VAL THR PRO ASP MSE THR ALA PHE ARG GLN
SEQRES 29 D 462 GLU LEU PHE GLY PRO VAL ALA ALA ILE THR VAL ALA LYS
SEQRES 30 D 462 ASP ALA ALA HIS ALA LEU ALA LEU ALA ASN ASP SER GLU
SEQRES 31 D 462 PHE GLY LEU SER ALA THR ILE PHE THR ALA ASP ASP THR
SEQRES 32 D 462 LEU ALA ALA GLU MSE ALA ALA ARG LEU GLU CYS GLY GLY
SEQRES 33 D 462 VAL PHE ILE ASN GLY TYR SER ALA SER ASP ALA ARG VAL
SEQRES 34 D 462 ALA PHE GLY GLY VAL LYS LYS SER GLY PHE GLY ARG GLU
SEQRES 35 D 462 LEU SER HIS PHE GLY LEU HIS GLU PHE CYS ASN VAL GLN
SEQRES 36 D 462 THR VAL TRP LYS ASN ARG VAL
MODRES 3ETF MSE A 23 MET SELENOMETHIONINE
MODRES 3ETF MSE A 47 MET SELENOMETHIONINE
MODRES 3ETF MSE A 71 MET SELENOMETHIONINE
MODRES 3ETF MSE A 79 MET SELENOMETHIONINE
MODRES 3ETF MSE A 107 MET SELENOMETHIONINE
MODRES 3ETF MSE A 134 MET SELENOMETHIONINE
MODRES 3ETF MSE A 171 MET SELENOMETHIONINE
MODRES 3ETF MSE A 199 MET SELENOMETHIONINE
MODRES 3ETF MSE A 297 MET SELENOMETHIONINE
MODRES 3ETF MSE A 310 MET SELENOMETHIONINE
MODRES 3ETF MSE A 359 MET SELENOMETHIONINE
MODRES 3ETF MSE A 408 MET SELENOMETHIONINE
MODRES 3ETF MSE B 23 MET SELENOMETHIONINE
MODRES 3ETF MSE B 47 MET SELENOMETHIONINE
MODRES 3ETF MSE B 71 MET SELENOMETHIONINE
MODRES 3ETF MSE B 79 MET SELENOMETHIONINE
MODRES 3ETF MSE B 107 MET SELENOMETHIONINE
MODRES 3ETF MSE B 134 MET SELENOMETHIONINE
MODRES 3ETF MSE B 171 MET SELENOMETHIONINE
MODRES 3ETF MSE B 199 MET SELENOMETHIONINE
MODRES 3ETF MSE B 297 MET SELENOMETHIONINE
MODRES 3ETF MSE B 310 MET SELENOMETHIONINE
MODRES 3ETF MSE B 359 MET SELENOMETHIONINE
MODRES 3ETF MSE B 408 MET SELENOMETHIONINE
MODRES 3ETF MSE C 23 MET SELENOMETHIONINE
MODRES 3ETF MSE C 47 MET SELENOMETHIONINE
MODRES 3ETF MSE C 71 MET SELENOMETHIONINE
MODRES 3ETF MSE C 79 MET SELENOMETHIONINE
MODRES 3ETF MSE C 107 MET SELENOMETHIONINE
MODRES 3ETF MSE C 134 MET SELENOMETHIONINE
MODRES 3ETF MSE C 171 MET SELENOMETHIONINE
MODRES 3ETF MSE C 199 MET SELENOMETHIONINE
MODRES 3ETF MSE C 297 MET SELENOMETHIONINE
MODRES 3ETF MSE C 310 MET SELENOMETHIONINE
MODRES 3ETF MSE C 359 MET SELENOMETHIONINE
MODRES 3ETF MSE C 408 MET SELENOMETHIONINE
MODRES 3ETF MSE D 23 MET SELENOMETHIONINE
MODRES 3ETF MSE D 47 MET SELENOMETHIONINE
MODRES 3ETF MSE D 71 MET SELENOMETHIONINE
MODRES 3ETF MSE D 79 MET SELENOMETHIONINE
MODRES 3ETF MSE D 107 MET SELENOMETHIONINE
MODRES 3ETF MSE D 134 MET SELENOMETHIONINE
MODRES 3ETF MSE D 171 MET SELENOMETHIONINE
MODRES 3ETF MSE D 199 MET SELENOMETHIONINE
MODRES 3ETF MSE D 297 MET SELENOMETHIONINE
MODRES 3ETF MSE D 310 MET SELENOMETHIONINE
MODRES 3ETF MSE D 359 MET SELENOMETHIONINE
MODRES 3ETF MSE D 408 MET SELENOMETHIONINE
HET MSE A 23 8
HET MSE A 47 8
HET MSE A 71 8
HET MSE A 79 8
HET MSE A 107 8
HET MSE A 134 8
HET MSE A 171 8
HET MSE A 199 8
HET MSE A 297 8
HET MSE A 310 8
HET MSE A 359 8
HET MSE A 408 8
HET MSE B 23 8
HET MSE B 47 8
HET MSE B 71 8
HET MSE B 79 8
HET MSE B 107 8
HET MSE B 134 8
HET MSE B 171 8
HET MSE B 199 8
HET MSE B 297 8
HET MSE B 310 8
HET MSE B 359 8
HET MSE B 408 8
HET MSE C 23 8
HET MSE C 47 8
HET MSE C 71 8
HET MSE C 79 8
HET MSE C 107 8
HET MSE C 134 8
HET MSE C 171 8
HET MSE C 199 8
HET MSE C 297 8
HET MSE C 310 8
HET MSE C 359 8
HET MSE C 408 8
HET MSE D 23 8
HET MSE D 47 8
HET MSE D 71 8
HET MSE D 79 8
HET MSE D 107 8
HET MSE D 134 8
HET MSE D 171 8
HET MSE D 199 8
HET MSE D 297 8
HET MSE D 310 8
HET MSE D 359 8
HET MSE D 408 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 48(C5 H11 N O2 SE)
FORMUL 5 HOH *1985(H2 O)
HELIX 1 1 ASN A 27 LYS A 46 1 20
HELIX 2 2 SER A 49 HIS A 67 1 19
HELIX 3 3 HIS A 67 GLY A 80 1 14
HELIX 4 4 PRO A 82 LEU A 108 1 27
HELIX 5 5 VAL A 115 GLN A 118 5 4
HELIX 6 6 LEU A 140 ALA A 153 1 14
HELIX 7 7 VAL A 165 ALA A 179 1 15
HELIX 8 8 ASN A 192 ASN A 201 1 10
HELIX 9 9 SER A 213 ALA A 227 1 15
HELIX 10 10 ASP A 248 GLN A 262 1 15
HELIX 11 11 ASN A 263 GLN A 266 5 4
HELIX 12 12 GLU A 278 LEU A 295 1 18
HELIX 13 13 ARG A 312 GLU A 329 1 18
HELIX 14 14 MSE A 359 GLN A 364 1 6
HELIX 15 15 ASP A 378 ASP A 388 1 11
HELIX 16 16 ASP A 401 LEU A 412 1 12
HELIX 17 17 VAL A 434 LYS A 436 5 3
HELIX 18 18 LEU A 443 GLU A 450 1 8
HELIX 19 19 ASN B 27 LYS B 46 1 20
HELIX 20 20 SER B 49 HIS B 67 1 19
HELIX 21 21 HIS B 67 GLY B 80 1 14
HELIX 22 22 PRO B 82 GLY B 104 1 23
HELIX 23 23 PRO B 105 ASN B 109 5 5
HELIX 24 24 VAL B 115 GLN B 118 5 4
HELIX 25 25 LEU B 140 ALA B 153 1 14
HELIX 26 26 VAL B 165 ALA B 179 1 15
HELIX 27 27 ASN B 192 ASN B 201 1 10
HELIX 28 28 SER B 213 ALA B 227 1 15
HELIX 29 29 ASP B 248 GLN B 262 1 15
HELIX 30 30 ASN B 263 GLN B 266 5 4
HELIX 31 31 ILE B 280 LEU B 295 1 16
HELIX 32 32 ARG B 312 GLY B 330 1 19
HELIX 33 33 MSE B 359 GLN B 364 1 6
HELIX 34 34 ASP B 378 ASP B 388 1 11
HELIX 35 35 ASP B 401 LEU B 412 1 12
HELIX 36 36 VAL B 434 LYS B 436 5 3
HELIX 37 37 LEU B 443 GLU B 450 1 8
HELIX 38 38 ASN C 27 LYS C 46 1 20
HELIX 39 39 SER C 49 HIS C 67 1 19
HELIX 40 40 HIS C 67 GLY C 80 1 14
HELIX 41 41 PRO C 82 GLY C 104 1 23
HELIX 42 42 PRO C 105 ASN C 109 5 5
HELIX 43 43 VAL C 115 GLN C 118 5 4
HELIX 44 44 LEU C 140 ALA C 153 1 14
HELIX 45 45 VAL C 165 ALA C 179 1 15
HELIX 46 46 ASN C 192 ASN C 201 1 10
HELIX 47 47 SER C 213 ALA C 227 1 15
HELIX 48 48 ASP C 248 GLN C 262 1 15
HELIX 49 49 ASN C 263 GLN C 266 5 4
HELIX 50 50 ILE C 280 LEU C 295 1 16
HELIX 51 51 ARG C 312 GLU C 329 1 18
HELIX 52 52 MSE C 359 GLN C 364 1 6
HELIX 53 53 ASP C 378 ASP C 388 1 11
HELIX 54 54 ASP C 401 LEU C 412 1 12
HELIX 55 55 LEU C 443 GLU C 450 1 8
HELIX 56 56 ASN D 27 LYS D 46 1 20
HELIX 57 57 SER D 49 HIS D 67 1 19
HELIX 58 58 HIS D 67 GLY D 80 1 14
HELIX 59 59 PRO D 82 GLY D 104 1 23
HELIX 60 60 PRO D 105 ASN D 109 5 5
HELIX 61 61 VAL D 115 GLN D 118 5 4
HELIX 62 62 LEU D 140 ALA D 153 1 14
HELIX 63 63 ALA D 162 ASN D 164 5 3
HELIX 64 64 VAL D 165 ALA D 179 1 15
HELIX 65 65 ASN D 192 ASN D 201 1 10
HELIX 66 66 SER D 213 ALA D 227 1 15
HELIX 67 67 ASP D 248 GLN D 262 1 15
HELIX 68 68 ASN D 263 GLN D 266 5 4
HELIX 69 69 GLU D 278 LEU D 295 1 18
HELIX 70 70 ARG D 312 GLY D 330 1 19
HELIX 71 71 MSE D 359 GLN D 364 1 6
HELIX 72 72 ASP D 378 ASP D 388 1 11
HELIX 73 73 ASP D 401 ALA D 410 1 10
HELIX 74 74 VAL D 434 LYS D 436 5 3
HELIX 75 75 LEU D 443 GLU D 450 1 8
SHEET 1 A 2 LEU A 10 VAL A 12 0
SHEET 2 A 2 THR A 19 ALA A 22 -1 O ALA A 21 N SER A 11
SHEET 1 B10 GLU A 111 PRO A 112 0
SHEET 2 B10 ALA A 120 PRO A 126 -1 O ILE A 122 N GLU A 111
SHEET 3 B10 CYS A 452 LYS A 459 -1 O GLN A 455 N GLU A 123
SHEET 4 B10 GLY D 416 ILE D 419 1 O VAL D 417 N THR A 456
SHEET 5 B10 ALA D 395 PHE D 398 1 N ALA D 395 O PHE D 418
SHEET 6 B10 ASP D 239 VAL D 243 1 N ILE D 242 O THR D 396
SHEET 7 B10 ALA D 271 GLU D 277 1 O GLU D 277 N VAL D 243
SHEET 8 B10 VAL D 370 ALA D 376 1 O THR D 374 N PHE D 274
SHEET 9 B10 THR D 350 ALA D 353 1 N LEU D 352 O ALA D 371
SHEET 10 B10 ARG D 332 LEU D 335 -1 N ARG D 332 O ALA D 353
SHEET 1 C 6 TYR A 186 TRP A 188 0
SHEET 2 C 6 SER A 156 LYS A 160 1 N LEU A 159 O GLY A 187
SHEET 3 C 6 VAL A 129 ILE A 133 1 N ALA A 132 O LYS A 160
SHEET 4 C 6 ILE A 205 THR A 211 1 O THR A 209 N LEU A 131
SHEET 5 C 6 CYS A 231 GLU A 234 1 O GLU A 234 N VAL A 210
SHEET 6 C 6 GLY A 438 PHE A 439 -1 O PHE A 439 N LEU A 233
SHEET 1 D10 ARG A 332 LEU A 335 0
SHEET 2 D10 THR A 350 ALA A 353 -1 O ALA A 353 N ARG A 332
SHEET 3 D10 VAL A 370 ALA A 376 1 O ALA A 371 N LEU A 352
SHEET 4 D10 ALA A 271 GLU A 277 1 N PHE A 274 O ALA A 372
SHEET 5 D10 ASP A 239 VAL A 243 1 N VAL A 243 O GLU A 277
SHEET 6 D10 ALA A 395 PHE A 398 1 O THR A 396 N ILE A 242
SHEET 7 D10 GLY A 416 ILE A 419 1 O PHE A 418 N ALA A 395
SHEET 8 D10 CYS D 452 LYS D 459 1 O THR D 456 N VAL A 417
SHEET 9 D10 ALA D 120 PRO D 126 -1 N GLU D 123 O GLN D 455
SHEET 10 D10 GLU D 111 PRO D 112 -1 N GLU D 111 O ILE D 122
SHEET 1 E 2 LEU B 10 VAL B 12 0
SHEET 2 E 2 THR B 19 ALA B 22 -1 O LEU B 20 N SER B 11
SHEET 1 F10 GLU B 111 PRO B 112 0
SHEET 2 F10 ALA B 120 PRO B 126 -1 O ILE B 122 N GLU B 111
SHEET 3 F10 CYS B 452 LYS B 459 -1 O GLN B 455 N GLU B 123
SHEET 4 F10 GLY C 416 ILE C 419 1 O VAL C 417 N TRP B 458
SHEET 5 F10 SER C 394 PHE C 398 1 N ILE C 397 O PHE C 418
SHEET 6 F10 ASP C 239 VAL C 243 1 N ILE C 242 O THR C 396
SHEET 7 F10 ALA C 271 GLU C 277 1 O GLU C 277 N VAL C 243
SHEET 8 F10 VAL C 370 ALA C 376 1 O ALA C 372 N PHE C 274
SHEET 9 F10 THR C 350 ALA C 353 1 N LEU C 352 O ALA C 371
SHEET 10 F10 ARG C 332 LEU C 335 -1 N ARG C 332 O ALA C 353
SHEET 1 G 6 TYR B 186 TRP B 188 0
SHEET 2 G 6 SER B 156 LYS B 160 1 N LEU B 159 O GLY B 187
SHEET 3 G 6 VAL B 129 ILE B 133 1 N ALA B 132 O LYS B 160
SHEET 4 G 6 ILE B 205 THR B 211 1 O ALA B 206 N VAL B 129
SHEET 5 G 6 CYS B 231 GLU B 234 1 O GLU B 234 N VAL B 210
SHEET 6 G 6 GLY B 438 PHE B 439 -1 O PHE B 439 N LEU B 233
SHEET 1 H10 ARG B 332 LEU B 335 0
SHEET 2 H10 THR B 350 ALA B 353 -1 O ALA B 353 N ARG B 332
SHEET 3 H10 VAL B 370 ALA B 376 1 O ALA B 371 N LEU B 352
SHEET 4 H10 ALA B 271 GLU B 277 1 N PHE B 274 O THR B 374
SHEET 5 H10 ASP B 239 VAL B 243 1 N PHE B 241 O ARG B 273
SHEET 6 H10 SER B 394 PHE B 398 1 O THR B 396 N ILE B 242
SHEET 7 H10 GLY B 416 ILE B 419 1 O PHE B 418 N ALA B 395
SHEET 8 H10 CYS C 452 LYS C 459 1 O THR C 456 N VAL B 417
SHEET 9 H10 ALA C 120 PRO C 126 -1 N GLU C 123 O GLN C 455
SHEET 10 H10 GLU C 111 PRO C 112 -1 N GLU C 111 O ILE C 122
SHEET 1 I 2 ALA C 9 VAL C 12 0
SHEET 2 I 2 THR C 19 MSE C 23 -1 O ALA C 21 N SER C 11
SHEET 1 J 6 TYR C 186 TRP C 188 0
SHEET 2 J 6 SER C 156 LYS C 160 1 N LEU C 159 O GLY C 187
SHEET 3 J 6 VAL C 129 ILE C 133 1 N ALA C 132 O LEU C 158
SHEET 4 J 6 ILE C 205 THR C 211 1 O ALA C 206 N VAL C 129
SHEET 5 J 6 LYS C 230 GLU C 234 1 O GLU C 234 N VAL C 210
SHEET 6 J 6 GLY C 438 PHE C 439 -1 O PHE C 439 N LEU C 233
SHEET 1 K 2 PHE C 391 GLY C 392 0
SHEET 2 K 2 VAL C 434 LYS C 435 -1 O VAL C 434 N GLY C 392
SHEET 1 L 2 LEU D 10 VAL D 12 0
SHEET 2 L 2 THR D 19 ALA D 22 -1 O LEU D 20 N SER D 11
SHEET 1 M 6 TYR D 186 TRP D 188 0
SHEET 2 M 6 SER D 156 LYS D 160 1 N LEU D 159 O GLY D 187
SHEET 3 M 6 VAL D 129 ILE D 133 1 N ALA D 132 O LYS D 160
SHEET 4 M 6 ILE D 205 THR D 211 1 O ALA D 206 N VAL D 129
SHEET 5 M 6 CYS D 231 GLU D 234 1 O GLU D 234 N VAL D 210
SHEET 6 M 6 GLY D 438 PHE D 439 -1 O PHE D 439 N LEU D 233
LINK C ALA A 22 N MSE A 23 1555 1555 1.33
LINK C MSE A 23 N PRO A 24 1555 1555 1.35
LINK C LYS A 46 N MSE A 47 1555 1555 1.34
LINK C MSE A 47 N THR A 48 1555 1555 1.34
LINK C GLU A 70 N MSE A 71 1555 1555 1.33
LINK C MSE A 71 N ALA A 72 1555 1555 1.33
LINK C GLU A 78 N MSE A 79 1555 1555 1.33
LINK C MSE A 79 N GLY A 80 1555 1555 1.34
LINK C ALA A 106 N MSE A 107 1555 1555 1.34
LINK C MSE A 107 N LEU A 108 1555 1555 1.33
LINK C ILE A 133 N MSE A 134 1555 1555 1.33
LINK C MSE A 134 N PRO A 135 1555 1555 1.35
LINK C GLN A 170 N MSE A 171 1555 1555 1.33
LINK C MSE A 171 N ILE A 172 1555 1555 1.33
LINK C GLN A 198 N MSE A 199 1555 1555 1.33
LINK C MSE A 199 N ILE A 200 1555 1555 1.33
LINK C LYS A 296 N MSE A 297 1555 1555 1.33
LINK C MSE A 297 N GLY A 298 1555 1555 1.33
LINK C PRO A 309 N MSE A 310 1555 1555 1.33
LINK C MSE A 310 N ALA A 311 1555 1555 1.33
LINK C AASP A 358 N MSE A 359 1555 1555 1.33
LINK C BASP A 358 N MSE A 359 1555 1555 1.33
LINK C MSE A 359 N THR A 360 1555 1555 1.33
LINK C AGLU A 407 N MSE A 408 1555 1555 1.33
LINK C BGLU A 407 N MSE A 408 1555 1555 1.33
LINK C MSE A 408 N ALA A 409 1555 1555 1.33
LINK C ALA B 22 N MSE B 23 1555 1555 1.33
LINK C MSE B 23 N PRO B 24 1555 1555 1.34
LINK C LYS B 46 N MSE B 47 1555 1555 1.34
LINK C MSE B 47 N THR B 48 1555 1555 1.33
LINK C GLU B 70 N MSE B 71 1555 1555 1.33
LINK C MSE B 71 N ALA B 72 1555 1555 1.33
LINK C GLU B 78 N MSE B 79 1555 1555 1.34
LINK C MSE B 79 N GLY B 80 1555 1555 1.34
LINK C ALA B 106 N MSE B 107 1555 1555 1.34
LINK C MSE B 107 N LEU B 108 1555 1555 1.33
LINK C ILE B 133 N MSE B 134 1555 1555 1.34
LINK C MSE B 134 N PRO B 135 1555 1555 1.34
LINK C GLN B 170 N MSE B 171 1555 1555 1.34
LINK C MSE B 171 N ILE B 172 1555 1555 1.33
LINK C GLN B 198 N MSE B 199 1555 1555 1.33
LINK C MSE B 199 N ILE B 200 1555 1555 1.33
LINK C LYS B 296 N MSE B 297 1555 1555 1.34
LINK C MSE B 297 N GLY B 298 1555 1555 1.32
LINK C PRO B 309 N MSE B 310 1555 1555 1.33
LINK C MSE B 310 N ALA B 311 1555 1555 1.34
LINK C ASP B 358 N MSE B 359 1555 1555 1.32
LINK C MSE B 359 N THR B 360 1555 1555 1.34
LINK C AGLU B 407 N MSE B 408 1555 1555 1.33
LINK C BGLU B 407 N MSE B 408 1555 1555 1.33
LINK C MSE B 408 N ALA B 409 1555 1555 1.33
LINK C ALA C 22 N MSE C 23 1555 1555 1.33
LINK C MSE C 23 N PRO C 24 1555 1555 1.35
LINK C LYS C 46 N MSE C 47 1555 1555 1.33
LINK C MSE C 47 N THR C 48 1555 1555 1.33
LINK C GLU C 70 N MSE C 71 1555 1555 1.33
LINK C MSE C 71 N ALA C 72 1555 1555 1.34
LINK C GLU C 78 N MSE C 79 1555 1555 1.33
LINK C MSE C 79 N GLY C 80 1555 1555 1.33
LINK C ALA C 106 N MSE C 107 1555 1555 1.33
LINK C MSE C 107 N LEU C 108 1555 1555 1.33
LINK C ILE C 133 N MSE C 134 1555 1555 1.34
LINK C MSE C 134 N PRO C 135 1555 1555 1.35
LINK C GLN C 170 N MSE C 171 1555 1555 1.34
LINK C MSE C 171 N ILE C 172 1555 1555 1.34
LINK C GLN C 198 N MSE C 199 1555 1555 1.33
LINK C MSE C 199 N ILE C 200 1555 1555 1.33
LINK C LYS C 296 N MSE C 297 1555 1555 1.33
LINK C MSE C 297 N GLY C 298 1555 1555 1.33
LINK C PRO C 309 N MSE C 310 1555 1555 1.33
LINK C MSE C 310 N ALA C 311 1555 1555 1.33
LINK C ASP C 358 N MSE C 359 1555 1555 1.33
LINK C MSE C 359 N THR C 360 1555 1555 1.34
LINK C AGLU C 407 N MSE C 408 1555 1555 1.33
LINK C BGLU C 407 N MSE C 408 1555 1555 1.33
LINK C MSE C 408 N ALA C 409 1555 1555 1.34
LINK C ALA D 22 N MSE D 23 1555 1555 1.33
LINK C MSE D 23 N PRO D 24 1555 1555 1.35
LINK C LYS D 46 N MSE D 47 1555 1555 1.34
LINK C MSE D 47 N THR D 48 1555 1555 1.33
LINK C GLU D 70 N MSE D 71 1555 1555 1.34
LINK C MSE D 71 N ALA D 72 1555 1555 1.34
LINK C GLU D 78 N MSE D 79 1555 1555 1.33
LINK C MSE D 79 N GLY D 80 1555 1555 1.34
LINK C ALA D 106 N MSE D 107 1555 1555 1.33
LINK C MSE D 107 N LEU D 108 1555 1555 1.33
LINK C ILE D 133 N MSE D 134 1555 1555 1.34
LINK C MSE D 134 N PRO D 135 1555 1555 1.35
LINK C GLN D 170 N MSE D 171 1555 1555 1.33
LINK C MSE D 171 N ILE D 172 1555 1555 1.33
LINK C GLN D 198 N MSE D 199 1555 1555 1.34
LINK C MSE D 199 N ILE D 200 1555 1555 1.33
LINK C LYS D 296 N MSE D 297 1555 1555 1.33
LINK C MSE D 297 N GLY D 298 1555 1555 1.33
LINK C PRO D 309 N MSE D 310 1555 1555 1.33
LINK C MSE D 310 N ALA D 311 1555 1555 1.33
LINK C ASP D 358 N MSE D 359 1555 1555 1.33
LINK C MSE D 359 N THR D 360 1555 1555 1.33
LINK C GLU D 407 N MSE D 408 1555 1555 1.33
LINK C MSE D 408 N ALA D 409 1555 1555 1.33
CRYST1 133.875 133.875 247.028 90.00 90.00 120.00 P 32 2 1 24
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 0.007470 0.004313 0.000000 0.00000
SCALE2 0.000000 0.008625 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004048 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
