HEADER TRANSPORT PROTEIN 23-NOV-09 3KSM
TITLE CRYSTAL STRUCTURE OF ABC-TYPE SUGAR TRANSPORT SYSTEM, PERIPLASMIC
TITLE 2 COMPONENT FROM HAHELLA CHEJUENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ABC-TYPE SUGAR TRANSPORT SYSTEM, PERIPLASMIC COMPONENT;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: ABC-TYPE SUGAR TRANSPORT;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HAHELLA CHEJUENSIS;
SOURCE 3 ORGANISM_TAXID: 349521;
SOURCE 4 STRAIN: KCTC 2396;
SOURCE 5 GENE: HCH_06819;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PSGX3(BC)
KEYWDS ABC-TYPE SUGAR TRANSPORT SYSTEM, PERIPLASMIC COMPONENT, PSI-II,
KEYWDS 2 11023L, STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, NEW YORK
KEYWDS 3 SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS, NYSGXRC, TRANSPORT
KEYWDS 4 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.BAGARIA,D.KUMARAN,S.K.BURLEY,S.SWAMINATHAN,NEW YORK SGX RESEARCH
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 4 10-FEB-21 3KSM 1 AUTHOR JRNL HETSYN
REVDAT 3 29-JUL-20 3KSM 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 13-JUL-11 3KSM 1 VERSN
REVDAT 1 15-DEC-09 3KSM 0
JRNL AUTH A.BAGARIA,D.KUMARAN,S.K.BURLEY,S.SWAMINATHAN
JRNL TITL CRYSTAL STRUCTURE OF ABC-TYPE SUGAR TRANSPORT SYSTEM,
JRNL TITL 2 PERIPLASMIC COMPONENT FROM HAHELLA CHEJUENSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 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
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 38369
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) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2028
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2675
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.1720
REMARK 3 BIN FREE R VALUE SET COUNT : 150
REMARK 3 BIN FREE R VALUE : 0.2270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4196
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 349
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.25
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.01000
REMARK 3 B12 (A**2) : 0.00000
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): 0.152
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.138
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.084
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.737
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4301 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5837 ; 1.478 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 555 ; 5.662 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 196 ;36.848 ;24.184
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 729 ;14.437 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 37 ;17.661 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 682 ; 0.123 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3241 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1980 ; 0.197 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2954 ; 0.300 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 351 ; 0.167 ; 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): 48 ; 0.170 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 0.161 ; 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): 2838 ; 1.010 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4367 ; 1.518 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1650 ; 2.761 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1466 ; 4.100 ; 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 : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3KSM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-09.
REMARK 100 THE DEPOSITION ID IS D_1000056396.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SI(111)CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38369
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.17800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.680
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5 M AMMONIUM SULFATE, 0.1 M HEPES PH
REMARK 280 7.5, 30% V/V (+/-)-2-METHYL-2,4-PENTANEDIOL, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,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
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: DIMERIC
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 PRO B 39
REMARK 465 PRO B 97
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 ASP A 129 -41.64 74.78
REMARK 500 LEU A 173 -74.88 -92.45
REMARK 500 ALA A 202 54.17 -148.21
REMARK 500 ASP A 259 169.41 74.57
REMARK 500 ASN A 280 70.53 -119.58
REMARK 500 ASP B 129 -43.34 73.69
REMARK 500 LEU B 173 -71.66 -94.98
REMARK 500 ARG B 174 119.95 -166.16
REMARK 500 ALA B 202 55.82 -145.14
REMARK 500 ASP B 259 170.00 79.05
REMARK 500 ASN B 280 71.26 -118.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 209 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-11023L RELATED DB: TARGETDB
DBREF 3KSM A 39 313 UNP Q2S7D2 Q2S7D2_HAHCH 39 313
DBREF 3KSM B 39 313 UNP Q2S7D2 Q2S7D2_HAHCH 39 313
SEQADV 3KSM GLU A 314 UNP Q2S7D2 EXPRESSION TAG
SEQADV 3KSM GLU B 314 UNP Q2S7D2 EXPRESSION TAG
SEQRES 1 A 276 PRO LYS LEU LEU LEU VAL LEU LYS GLY ASP SER ASN ALA
SEQRES 2 A 276 TYR TRP ARG GLN VAL TYR LEU GLY ALA GLN LYS ALA ALA
SEQRES 3 A 276 ASP GLU ALA GLY VAL THR LEU LEU HIS ARG SER THR LYS
SEQRES 4 A 276 ASP ASP GLY ASP ILE ALA GLY GLN ILE GLN ILE LEU SER
SEQRES 5 A 276 TYR HIS LEU SER GLN ALA PRO PRO ASP ALA LEU ILE LEU
SEQRES 6 A 276 ALA PRO ASN SER ALA GLU ASP LEU THR PRO SER VAL ALA
SEQRES 7 A 276 GLN TYR ARG ALA ARG ASN ILE PRO VAL LEU VAL VAL ASP
SEQRES 8 A 276 SER ASP LEU ALA GLY ASP ALA HIS GLN GLY LEU VAL ALA
SEQRES 9 A 276 THR ASP ASN TYR ALA ALA GLY GLN LEU ALA ALA ARG ALA
SEQRES 10 A 276 LEU LEU ALA THR LEU ASP LEU SER LYS GLU ARG ASN ILE
SEQRES 11 A 276 ALA LEU LEU ARG LEU ARG ALA GLY ASN ALA SER THR ASP
SEQRES 12 A 276 GLN ARG GLU GLN GLY PHE LEU ASP VAL LEU ARG LYS HIS
SEQRES 13 A 276 ASP LYS ILE ARG ILE ILE ALA ALA PRO TYR ALA GLY ASP
SEQRES 14 A 276 ASP ARG GLY ALA ALA ARG SER GLU MSE LEU ARG LEU LEU
SEQRES 15 A 276 LYS GLU THR PRO THR ILE ASP GLY LEU PHE THR PRO ASN
SEQRES 16 A 276 GLU SER THR THR ILE GLY ALA LEU VAL ALA ILE ARG GLN
SEQRES 17 A 276 SER GLY MSE SER LYS GLN PHE GLY PHE ILE GLY PHE ASP
SEQRES 18 A 276 GLN THR GLU GLU LEU GLU ALA ALA MSE TYR ALA GLY GLU
SEQRES 19 A 276 ILE SER ASN LEU VAL VAL GLN ASN PRO GLU TYR MSE GLY
SEQRES 20 A 276 TYR LEU ALA VAL GLN ARG ALA LEU ASP LEU VAL ARG GLY
SEQRES 21 A 276 LYS PRO ILE PRO ALA PHE THR ASP THR GLY VAL ARG LEU
SEQRES 22 A 276 LEU GLN GLU
SEQRES 1 B 276 PRO LYS LEU LEU LEU VAL LEU LYS GLY ASP SER ASN ALA
SEQRES 2 B 276 TYR TRP ARG GLN VAL TYR LEU GLY ALA GLN LYS ALA ALA
SEQRES 3 B 276 ASP GLU ALA GLY VAL THR LEU LEU HIS ARG SER THR LYS
SEQRES 4 B 276 ASP ASP GLY ASP ILE ALA GLY GLN ILE GLN ILE LEU SER
SEQRES 5 B 276 TYR HIS LEU SER GLN ALA PRO PRO ASP ALA LEU ILE LEU
SEQRES 6 B 276 ALA PRO ASN SER ALA GLU ASP LEU THR PRO SER VAL ALA
SEQRES 7 B 276 GLN TYR ARG ALA ARG ASN ILE PRO VAL LEU VAL VAL ASP
SEQRES 8 B 276 SER ASP LEU ALA GLY ASP ALA HIS GLN GLY LEU VAL ALA
SEQRES 9 B 276 THR ASP ASN TYR ALA ALA GLY GLN LEU ALA ALA ARG ALA
SEQRES 10 B 276 LEU LEU ALA THR LEU ASP LEU SER LYS GLU ARG ASN ILE
SEQRES 11 B 276 ALA LEU LEU ARG LEU ARG ALA GLY ASN ALA SER THR ASP
SEQRES 12 B 276 GLN ARG GLU GLN GLY PHE LEU ASP VAL LEU ARG LYS HIS
SEQRES 13 B 276 ASP LYS ILE ARG ILE ILE ALA ALA PRO TYR ALA GLY ASP
SEQRES 14 B 276 ASP ARG GLY ALA ALA ARG SER GLU MSE LEU ARG LEU LEU
SEQRES 15 B 276 LYS GLU THR PRO THR ILE ASP GLY LEU PHE THR PRO ASN
SEQRES 16 B 276 GLU SER THR THR ILE GLY ALA LEU VAL ALA ILE ARG GLN
SEQRES 17 B 276 SER GLY MSE SER LYS GLN PHE GLY PHE ILE GLY PHE ASP
SEQRES 18 B 276 GLN THR GLU GLU LEU GLU ALA ALA MSE TYR ALA GLY GLU
SEQRES 19 B 276 ILE SER ASN LEU VAL VAL GLN ASN PRO GLU TYR MSE GLY
SEQRES 20 B 276 TYR LEU ALA VAL GLN ARG ALA LEU ASP LEU VAL ARG GLY
SEQRES 21 B 276 LYS PRO ILE PRO ALA PHE THR ASP THR GLY VAL ARG LEU
SEQRES 22 B 276 LEU GLN GLU
MODRES 3KSM MSE A 216 MET SELENOMETHIONINE
MODRES 3KSM MSE A 249 MET SELENOMETHIONINE
MODRES 3KSM MSE A 268 MET SELENOMETHIONINE
MODRES 3KSM MSE A 284 MET SELENOMETHIONINE
MODRES 3KSM MSE B 216 MET SELENOMETHIONINE
MODRES 3KSM MSE B 249 MET SELENOMETHIONINE
MODRES 3KSM MSE B 268 MET SELENOMETHIONINE
MODRES 3KSM MSE B 284 MET SELENOMETHIONINE
HET MSE A 216 8
HET MSE A 249 8
HET MSE A 268 8
HET MSE A 284 8
HET MSE B 216 8
HET MSE B 249 8
HET MSE B 268 8
HET MSE B 284 8
HET BDR A 1 10
HET BDR B 1 10
HETNAM MSE SELENOMETHIONINE
HETNAM BDR BETA-D-RIBOFURANOSE
HETSYN BDR BETA-D-RIBOSE; D-RIBOSE; RIBOSE; BETA-D-RIBOFURANOSYL
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 3 BDR 2(C5 H10 O5)
FORMUL 5 HOH *349(H2 O)
HELIX 1 1 ALA A 51 GLY A 68 1 18
HELIX 2 2 ASP A 81 ALA A 96 1 16
HELIX 3 3 LEU A 111 ARG A 121 1 11
HELIX 4 4 ASP A 144 LEU A 160 1 17
HELIX 5 5 ASN A 177 ARG A 192 1 16
HELIX 6 6 ASP A 208 THR A 223 1 16
HELIX 7 7 ASN A 233 SER A 247 1 15
HELIX 8 8 THR A 261 ALA A 270 1 10
HELIX 9 9 ASN A 280 ARG A 297 1 18
HELIX 10 10 ALA B 51 GLY B 68 1 18
HELIX 11 11 ASP B 81 GLN B 95 1 15
HELIX 12 12 LEU B 111 ARG B 121 1 11
HELIX 13 13 ASP B 144 LEU B 160 1 17
HELIX 14 14 ASN B 177 ARG B 192 1 16
HELIX 15 15 ASP B 208 THR B 223 1 16
HELIX 16 16 ASN B 233 SER B 247 1 15
HELIX 17 17 THR B 261 ALA B 270 1 10
HELIX 18 18 ASN B 280 GLY B 298 1 19
SHEET 1 A 6 THR A 70 HIS A 73 0
SHEET 2 A 6 LYS A 40 VAL A 44 1 N LEU A 41 O LEU A 72
SHEET 3 A 6 ALA A 100 LEU A 103 1 O ILE A 102 N LEU A 42
SHEET 4 A 6 VAL A 125 VAL A 128 1 O LEU A 126 N LEU A 101
SHEET 5 A 6 GLY A 139 ALA A 142 1 O GLY A 139 N VAL A 127
SHEET 6 A 6 PHE A 304 ASP A 306 1 O THR A 305 N LEU A 140
SHEET 1 B 6 ILE A 197 ALA A 201 0
SHEET 2 B 6 ARG A 166 LEU A 170 1 N ILE A 168 O ARG A 198
SHEET 3 B 6 GLY A 228 PHE A 230 1 O GLY A 228 N ALA A 169
SHEET 4 B 6 GLY A 254 PHE A 258 1 O ILE A 256 N LEU A 229
SHEET 5 B 6 ASN A 275 VAL A 278 1 O ASN A 275 N GLY A 257
SHEET 6 B 6 ARG A 310 LEU A 311 -1 O ARG A 310 N VAL A 278
SHEET 1 C 6 LEU B 71 HIS B 73 0
SHEET 2 C 6 LEU B 41 VAL B 44 1 N LEU B 41 O LEU B 72
SHEET 3 C 6 ALA B 100 LEU B 103 1 O ILE B 102 N LEU B 42
SHEET 4 C 6 VAL B 125 VAL B 128 1 O LEU B 126 N LEU B 101
SHEET 5 C 6 GLY B 139 ALA B 142 1 O GLY B 139 N VAL B 127
SHEET 6 C 6 PHE B 304 ASP B 306 1 O THR B 305 N LEU B 140
SHEET 1 D 6 ILE B 197 ALA B 201 0
SHEET 2 D 6 ARG B 166 LEU B 170 1 N ILE B 168 O ARG B 198
SHEET 3 D 6 GLY B 228 PHE B 230 1 O GLY B 228 N ALA B 169
SHEET 4 D 6 GLY B 254 PHE B 258 1 O ILE B 256 N LEU B 229
SHEET 5 D 6 ASN B 275 VAL B 278 1 O VAL B 277 N GLY B 257
SHEET 6 D 6 ARG B 310 LEU B 311 -1 O ARG B 310 N VAL B 278
LINK C MSE A 216 N LEU A 217 1555 1555 1.33
LINK C MSE A 249 N SER A 250 1555 1555 1.33
LINK C MSE A 268 N TYR A 269 1555 1555 1.33
LINK C MSE A 284 N GLY A 285 1555 1555 1.34
LINK C MSE B 216 N LEU B 217 1555 1555 1.34
LINK C MSE B 249 N SER B 250 1555 1555 1.33
LINK C MSE B 268 N TYR B 269 1555 1555 1.33
LINK C MSE B 284 N GLY B 285 1555 1555 1.34
CRYST1 37.439 47.712 79.723 103.49 90.49 91.06 P 1 2
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 0.026710 0.000493 0.000353 0.00000
SCALE2 0.000000 0.020963 0.005035 0.00000
SCALE3 0.000000 0.000000 0.012901 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
