HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 19-OCT-01 1K7J
TITLE STRUCTURAL GENOMICS, PROTEIN TF1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN YCIO;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PROTEIN TF1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: MC1061;
SOURCE 5 GENE: YCIO;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS STRUCTURAL GENOMICS, X-RAY CRYSTALLOGRAPHY, YCIO, PUTATIVE
KEYWDS 2 TRANSLATION FACTOR, PSI, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 3 MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, UNKNOWN
KEYWDS 4 FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR R.ZHANG,I.DEMENTIEVA,J.THORN,M.DONNELLY,A.JOACHIMIAK,
AUTHOR 2 MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 3 24-FEB-09 1K7J 1 VERSN
REVDAT 2 18-JAN-05 1K7J 1 AUTHOR KEYWDS REMARK
REVDAT 1 14-AUG-02 1K7J 0
JRNL AUTH R.ZHANG,I.DEMENTIEVA,J.THORN,M.DONNELLY,
JRNL AUTH 2 A.JOACHIMIAK
JRNL TITL STRUCTURAL GENOMICS, PROTEIN TF1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 409500.450
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 81.7
REMARK 3 NUMBER OF REFLECTIONS : 77132
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 SET) : 0.195
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 3724
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 50.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7457
REMARK 3 BIN R VALUE (WORKING SET) : 0.1870
REMARK 3 BIN FREE R VALUE : 0.1890
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 409
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.009
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1628
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 235
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.97000
REMARK 3 B22 (A**2) : 1.97000
REMARK 3 B33 (A**2) : -3.94000
REMARK 3 B12 (A**2) : 1.17000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.15
REMARK 3 ESD FROM SIGMAA (A) : 0.00
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.16
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.02
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.82
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 45.44
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: USED MLHL:MAXIMUM LIKELIHOOD TARGET
REMARK 3 USING AMPLITUDES IN CNS
REMARK 4
REMARK 4 1K7J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-01.
REMARK 100 THE RCSB ID CODE IS RCSB014658.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-AUG-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
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) : 0.9795, 0.9798, 0.94656
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC-2
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DTCOLLECT
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49419
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 12.570
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.0300
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 (%) : 95.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.28
REMARK 200 R MERGE FOR SHELL (I) : 0.29300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.630
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% AMMONIUM SULFATE, 0.1M NA
REMARK 280 CITRATE, PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
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,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 45.10033
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 90.20067
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 90.20067
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 45.10033
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: 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 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 60 -179.33 -66.17
REMARK 500 ASN A 92 45.18 -140.05
REMARK 500 ASN A 96 -8.26 64.98
REMARK 500 ASP A 190 29.74 48.65
REMARK 500
REMARK 500 REMARK: NULL
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 207
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC115 RELATED DB: TARGETDB
DBREF 1K7J A 1 206 UNP P45847 YCIO_ECOLI 1 206
SEQADV 1K7J MSE A 1 UNP P45847 MET 1 MODIFIED RESIDUE
SEQADV 1K7J MSE A 50 UNP P45847 MET 50 MODIFIED RESIDUE
SEQADV 1K7J MSE A 68 UNP P45847 MET 68 MODIFIED RESIDUE
SEQADV 1K7J MSE A 89 UNP P45847 MET 89 MODIFIED RESIDUE
SEQADV 1K7J MSE A 121 UNP P45847 MET 121 MODIFIED RESIDUE
SEQADV 1K7J MSE A 140 UNP P45847 MET 140 MODIFIED RESIDUE
SEQADV 1K7J MSE A 146 UNP P45847 MET 146 MODIFIED RESIDUE
SEQRES 1 A 206 MSE SER GLN PHE PHE TYR ILE HIS PRO ASP ASN PRO GLN
SEQRES 2 A 206 GLN ARG LEU ILE ASN GLN ALA VAL GLU ILE VAL ARG LYS
SEQRES 3 A 206 GLY GLY VAL ILE VAL TYR PRO THR ASP SER GLY TYR ALA
SEQRES 4 A 206 LEU GLY CYS LYS ILE GLU ASP LYS ASN ALA MSE GLU ARG
SEQRES 5 A 206 ILE CYS ARG ILE ARG GLN LEU PRO ASP GLY HIS ASN PHE
SEQRES 6 A 206 THR LEU MSE CYS ARG ASP LEU SER GLU LEU SER THR TYR
SEQRES 7 A 206 SER PHE VAL ASP ASN VAL ALA PHE ARG LEU MSE LYS ASN
SEQRES 8 A 206 ASN THR PRO GLY ASN TYR THR PHE ILE LEU LYS GLY THR
SEQRES 9 A 206 LYS GLU VAL PRO ARG ARG LEU LEU GLN GLU LYS ARG LYS
SEQRES 10 A 206 THR ILE GLY MSE ARG VAL PRO SER ASN PRO ILE ALA GLN
SEQRES 11 A 206 ALA LEU LEU GLU ALA LEU GLY GLU PRO MSE LEU SER THR
SEQRES 12 A 206 SER LEU MSE LEU PRO GLY SER GLU PHE THR GLU SER ASP
SEQRES 13 A 206 PRO GLU GLU ILE LYS ASP ARG LEU GLU LYS GLN VAL ASP
SEQRES 14 A 206 LEU ILE ILE HIS GLY GLY TYR LEU GLY GLN LYS PRO THR
SEQRES 15 A 206 THR VAL ILE ASP LEU THR ASP ASP THR PRO VAL VAL VAL
SEQRES 16 A 206 ARG GLU GLY VAL GLY ASP VAL LYS PRO PHE LEU
MODRES 1K7J MSE A 1 MET SELENOMETHIONINE
MODRES 1K7J MSE A 50 MET SELENOMETHIONINE
MODRES 1K7J MSE A 68 MET SELENOMETHIONINE
MODRES 1K7J MSE A 89 MET SELENOMETHIONINE
MODRES 1K7J MSE A 121 MET SELENOMETHIONINE
MODRES 1K7J MSE A 140 MET SELENOMETHIONINE
MODRES 1K7J MSE A 146 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 50 8
HET MSE A 68 8
HET MSE A 89 8
HET MSE A 121 8
HET MSE A 140 8
HET MSE A 146 8
HET SO4 A 207 5
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
FORMUL 1 MSE 7(C5 H11 N O2 SE)
FORMUL 2 SO4 O4 S 2-
FORMUL 3 HOH *235(H2 O)
HELIX 1 1 GLN A 13 LYS A 26 1 14
HELIX 2 2 ASP A 46 GLN A 58 1 13
HELIX 3 3 ASP A 71 SER A 79 1 9
HELIX 4 4 ASP A 82 ASN A 91 1 10
HELIX 5 5 PRO A 108 LEU A 112 5 5
HELIX 6 6 ASN A 126 GLY A 137 1 12
HELIX 7 7 ASP A 156 GLU A 165 1 10
HELIX 8 8 THR A 188 THR A 191 5 4
HELIX 9 9 VAL A 202 LEU A 206 5 5
SHEET 1 A10 GLN A 3 TYR A 6 0
SHEET 2 A10 LEU A 170 HIS A 173 1 O HIS A 173 N PHE A 5
SHEET 3 A10 ILE A 30 THR A 34 1 N VAL A 31 O ILE A 172
SHEET 4 A10 GLY A 37 LYS A 43 -1 O GLY A 41 N ILE A 30
SHEET 5 A10 MSE A 140 SER A 144 -1 O THR A 143 N LEU A 40
SHEET 6 A10 THR A 66 MSE A 68 -1 N THR A 66 O SER A 142
SHEET 7 A10 THR A 118 ARG A 122 1 O GLY A 120 N LEU A 67
SHEET 8 A10 TYR A 97 LYS A 102 -1 N PHE A 99 O MSE A 121
SHEET 9 A10 THR A 183 ASP A 186 1 O ILE A 185 N ILE A 100
SHEET 10 A10 VAL A 193 ARG A 196 -1 O VAL A 193 N ASP A 186
LINK C MSE A 1 N SER A 2 1555 1555 1.33
LINK C ALA A 49 N MSE A 50 1555 1555 1.33
LINK C MSE A 50 N GLU A 51 1555 1555 1.33
LINK C LEU A 67 N MSE A 68 1555 1555 1.33
LINK C MSE A 68 N CYS A 69 1555 1555 1.33
LINK C LEU A 88 N MSE A 89 1555 1555 1.33
LINK C MSE A 89 N LYS A 90 1555 1555 1.33
LINK C GLY A 120 N MSE A 121 1555 1555 1.33
LINK C MSE A 121 N ARG A 122 1555 1555 1.33
LINK C PRO A 139 N MSE A 140 1555 1555 1.32
LINK C MSE A 140 N LEU A 141 1555 1555 1.33
LINK C LEU A 145 N MSE A 146 1555 1555 1.33
LINK C MSE A 146 N LEU A 147 1555 1555 1.33
CISPEP 1 THR A 93 PRO A 94 0 -0.16
SITE 1 AC1 8 ARG A 57 HIS A 63 THR A 66 THR A 143
SITE 2 AC1 8 SER A 144 ARG A 196 HOH A 302 HOH A 317
CRYST1 56.260 56.260 135.301 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 0.017775 0.010262 0.000000 0.00000
SCALE2 0.000000 0.020524 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007391 0.00000
HETATM 1 N MSE A 1 16.452 24.520 19.847 1.00 20.43 N
HETATM 2 CA MSE A 1 17.645 25.184 19.247 1.00 20.20 C
HETATM 3 C MSE A 1 18.737 24.149 18.984 1.00 17.90 C
HETATM 4 O MSE A 1 18.920 23.212 19.761 1.00 17.34 O
HETATM 5 CB MSE A 1 18.181 26.263 20.193 1.00 24.14 C
HETATM 6 CG MSE A 1 18.826 27.450 19.482 1.00 28.98 C
HETATM 7 SE MSE A 1 17.520 28.781 18.927 1.00 38.43 SE
HETATM 8 CE MSE A 1 16.429 27.702 17.768 1.00 33.99 C
(ATOM LINES ARE NOT SHOWN.)
END
