HEADER HYDROLASE 16-DEC-05 2DBY
TITLE CRYSTAL STRUCTURE OF THE GTP-BINDING PROTEIN YCHF IN COMPLEXED WITH
TITLE 2 GDP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GTP-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GTP-BINDING PROTEIN YCHF;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET11B
KEYWDS GTP-BINDING PROTEIN, GDP, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KUKIMOTO-NIINO,K.MURAYAMA,M.SHIROUZU,S.KURAMITSU,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 13-JUL-11 2DBY 1 VERSN
REVDAT 2 24-FEB-09 2DBY 1 VERSN
REVDAT 1 16-JUN-06 2DBY 0
JRNL AUTH M.KUKIMOTO-NIINO,K.MURAYAMA,M.SHIROUZU,S.KURAMITSU,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL CRYSTAL STRUCTURE OF THE GTP-BINDING PROTEIN YCHF IN
JRNL TITL 2 COMPLEXED WITH GDP
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.76 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 1.76
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1530045.990
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 37703
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) : 0.191
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3772
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.86
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4973
REMARK 3 BIN R VALUE (WORKING SET) : 0.2200
REMARK 3 BIN FREE R VALUE : 0.2600
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 539
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2763
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 359
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.08000
REMARK 3 B22 (A**2) : -0.14000
REMARK 3 B33 (A**2) : -3.94000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.08
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) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.13
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.60
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.95
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 : 0.38
REMARK 3 BSOL : 47.92
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 : LIGAND.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : LIGAND.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DBY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-DEC-05.
REMARK 100 THE RCSB ID CODE IS RCSB025232.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794, 0.9789, 0.9640
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU JUPITER
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37754
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.760
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.664
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.9059
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.28900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.253
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 (%): 46.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.7M SODIUM FORMATE, 0.1M SODIUM
REMARK 280 ACETATE, PH 5.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 30.19200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 66.58450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.19200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 66.58450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER.
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 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 ASP A 112
REMARK 465 PRO A 113
REMARK 465 ASP A 114
REMARK 465 VAL A 115
REMARK 465 VAL A 116
REMARK 465 HIS A 117
REMARK 465 VAL A 118
REMARK 465 MET A 119
REMARK 465 GLY A 120
REMARK 465 ARG A 121
REMARK 465 VAL A 122
REMARK 465 ASN A 367
REMARK 465 ALA A 368
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 827 DISTANCE = 5.68 ANGSTROMS
REMARK 525 HOH A 834 DISTANCE = 5.58 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TTK003001291.1 RELATED DB: TARGETDB
DBREF 2DBY A 1 368 UNP Q5SJ29 Q5SJ29_THET8 1 368
SEQADV 2DBY MSE A 1 UNP Q5SJ29 MET 1 MODIFIED RESIDUE
SEQADV 2DBY MSE A 317 UNP Q5SJ29 MET 317 MODIFIED RESIDUE
SEQRES 1 A 368 MSE LEU ALA VAL GLY ILE VAL GLY LEU PRO ASN VAL GLY
SEQRES 2 A 368 LYS SER THR LEU PHE ASN ALA LEU THR ARG ALA ASN ALA
SEQRES 3 A 368 LEU ALA ALA ASN TYR PRO PHE ALA THR ILE ASP LYS ASN
SEQRES 4 A 368 VAL GLY VAL VAL PRO LEU GLU ASP GLU ARG LEU TYR ALA
SEQRES 5 A 368 LEU GLN ARG THR PHE ALA LYS GLY GLU ARG VAL PRO PRO
SEQRES 6 A 368 VAL VAL PRO THR HIS VAL GLU PHE VAL ASP ILE ALA GLY
SEQRES 7 A 368 LEU VAL LYS GLY ALA HIS LYS GLY GLU GLY LEU GLY ASN
SEQRES 8 A 368 GLN PHE LEU ALA HIS ILE ARG GLU VAL ALA ALA ILE ALA
SEQRES 9 A 368 HIS VAL LEU ARG CYS PHE PRO ASP PRO ASP VAL VAL HIS
SEQRES 10 A 368 VAL MET GLY ARG VAL ASP PRO LEU GLU ASP ALA GLU VAL
SEQRES 11 A 368 VAL GLU THR GLU LEU LEU LEU ALA ASP LEU ALA THR LEU
SEQRES 12 A 368 GLU ARG ARG LEU GLU ARG LEU ARG LYS GLU ALA ARG ALA
SEQRES 13 A 368 ASP ARG GLU ARG LEU PRO LEU LEU GLU ALA ALA GLU GLY
SEQRES 14 A 368 LEU TYR VAL HIS LEU GLN GLU GLY LYS PRO ALA ARG THR
SEQRES 15 A 368 PHE PRO PRO SER GLU ALA VAL ALA ARG PHE LEU LYS GLU
SEQRES 16 A 368 THR PRO LEU LEU THR ALA LYS PRO VAL ILE TYR VAL ALA
SEQRES 17 A 368 ASN VAL ALA GLU GLU ASP LEU PRO ASP GLY ARG GLY ASN
SEQRES 18 A 368 PRO GLN VAL GLU ALA VAL ARG ARG LYS ALA LEU GLU GLU
SEQRES 19 A 368 GLY ALA GLU VAL VAL VAL VAL SER ALA ARG LEU GLU ALA
SEQRES 20 A 368 GLU LEU ALA GLU LEU SER GLY GLU GLU ALA ARG GLU LEU
SEQRES 21 A 368 LEU ALA ALA TYR GLY LEU GLN GLU SER GLY LEU GLN ARG
SEQRES 22 A 368 LEU ALA ARG ALA GLY TYR ARG ALA LEU ASP LEU LEU THR
SEQRES 23 A 368 PHE PHE THR ALA GLY GLU LYS GLU VAL ARG ALA TRP THR
SEQRES 24 A 368 VAL ARG ARG GLY THR LYS ALA PRO ARG ALA ALA GLY GLU
SEQRES 25 A 368 ILE HIS SER ASP MSE GLU ARG GLY PHE ILE ARG ALA GLU
SEQRES 26 A 368 VAL ILE PRO TRP ASP LYS LEU VAL GLU ALA GLY GLY TRP
SEQRES 27 A 368 ALA ARG ALA LYS GLU ARG GLY TRP VAL ARG LEU GLU GLY
SEQRES 28 A 368 LYS ASP TYR GLU VAL GLN ASP GLY ASP VAL ILE TYR VAL
SEQRES 29 A 368 LEU PHE ASN ALA
MODRES 2DBY MSE A 1 MET SELENOMETHIONINE
MODRES 2DBY MSE A 317 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 317 8
HET GDP A 501 28
HET FMT A 401 3
HET FMT A 402 3
HET FMT A 403 3
HETNAM MSE SELENOMETHIONINE
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM FMT FORMIC ACID
FORMUL 1 MSE 2(C5 H11 N O2 SE)
FORMUL 2 GDP C10 H15 N5 O11 P2
FORMUL 3 FMT 3(C H2 O2)
FORMUL 6 HOH *359(H2 O)
HELIX 1 1 GLY A 13 ALA A 26 1 14
HELIX 2 2 PRO A 32 ASP A 37 5 6
HELIX 3 3 ASP A 47 ALA A 58 1 12
HELIX 4 4 GLY A 90 GLU A 99 1 10
HELIX 5 5 ASP A 123 ASP A 157 1 35
HELIX 6 6 ARG A 160 GLU A 176 1 17
HELIX 7 7 PRO A 179 PHE A 183 5 5
HELIX 8 8 SER A 186 THR A 196 1 11
HELIX 9 9 LEU A 198 LYS A 202 5 5
HELIX 10 10 ALA A 211 LEU A 215 5 5
HELIX 11 11 ASN A 221 GLY A 235 1 15
HELIX 12 12 SER A 242 GLU A 251 1 10
HELIX 13 13 SER A 253 TYR A 264 1 12
HELIX 14 14 SER A 269 LEU A 282 1 14
HELIX 15 15 LYS A 305 HIS A 314 1 10
HELIX 16 16 SER A 315 ARG A 319 5 5
HELIX 17 17 TRP A 329 GLY A 336 1 8
HELIX 18 18 GLY A 337 ARG A 344 1 8
SHEET 1 A 6 VAL A 40 PRO A 44 0
SHEET 2 A 6 HIS A 70 ASP A 75 -1 O PHE A 73 N GLY A 41
SHEET 3 A 6 ALA A 3 VAL A 7 1 N ILE A 6 O VAL A 74
SHEET 4 A 6 ALA A 102 ARG A 108 1 O ALA A 102 N GLY A 5
SHEET 5 A 6 VAL A 204 ASN A 209 1 O VAL A 207 N HIS A 105
SHEET 6 A 6 GLU A 237 VAL A 241 1 O GLU A 237 N TYR A 206
SHEET 1 B 3 VAL A 66 VAL A 67 0
SHEET 2 B 3 VAL A 295 ARG A 301 1 O ALA A 297 N VAL A 67
SHEET 3 B 3 LEU A 284 ALA A 290 -1 N PHE A 287 O TRP A 298
SHEET 1 C 3 ARG A 348 GLU A 350 0
SHEET 2 C 3 ARG A 323 PRO A 328 -1 N ALA A 324 O GLU A 350
SHEET 3 C 3 ASP A 360 LEU A 365 -1 O TYR A 363 N GLU A 325
LINK C MSE A 1 N LEU A 2 1555 1555 1.33
LINK C ASP A 316 N MSE A 317 1555 1555 1.33
LINK C MSE A 317 N GLU A 318 1555 1555 1.33
CISPEP 1 LEU A 215 PRO A 216 0 0.57
SITE 1 AC1 16 ASN A 11 VAL A 12 GLY A 13 LYS A 14
SITE 2 AC1 16 SER A 15 THR A 16 GLN A 92 ARG A 108
SITE 3 AC1 16 PHE A 110 ASN A 209 VAL A 210 SER A 242
SITE 4 AC1 16 ALA A 243 ARG A 244 HOH A 826 HOH A 858
SITE 1 AC2 3 HIS A 105 ALA A 128 HOH A 566
SITE 1 AC3 3 ARG A 155 TYR A 363 VAL A 364
SITE 1 AC4 8 ALA A 28 ALA A 29 ASN A 30 PRO A 44
SITE 2 AC4 8 PRO A 68 THR A 69 HIS A 70 HOH A 554
CRYST1 60.384 133.169 46.432 90.00 90.00 90.00 P 21 21 2 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 0.016561 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007509 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021537 0.00000
HETATM 1 N MSE A 1 28.982 52.339 32.992 1.00 31.06 N
HETATM 2 CA MSE A 1 28.175 52.566 31.755 1.00 27.77 C
HETATM 3 C MSE A 1 26.696 52.705 32.110 1.00 28.39 C
HETATM 4 O MSE A 1 26.143 51.882 32.864 1.00 21.00 O
HETATM 5 CB MSE A 1 28.327 51.382 30.786 1.00 36.18 C
HETATM 6 CG MSE A 1 29.214 51.616 29.562 1.00 37.26 C
HETATM 7 SE MSE A 1 28.987 50.148 28.287 1.00 51.26 SE
HETATM 8 CE MSE A 1 29.636 48.720 29.437 1.00 38.97 C
(ATOM LINES ARE NOT SHOWN.)
END
