HEADER TRANSFERASE 21-OCT-08 2ZUL
TITLE CRYSTAL STRUCTURE OF THERMUS THERMOPHILUS 16S RRNA METHYLTRANSFERASE
TITLE 2 RSMC (TTHA0533) IN COMPLEX WITH COFACTOR S-ADENOSYL-L-METHIONINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 16S RRNA METHYLTRANSFERASE RSMC;
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_STRAIN: B834 DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-11A
KEYWDS METHYLTRANSFERASE, 16S RRNA METHYLTRANSFERASE, S-ADENOSYL-L-
KEYWDS 2 METHIONINE, TRANSFERASE, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 3 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS 4 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI
EXPDTA X-RAY DIFFRACTION
AUTHOR H.WANG,M.KAWAZOE,A.TATSUGUCHI,C.NAOE,C.TAKEMOTO,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 13-MAR-24 2ZUL 1 REMARK
REVDAT 2 13-JUL-11 2ZUL 1 VERSN
REVDAT 1 27-OCT-09 2ZUL 0
JRNL AUTH H.WANG,M.KAWAZOE,A.TATSUGUCHI,C.NAOE,C.TAKEMOTO,S.YOKOYAMA
JRNL TITL CRYSTAL STRUCTURE OF THERMUS THERMOPHILUS 16S RRNA
JRNL TITL 2 METHYLTRANSFERASE RSMC (TTHA0533) IN COMPLEX WITH COFACTOR
JRNL TITL 3 S-ADENOSYL-L-METHIONINE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 68872.800
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 34577
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) : 0.183
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3442
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4591
REMARK 3 BIN R VALUE (WORKING SET) : 0.2030
REMARK 3 BIN FREE R VALUE : 0.2470
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 555
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2850
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 296
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.15000
REMARK 3 B22 (A**2) : 1.07000
REMARK 3 B33 (A**2) : -1.22000
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) : 0.14
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.780
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) : 3.060 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.500 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 5.010 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.700 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 41.65
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 : SAM_XPLOR_PARAM.TXT
REMARK 3 PARAMETER FILE 5 : 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 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ZUL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-OCT-08.
REMARK 100 THE DEPOSITION ID IS D_1000028444.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-08; 20-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY; PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A; BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000; 0.9790
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210; ADSC QUANTUM
REMARK 200 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35690
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 (%) : 99.1
REMARK 200 DATA REDUNDANCY : 7.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 7.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.41300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
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 (%): 47.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, SODIUM THIOCYANATE, HEPES, PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 25.42600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.81600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.03600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.81600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.42600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.03600
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 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 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 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 MET A 1
REMARK 465 SER A 2
REMARK 465 ARG A 375
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 ASN A 53 64.78 -163.55
REMARK 500 VAL A 289 -123.13 56.34
REMARK 500 ALA A 363 -134.17 -141.29
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 SAM A 376
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TTK003001444.1 RELATED DB: TARGETDB
DBREF 2ZUL A 1 375 UNP Q5SKW0 Q5SKW0_THET8 1 375
SEQRES 1 A 375 MET SER LEU THR ARG GLU ALA TYR HIS ARG LEU THR PRO
SEQRES 2 A 375 LEU PRO HIS PRO GLY GLY ARG LEU PHE ILE LYS PRO GLY
SEQRES 3 A 375 ALA ARG GLY TYR ARG ASP PRO VAL HIS ASP LEU LEU GLN
SEQRES 4 A 375 LYS THR VAL GLU PRO PHE GLY GLU ARG ALA LEU ASP LEU
SEQRES 5 A 375 ASN PRO GLY VAL GLY TRP GLY SER LEU PRO LEU GLU GLY
SEQRES 6 A 375 ARG MET ALA VAL GLU ARG LEU GLU THR SER ARG ALA ALA
SEQRES 7 A 375 PHE ARG CYS LEU THR ALA SER GLY LEU GLN ALA ARG LEU
SEQRES 8 A 375 ALA LEU PRO TRP GLU ALA ALA ALA GLY ALA TYR ASP LEU
SEQRES 9 A 375 VAL VAL LEU ALA LEU PRO ALA GLY ARG GLY THR ALA TYR
SEQRES 10 A 375 VAL GLN ALA SER LEU VAL ALA ALA ALA ARG ALA LEU ARG
SEQRES 11 A 375 MET GLY GLY ARG LEU TYR LEU ALA GLY ASP LYS ASN LYS
SEQRES 12 A 375 GLY PHE GLU ARG TYR PHE LYS GLU ALA ARG ALA LEU LEU
SEQRES 13 A 375 GLY TYR GLY VAL VAL VAL ARG ARG GLU GLY PRO TYR ARG
SEQRES 14 A 375 VAL ALA LEU LEU GLU LYS GLU LYS GLU ALA PRO PRO LEU
SEQRES 15 A 375 PRO SER LEU TRP ARG ALA PHE SER ALA ARG ILE LEU GLY
SEQRES 16 A 375 ALA GLU TYR THR PHE HIS HIS LEU PRO GLY VAL PHE SER
SEQRES 17 A 375 ALA GLY LYS VAL ASP PRO ALA SER LEU LEU LEU LEU GLU
SEQRES 18 A 375 ALA LEU GLN GLU ARG LEU GLY PRO GLU GLY VAL ARG GLY
SEQRES 19 A 375 ARG GLN VAL LEU ASP LEU GLY ALA GLY TYR GLY ALA LEU
SEQRES 20 A 375 THR LEU PRO LEU ALA ARG MET GLY ALA GLU VAL VAL GLY
SEQRES 21 A 375 VAL GLU ASP ASP LEU ALA SER VAL LEU SER LEU GLN LYS
SEQRES 22 A 375 GLY LEU GLU ALA ASN ALA LEU LYS ALA GLN ALA LEU HIS
SEQRES 23 A 375 SER ASP VAL ASP GLU ALA LEU THR GLU GLU ALA ARG PHE
SEQRES 24 A 375 ASP ILE ILE VAL THR ASN PRO PRO PHE HIS VAL GLY GLY
SEQRES 25 A 375 ALA VAL ILE LEU ASP VAL ALA GLN ALA PHE VAL ASN VAL
SEQRES 26 A 375 ALA ALA ALA ARG LEU ARG PRO GLY GLY VAL PHE PHE LEU
SEQRES 27 A 375 VAL SER ASN PRO PHE LEU LYS TYR GLU PRO LEU LEU GLU
SEQRES 28 A 375 GLU LYS PHE GLY ALA PHE GLN THR LEU LYS VAL ALA GLU
SEQRES 29 A 375 TYR LYS VAL LEU PHE ALA GLU LYS ARG GLY ARG
HET SAM A 376 27
HETNAM SAM S-ADENOSYLMETHIONINE
FORMUL 2 SAM C15 H22 N6 O5 S
FORMUL 3 HOH *296(H2 O)
HELIX 1 1 THR A 4 ARG A 10 1 7
HELIX 2 2 ASP A 32 VAL A 42 1 11
HELIX 3 3 SER A 60 GLU A 64 5 5
HELIX 4 4 SER A 75 SER A 85 1 11
HELIX 5 5 LEU A 93 ALA A 97 5 5
HELIX 6 6 PRO A 110 ARG A 113 5 4
HELIX 7 7 GLY A 114 ALA A 128 1 15
HELIX 8 8 GLY A 144 GLY A 157 1 14
HELIX 9 9 ASP A 213 GLY A 228 1 16
HELIX 10 10 LEU A 247 MET A 254 1 8
HELIX 11 11 ASP A 264 ASN A 278 1 15
HELIX 12 12 LEU A 316 ARG A 329 1 14
HELIX 13 13 LYS A 345 GLY A 355 1 11
SHEET 1 A 2 THR A 12 HIS A 16 0
SHEET 2 A 2 GLY A 19 ILE A 23 -1 O ILE A 23 N THR A 12
SHEET 1 B 7 ARG A 90 LEU A 91 0
SHEET 2 B 7 ALA A 68 GLU A 73 1 N ARG A 71 O ARG A 90
SHEET 3 B 7 ARG A 48 ASP A 51 1 N ALA A 49 O ALA A 68
SHEET 4 B 7 TYR A 102 ALA A 108 1 O VAL A 106 N LEU A 50
SHEET 5 B 7 LEU A 129 ASP A 140 1 O TYR A 136 N VAL A 105
SHEET 6 B 7 TYR A 168 GLU A 174 -1 O ALA A 171 N LEU A 137
SHEET 7 B 7 GLY A 159 GLU A 165 -1 N VAL A 162 O VAL A 170
SHEET 1 C 2 ARG A 187 ILE A 193 0
SHEET 2 C 2 ALA A 196 HIS A 202 -1 O ALA A 196 N ILE A 193
SHEET 1 D 7 GLN A 283 HIS A 286 0
SHEET 2 D 7 GLU A 257 GLU A 262 1 N GLY A 260 O GLN A 283
SHEET 3 D 7 GLN A 236 LEU A 240 1 N VAL A 237 O VAL A 259
SHEET 4 D 7 PHE A 299 THR A 304 1 O VAL A 303 N LEU A 238
SHEET 5 D 7 LEU A 330 SER A 340 1 O ARG A 331 N PHE A 299
SHEET 6 D 7 LYS A 366 GLU A 371 -1 O LEU A 368 N LEU A 338
SHEET 7 D 7 GLN A 358 VAL A 362 -1 N GLN A 358 O PHE A 369
SITE 1 AC1 23 TYR A 8 PHE A 207 SER A 216 GLY A 241
SITE 2 AC1 23 ALA A 242 GLY A 243 ALA A 246 GLU A 262
SITE 3 AC1 23 ASP A 263 SER A 287 ASP A 288 VAL A 289
SITE 4 AC1 23 ASN A 305 PRO A 306 VAL A 318 PHE A 322
SITE 5 AC1 23 HOH A 378 HOH A 380 HOH A 386 HOH A 394
SITE 6 AC1 23 HOH A 415 HOH A 425 HOH A 608
CRYST1 50.852 80.072 93.632 90.00 90.00 90.00 P 21 21 21 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 0.019665 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012489 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010680 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
