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Chemical substance (3) PDB-CCD (3) Gene (2) KEGG GENES (2) Protein sequence (3) UniProt (1) PDBSTR (2) Protein domain (6) InterPro (6) All databases (14)
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HEADER HYDROLASE 24-FEB-15 4YER
TITLE CRYSTAL STRUCTURE OF AN ABC TRANSPORTER ATP-BINDING PROTEIN (TM_1403)
TITLE 2 FROM THERMOTOGA MARITIMA MSB8 AT 2.35 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ABC TRANSPORTER ATP-BINDING PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ABC-TYPE MULTIDRUG TRANSPORT SYSTEM,ATPASE COMPONENT,
COMPND 5 ANTIBIOTIC ABC TRANSPORTER,ATP-BINDING PROTEIN,PUTATIVE;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 243274;
SOURCE 4 STRAIN: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
SOURCE 5 GENE: TM_1403, THEMA_07300, TMARI_1410;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: MH4TEVA
KEYWDS PF00005 FAMILY PROTEIN, P-LOOP CONTAINING NUCLEOSIDE TRIPHOSPHATE
KEYWDS 2 HYDROLASES FOLD, STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-BIOLOGY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 6 01-FEB-23 4YER 1 SEQADV
REVDAT 5 25-DEC-19 4YER 1 REMARK
REVDAT 4 24-JAN-18 4YER 1 JRNL
REVDAT 3 01-NOV-17 4YER 1 REMARK
REVDAT 2 20-SEP-17 4YER 1 SOURCE REMARK
REVDAT 1 11-MAR-15 4YER 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF AN ABC TRANSPORTER ATP-BINDING PROTEIN
JRNL TITL 2 (TM_1403) FROM THERMOTOGA MARITIMA MSB8 AT 2.35 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 29234
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) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1481
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 15
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.43
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.95
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2807
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2138
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2663
REMARK 3 BIN R VALUE (WORKING SET) : 0.2115
REMARK 3 BIN FREE R VALUE : 0.2557
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.13
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 144
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4310
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 60
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.33100
REMARK 3 B22 (A**2) : 5.36420
REMARK 3 B33 (A**2) : -7.69510
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) : 0.305
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.920
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 8648 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 15665 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2427 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 95 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1303 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 8648 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 606 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 9117 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 0.96
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.36
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.95
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|1-313 }
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7363 -19.1565 80.0341
REMARK 3 T TENSOR
REMARK 3 T11: -0.2296 T22: -0.2359
REMARK 3 T33: 0.0628 T12: -0.0150
REMARK 3 T13: -0.0474 T23: 0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 1.9818 L22: 1.6793
REMARK 3 L33: 1.9414 L12: -0.0670
REMARK 3 L13: 0.0071 L23: 0.3962
REMARK 3 S TENSOR
REMARK 3 S11: 0.0203 S12: 0.0559 S13: -0.1155
REMARK 3 S21: 0.0341 S22: 0.0163 S23: -0.1587
REMARK 3 S31: 0.2838 S32: -0.0083 S33: -0.0367
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|1-313 }
REMARK 3 ORIGIN FOR THE GROUP (A): -12.0484 -30.7797 80.9971
REMARK 3 T TENSOR
REMARK 3 T11: -0.2417 T22: -0.2205
REMARK 3 T33: 0.0814 T12: -0.0044
REMARK 3 T13: 0.0269 T23: -0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 1.8420 L22: 2.9097
REMARK 3 L33: 1.0675 L12: -0.4423
REMARK 3 L13: 0.2788 L23: -0.9456
REMARK 3 S TENSOR
REMARK 3 S11: 0.0340 S12: 0.0490 S13: 0.2773
REMARK 3 S21: -0.0199 S22: -0.0873 S23: -0.1461
REMARK 3 S31: -0.0883 S32: 0.0050 S33: 0.0533
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1. ZERO OCCUPANCY HYDROGENS WERE
REMARK 3 INCLUDED DURING REFINEMENT TO IMPROVE THE ANTI-BUMPING
REMARK 3 RESTRAINTS. 2. ATOM RECORDS CONTAIN SUM OF TLS AND RESIDUAL B
REMARK 3 FACTORS. 3. ANISOU RECORDS CONTAIN SUM OF TLS AND RESIDUAL U
REMARK 3 FACTORS. 4. A MET-INHIBITION PROTOCOL WAS USED FOR
REMARK 3 SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE
REMARK 3 OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO
REMARK 3 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 5. NCS RESTRAINTS WERE APPLIED DURING REFINEMENT
REMARK 3 USING LSSR (-AUTONCS) IN BUSTER. 6. LIGAND MOLECULES ADENOSINE-5'
REMARK 3 -DIPHOSPHATE (ADP) ARE MODELED IN EACH CHAIN BASED ON ELECTRON
REMARK 3 DENSITY AND HOMOLOGOUS STRUCTURES.
REMARK 4
REMARK 4 4YER COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000206742.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-FEB-07; 08-FEB-07
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 4.28; 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : SSRL; SSRL
REMARK 200 BEAMLINE : BL1-5; BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.999974;
REMARK 200 0.97926,0.91837,0.97894
REMARK 200 MONOCHROMATOR : 2-CRYSTAL, SI111; SINGLE CRYSTAL
REMARK 200 SI(111) BENT
REMARK 200 OPTICS : 2-CRYSTAL MONOCHROMATOR, SI111,
REMARK 200 1M LONG RH COATED BENT
REMARK 200 CYLINDRICAL MIRROR FOR
REMARK 200 HORIZONTAL AND VERTICAL
REMARK 200 FOCUSSING; FLAT MIRROR (VERTICAL
REMARK 200 FOCUSING); SINGLE CRYSTAL SI(111)
REMARK 200 BENT MONOCHROMATOR (HO RIZONTAL
REMARK 200 FOCUSING)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; MARMOSAIC 325 MM
REMARK 200 CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29295
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 29.725
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.41
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.80000
REMARK 200 R SYM FOR SHELL (I) : 0.80000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELX, SHARP, SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 54.0% POLYETHYLENE GLYCOL 200, 0.2M
REMARK 280 SODIUM CHLORIDE, 0.1M PHOSPHATE-CITRATE PH 4.28, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K. 0.2M SODIUM CHLORIDE, 55.0%
REMARK 280 POLYETHYLENE GLYCOL 200, 0.1M PHOSPHATE-CITRATE PH 4.2, VAPOR
REMARK 280 DIFFUSION, SITTING 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 30.65500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.10500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.59000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.10500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.65500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.59000
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: DIMER ACCORDING TO ANALYTICAL SIZE EXCLUSION
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
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 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 GLY A 0
REMARK 465 PHE A 236
REMARK 465 SER A 237
REMARK 465 GLU A 238
REMARK 465 ALA A 239
REMARK 465 VAL A 240
REMARK 465 GLU A 241
REMARK 465 CYS A 242
REMARK 465 LEU A 243
REMARK 465 GLU A 244
REMARK 465 GLY A 245
REMARK 465 SER A 266
REMARK 465 GLY A 267
REMARK 465 ARG A 268
REMARK 465 ALA A 269
REMARK 465 ILE A 270
REMARK 465 PRO A 271
REMARK 465 LYS A 272
REMARK 465 ILE A 273
REMARK 465 PHE A 274
REMARK 465 GLU A 275
REMARK 465 LEU A 276
REMARK 465 ALA A 277
REMARK 465 GLN A 278
REMARK 465 GLN A 279
REMARK 465 LYS A 280
REMARK 465 GLY A 281
REMARK 465 LEU A 282
REMARK 465 LYS A 283
REMARK 465 SER A 314
REMARK 465 PHE A 315
REMARK 465 LYS A 316
REMARK 465 THR A 317
REMARK 465 MSE A 318
REMARK 465 ALA A 319
REMARK 465 ARG A 320
REMARK 465 MSE A 321
REMARK 465 ARG A 322
REMARK 465 MSE A 323
REMARK 465 ARG A 324
REMARK 465 MSE A 325
REMARK 465 ARG A 326
REMARK 465 ARG A 327
REMARK 465 GLY B 0
REMARK 465 PHE B 236
REMARK 465 SER B 237
REMARK 465 GLU B 238
REMARK 465 ALA B 239
REMARK 465 VAL B 240
REMARK 465 GLU B 241
REMARK 465 CYS B 242
REMARK 465 LEU B 243
REMARK 465 GLU B 244
REMARK 465 GLY B 245
REMARK 465 ASP B 246
REMARK 465 PHE B 247
REMARK 465 ILE B 248
REMARK 465 GLU B 249
REMARK 465 SER B 250
REMARK 465 ASN B 262
REMARK 465 VAL B 263
REMARK 465 GLU B 264
REMARK 465 ASP B 265
REMARK 465 SER B 266
REMARK 465 GLY B 267
REMARK 465 ARG B 268
REMARK 465 ALA B 269
REMARK 465 ILE B 270
REMARK 465 PRO B 271
REMARK 465 LYS B 272
REMARK 465 ILE B 273
REMARK 465 PHE B 274
REMARK 465 GLU B 275
REMARK 465 LEU B 276
REMARK 465 ALA B 277
REMARK 465 GLN B 278
REMARK 465 GLN B 279
REMARK 465 LYS B 280
REMARK 465 GLY B 281
REMARK 465 LEU B 282
REMARK 465 SER B 314
REMARK 465 PHE B 315
REMARK 465 LYS B 316
REMARK 465 THR B 317
REMARK 465 MSE B 318
REMARK 465 ALA B 319
REMARK 465 ARG B 320
REMARK 465 MSE B 321
REMARK 465 ARG B 322
REMARK 465 MSE B 323
REMARK 465 ARG B 324
REMARK 465 MSE B 325
REMARK 465 ARG B 326
REMARK 465 ARG B 327
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 MSE A 1 CG SE CE
REMARK 470 LYS A 29 CG CD CE NZ
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 ARG A 73 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 77 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 103 CG CD CE NZ
REMARK 470 GLU A 110 CG CD OE1 OE2
REMARK 470 LYS A 111 CG CD CE NZ
REMARK 470 LEU A 112 CG CD1 CD2
REMARK 470 LYS A 113 CG CD CE NZ
REMARK 470 LYS A 114 CG CD CE NZ
REMARK 470 GLU A 121 CG CD OE1 OE2
REMARK 470 GLU A 127 CG CD OE1 OE2
REMARK 470 GLU A 153 CG CD OE1 OE2
REMARK 470 HIS A 169 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 225 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 229 CG CD CE NZ
REMARK 470 GLU A 230 CG CD OE1 OE2
REMARK 470 ARG A 235 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 252 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 253 CG CD CE NZ
REMARK 470 GLU A 285 CG CD OE1 OE2
REMARK 470 GLU A 286 CG CD OE1 OE2
REMARK 470 LYS A 291 CG CD CE NZ
REMARK 470 ARG A 307 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 309 CG CD OE1 OE2
REMARK 470 MSE B 1 CG SE CE
REMARK 470 LYS B 55 CG CD CE NZ
REMARK 470 ARG B 73 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 76 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 85 CG OD1 OD2
REMARK 470 ARG B 90 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 111 CG CD CE NZ
REMARK 470 LYS B 113 CG CD CE NZ
REMARK 470 LYS B 114 CG CD CE NZ
REMARK 470 GLU B 118 CG CD OE1 OE2
REMARK 470 LYS B 131 CG CD CE NZ
REMARK 470 LYS B 134 CG CD CE NZ
REMARK 470 HIS B 169 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 225 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 229 CG CD CE NZ
REMARK 470 GLU B 230 CG CD OE1 OE2
REMARK 470 ILE B 231 CG1 CG2 CD1
REMARK 470 ARG B 235 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 252 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 253 CG CD CE NZ
REMARK 470 GLU B 285 CG CD OE1 OE2
REMARK 470 GLU B 286 CG CD OE1 OE2
REMARK 470 LYS B 291 CG CD CE NZ
REMARK 470 ARG B 307 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 309 CG CD OE1 OE2
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 85 99.72 -58.73
REMARK 500 ASP A 130 54.17 -104.17
REMARK 500 THR A 135 30.98 -93.77
REMARK 500 ASP B 130 54.39 -103.04
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 ADP A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP B 400
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: JCSG-283264 RELATED DB: TARGETTRACK
DBREF 4YER A 1 327 UNP Q9X1C3 Q9X1C3_THEMA 1 327
DBREF 4YER B 1 327 UNP Q9X1C3 Q9X1C3_THEMA 1 327
SEQADV 4YER GLY A 0 UNP Q9X1C3 EXPRESSION TAG
SEQADV 4YER GLY B 0 UNP Q9X1C3 EXPRESSION TAG
SEQRES 1 A 328 GLY MSE GLU ASP ILE ILE VAL VAL GLU ASN LEU VAL LYS
SEQRES 2 A 328 LYS PHE GLY ASP PHE GLU ALA VAL LYS GLY VAL SER PHE
SEQRES 3 A 328 SER VAL LYS LYS GLY GLU ILE PHE ALA PHE LEU GLY PRO
SEQRES 4 A 328 ASN GLY ALA GLY LYS THR THR THR ILE HIS MSE LEU THR
SEQRES 5 A 328 THR LEU LEU LYS PRO THR SER GLY LYS ALA TRP VAL ALA
SEQRES 6 A 328 GLY HIS ASP VAL LEU LYS GLU PRO ARG GLU VAL ARG ARG
SEQRES 7 A 328 LYS ILE GLY ILE VAL PHE GLN ASP GLN SER LEU ASP ARG
SEQRES 8 A 328 GLU LEU THR ALA TYR GLU ASN MSE TYR ILE HIS GLY LYS
SEQRES 9 A 328 ILE TYR GLY TYR GLY GLY GLU LYS LEU LYS LYS ARG ILE
SEQRES 10 A 328 LEU GLU LEU LEU GLU PHE VAL GLU LEU LEU GLU PHE LYS
SEQRES 11 A 328 ASP LYS PRO VAL LYS THR PHE SER GLY GLY MSE ALA ARG
SEQRES 12 A 328 ARG LEU GLU ILE ALA ARG SER LEU ILE HIS GLU PRO GLU
SEQRES 13 A 328 VAL LEU PHE LEU ASP GLU PRO THR ILE GLY LEU ASP PRO
SEQRES 14 A 328 HIS THR ARG ALA HIS MSE TRP GLU TYR ILE SER LYS MSE
SEQRES 15 A 328 LYS LYS GLU HIS ASN MSE THR ILE PHE LEU THR THR HIS
SEQRES 16 A 328 TYR MSE ASP GLU ALA GLU GLN LEU ALA ASP ARG VAL ALA
SEQRES 17 A 328 ILE ILE ASP HIS GLY LYS ILE ILE ALA LEU GLY THR PRO
SEQRES 18 A 328 THR GLU LEU LYS ARG MSE VAL GLY LYS GLU ILE ILE TYR
SEQRES 19 A 328 VAL ARG PHE SER GLU ALA VAL GLU CYS LEU GLU GLY ASP
SEQRES 20 A 328 PHE ILE GLU SER CYS ARG LYS LEU PRO ASP GLY ARG LEU
SEQRES 21 A 328 GLU LEU ASN VAL GLU ASP SER GLY ARG ALA ILE PRO LYS
SEQRES 22 A 328 ILE PHE GLU LEU ALA GLN GLN LYS GLY LEU LYS ILE GLU
SEQRES 23 A 328 GLU ILE THR TYR HIS LYS PRO THR LEU ASN ASP VAL PHE
SEQRES 24 A 328 LEU HIS LEU THR GLY ARG GLU LEU ARG GLU GLU GLY PRO
SEQRES 25 A 328 GLU ASN SER PHE LYS THR MSE ALA ARG MSE ARG MSE ARG
SEQRES 26 A 328 MSE ARG ARG
SEQRES 1 B 328 GLY MSE GLU ASP ILE ILE VAL VAL GLU ASN LEU VAL LYS
SEQRES 2 B 328 LYS PHE GLY ASP PHE GLU ALA VAL LYS GLY VAL SER PHE
SEQRES 3 B 328 SER VAL LYS LYS GLY GLU ILE PHE ALA PHE LEU GLY PRO
SEQRES 4 B 328 ASN GLY ALA GLY LYS THR THR THR ILE HIS MSE LEU THR
SEQRES 5 B 328 THR LEU LEU LYS PRO THR SER GLY LYS ALA TRP VAL ALA
SEQRES 6 B 328 GLY HIS ASP VAL LEU LYS GLU PRO ARG GLU VAL ARG ARG
SEQRES 7 B 328 LYS ILE GLY ILE VAL PHE GLN ASP GLN SER LEU ASP ARG
SEQRES 8 B 328 GLU LEU THR ALA TYR GLU ASN MSE TYR ILE HIS GLY LYS
SEQRES 9 B 328 ILE TYR GLY TYR GLY GLY GLU LYS LEU LYS LYS ARG ILE
SEQRES 10 B 328 LEU GLU LEU LEU GLU PHE VAL GLU LEU LEU GLU PHE LYS
SEQRES 11 B 328 ASP LYS PRO VAL LYS THR PHE SER GLY GLY MSE ALA ARG
SEQRES 12 B 328 ARG LEU GLU ILE ALA ARG SER LEU ILE HIS GLU PRO GLU
SEQRES 13 B 328 VAL LEU PHE LEU ASP GLU PRO THR ILE GLY LEU ASP PRO
SEQRES 14 B 328 HIS THR ARG ALA HIS MSE TRP GLU TYR ILE SER LYS MSE
SEQRES 15 B 328 LYS LYS GLU HIS ASN MSE THR ILE PHE LEU THR THR HIS
SEQRES 16 B 328 TYR MSE ASP GLU ALA GLU GLN LEU ALA ASP ARG VAL ALA
SEQRES 17 B 328 ILE ILE ASP HIS GLY LYS ILE ILE ALA LEU GLY THR PRO
SEQRES 18 B 328 THR GLU LEU LYS ARG MSE VAL GLY LYS GLU ILE ILE TYR
SEQRES 19 B 328 VAL ARG PHE SER GLU ALA VAL GLU CYS LEU GLU GLY ASP
SEQRES 20 B 328 PHE ILE GLU SER CYS ARG LYS LEU PRO ASP GLY ARG LEU
SEQRES 21 B 328 GLU LEU ASN VAL GLU ASP SER GLY ARG ALA ILE PRO LYS
SEQRES 22 B 328 ILE PHE GLU LEU ALA GLN GLN LYS GLY LEU LYS ILE GLU
SEQRES 23 B 328 GLU ILE THR TYR HIS LYS PRO THR LEU ASN ASP VAL PHE
SEQRES 24 B 328 LEU HIS LEU THR GLY ARG GLU LEU ARG GLU GLU GLY PRO
SEQRES 25 B 328 GLU ASN SER PHE LYS THR MSE ALA ARG MSE ARG MSE ARG
SEQRES 26 B 328 MSE ARG ARG
MODRES 4YER MSE A 1 MET MODIFIED RESIDUE
MODRES 4YER MSE A 49 MET MODIFIED RESIDUE
MODRES 4YER MSE A 98 MET MODIFIED RESIDUE
MODRES 4YER MSE A 140 MET MODIFIED RESIDUE
MODRES 4YER MSE A 174 MET MODIFIED RESIDUE
MODRES 4YER MSE A 181 MET MODIFIED RESIDUE
MODRES 4YER MSE A 187 MET MODIFIED RESIDUE
MODRES 4YER MSE A 196 MET MODIFIED RESIDUE
MODRES 4YER MSE A 226 MET MODIFIED RESIDUE
MODRES 4YER MSE B 1 MET MODIFIED RESIDUE
MODRES 4YER MSE B 49 MET MODIFIED RESIDUE
MODRES 4YER MSE B 98 MET MODIFIED RESIDUE
MODRES 4YER MSE B 140 MET MODIFIED RESIDUE
MODRES 4YER MSE B 174 MET MODIFIED RESIDUE
MODRES 4YER MSE B 181 MET MODIFIED RESIDUE
MODRES 4YER MSE B 187 MET MODIFIED RESIDUE
MODRES 4YER MSE B 196 MET MODIFIED RESIDUE
MODRES 4YER MSE B 226 MET MODIFIED RESIDUE
HET MSE A 1 5
HET MSE A 49 8
HET MSE A 98 8
HET MSE A 140 8
HET MSE A 174 8
HET MSE A 181 8
HET MSE A 187 8
HET MSE A 196 8
HET MSE A 226 8
HET MSE B 1 5
HET MSE B 49 8
HET MSE B 98 8
HET MSE B 140 8
HET MSE B 174 8
HET MSE B 181 8
HET MSE B 187 8
HET MSE B 196 8
HET MSE B 226 8
HET ADP A 400 27
HET CL A 401 1
HET CL A 402 1
HET ADP B 400 27
HETNAM MSE SELENOMETHIONINE
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM CL CHLORIDE ION
FORMUL 1 MSE 18(C5 H11 N O2 SE)
FORMUL 3 ADP 2(C10 H15 N5 O10 P2)
FORMUL 4 CL 2(CL 1-)
FORMUL 7 HOH *60(H2 O)
HELIX 1 AA1 GLY A 42 THR A 51 1 10
HELIX 2 AA2 GLU A 71 LYS A 78 1 8
HELIX 3 AA3 THR A 93 TYR A 105 1 13
HELIX 4 AA4 GLY A 108 VAL A 123 1 16
HELIX 5 AA5 LEU A 125 LYS A 129 5 5
HELIX 6 AA6 PRO A 132 PHE A 136 5 5
HELIX 7 AA7 SER A 137 LEU A 150 1 14
HELIX 8 AA8 ASP A 167 ASN A 186 1 20
HELIX 9 AA9 TYR A 195 ALA A 203 1 9
HELIX 10 AB1 THR A 219 ARG A 225 1 7
HELIX 11 AB2 THR A 293 GLY A 303 1 11
HELIX 12 AB3 GLY B 42 THR B 51 1 10
HELIX 13 AB4 GLU B 71 LYS B 78 1 8
HELIX 14 AB5 THR B 93 TYR B 105 1 13
HELIX 15 AB6 GLY B 108 VAL B 123 1 16
HELIX 16 AB7 LEU B 125 LYS B 129 5 5
HELIX 17 AB8 PRO B 132 PHE B 136 5 5
HELIX 18 AB9 SER B 137 LEU B 150 1 14
HELIX 19 AC1 ASP B 167 ASN B 186 1 20
HELIX 20 AC2 TYR B 195 ALA B 203 1 9
HELIX 21 AC3 THR B 219 ARG B 225 1 7
HELIX 22 AC4 THR B 293 GLY B 303 1 11
SHEET 1 AA1 4 PHE A 17 LYS A 28 0
SHEET 2 AA1 4 ASP A 3 PHE A 14 -1 N PHE A 14 O PHE A 17
SHEET 3 AA1 4 SER A 58 VAL A 63 -1 O SER A 58 N VAL A 11
SHEET 4 AA1 4 HIS A 66 ASP A 67 -1 O HIS A 66 N VAL A 63
SHEET 1 AA2 6 ILE A 79 VAL A 82 0
SHEET 2 AA2 6 VAL A 156 ASP A 160 1 O PHE A 158 N GLY A 80
SHEET 3 AA2 6 THR A 188 THR A 193 1 O THR A 188 N LEU A 157
SHEET 4 AA2 6 ILE A 32 LEU A 36 1 N PHE A 33 O ILE A 189
SHEET 5 AA2 6 ARG A 205 ASP A 210 1 O ILE A 209 N LEU A 36
SHEET 6 AA2 6 LYS A 213 GLY A 218 -1 O GLY A 218 N VAL A 206
SHEET 1 AA3 8 ILE A 248 LYS A 253 0
SHEET 2 AA3 8 LEU A 259 VAL A 263 -1 O ASN A 262 N GLU A 249
SHEET 3 AA3 8 ILE A 231 ARG A 235 -1 N ILE A 232 O LEU A 261
SHEET 4 AA3 8 GLU A 286 HIS A 290 -1 O THR A 288 N TYR A 233
SHEET 5 AA3 8 ILE B 284 HIS B 290 -1 O TYR B 289 N ILE A 287
SHEET 6 AA3 8 ILE B 231 ARG B 235 -1 N ARG B 235 O GLU B 285
SHEET 7 AA3 8 LEU B 259 LEU B 261 -1 O LEU B 261 N ILE B 232
SHEET 8 AA3 8 ARG B 252 LYS B 253 -1 N ARG B 252 O GLU B 260
SHEET 1 AA4 4 PHE B 17 LYS B 28 0
SHEET 2 AA4 4 ASP B 3 PHE B 14 -1 N VAL B 7 O PHE B 25
SHEET 3 AA4 4 SER B 58 VAL B 63 -1 O SER B 58 N VAL B 11
SHEET 4 AA4 4 HIS B 66 ASP B 67 -1 O HIS B 66 N VAL B 63
SHEET 1 AA5 6 ILE B 79 VAL B 82 0
SHEET 2 AA5 6 VAL B 156 ASP B 160 1 O PHE B 158 N GLY B 80
SHEET 3 AA5 6 THR B 188 THR B 193 1 O THR B 188 N LEU B 157
SHEET 4 AA5 6 ILE B 32 LEU B 36 1 N PHE B 33 O ILE B 189
SHEET 5 AA5 6 ARG B 205 ASP B 210 1 O ILE B 209 N LEU B 36
SHEET 6 AA5 6 LYS B 213 GLY B 218 -1 O GLY B 218 N VAL B 206
LINK C MSE A 1 N GLU A 2 1555 1555 1.34
LINK C HIS A 48 N MSE A 49 1555 1555 1.35
LINK C MSE A 49 N LEU A 50 1555 1555 1.35
LINK C ASN A 97 N MSE A 98 1555 1555 1.35
LINK C MSE A 98 N TYR A 99 1555 1555 1.36
LINK C GLY A 139 N MSE A 140 1555 1555 1.34
LINK C MSE A 140 N ALA A 141 1555 1555 1.35
LINK C HIS A 173 N MSE A 174 1555 1555 1.35
LINK C MSE A 174 N TRP A 175 1555 1555 1.34
LINK C LYS A 180 N MSE A 181 1555 1555 1.33
LINK C MSE A 181 N LYS A 182 1555 1555 1.35
LINK C ASN A 186 N MSE A 187 1555 1555 1.32
LINK C MSE A 187 N THR A 188 1555 1555 1.33
LINK C TYR A 195 N MSE A 196 1555 1555 1.34
LINK C MSE A 196 N ASP A 197 1555 1555 1.34
LINK C ARG A 225 N MSE A 226 1555 1555 1.35
LINK C MSE A 226 N VAL A 227 1555 1555 1.35
LINK C MSE B 1 N GLU B 2 1555 1555 1.35
LINK C HIS B 48 N MSE B 49 1555 1555 1.36
LINK C MSE B 49 N LEU B 50 1555 1555 1.35
LINK C ASN B 97 N MSE B 98 1555 1555 1.33
LINK C MSE B 98 N TYR B 99 1555 1555 1.34
LINK C GLY B 139 N MSE B 140 1555 1555 1.34
LINK C MSE B 140 N ALA B 141 1555 1555 1.35
LINK C HIS B 173 N MSE B 174 1555 1555 1.34
LINK C MSE B 174 N TRP B 175 1555 1555 1.34
LINK C LYS B 180 N MSE B 181 1555 1555 1.35
LINK C MSE B 181 N LYS B 182 1555 1555 1.35
LINK C ASN B 186 N MSE B 187 1555 1555 1.32
LINK C MSE B 187 N THR B 188 1555 1555 1.35
LINK C TYR B 195 N MSE B 196 1555 1555 1.33
LINK C MSE B 196 N ASP B 197 1555 1555 1.36
LINK C ARG B 225 N MSE B 226 1555 1555 1.35
LINK C MSE B 226 N VAL B 227 1555 1555 1.35
SITE 1 AC1 14 PHE A 14 PHE A 17 ALA A 19 PRO A 38
SITE 2 AC1 14 ASN A 39 GLY A 40 ALA A 41 GLY A 42
SITE 3 AC1 14 LYS A 43 THR A 44 THR A 45 THR B 135
SITE 4 AC1 14 PHE B 136 SER B 137
SITE 1 AC2 3 ASP A 210 LYS A 213 LYS B 13
SITE 1 AC3 4 HIS A 194 GLU A 308 HIS B 194 GLU B 308
SITE 1 AC4 16 LYS A 134 THR A 135 PHE A 136 SER A 137
SITE 2 AC4 16 PHE B 14 PHE B 17 ALA B 19 PRO B 38
SITE 3 AC4 16 ASN B 39 GLY B 40 ALA B 41 GLY B 42
SITE 4 AC4 16 LYS B 43 THR B 44 THR B 45 HOH B 512
CRYST1 61.310 101.180 110.210 90.00 90.00 90.00 P 21 21 21 8
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 0.016311 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009883 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009074 0.00000
HETATM 1 N MSE A 1 32.520 -8.734 79.576 1.00 79.30 N
ANISOU 1 N MSE A 1 6770 9596 13762 -397 -173 -523 N
HETATM 2 CA MSE A 1 31.184 -9.251 79.872 1.00 77.56 C
ANISOU 2 CA MSE A 1 6781 9301 13388 -315 -240 -465 C
HETATM 3 C MSE A 1 30.167 -8.568 78.920 1.00 79.76 C
ANISOU 3 C MSE A 1 7213 9501 13591 -400 -107 -357 C
HETATM 4 O MSE A 1 29.488 -7.597 79.282 1.00 79.28 O
ANISOU 4 O MSE A 1 7242 9352 13528 -484 -128 -324 O
HETATM 5 CB MSE A 1 30.855 -9.020 81.362 1.00 79.66 C
ANISOU 5 CB MSE A 1 7096 9527 13644 -305 -424 -511 C
(ATOM LINES ARE NOT SHOWN.)
END