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PDB Full entry for 1ARO
HEADER COMPLEX (POLYMERASE/HYDROLASE) 08-AUG-97 1ARO
TITLE T7 RNA POLYMERASE COMPLEXED WITH T7 LYSOZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: T7 RNA POLYMERASE;
COMPND 3 CHAIN: P;
COMPND 4 EC: 2.7.7.6;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: C347S, C723S, C839S;
COMPND 7 BIOLOGICAL_UNIT: MONOMER;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: T7 LYSOZYME;
COMPND 10 CHAIN: L;
COMPND 11 SYNONYM: N-ACETYLMURAMOYL-L-ALANINE AMIDASE;
COMPND 12 EC: 3.5.1.28;
COMPND 13 ENGINEERED: YES;
COMPND 14 BIOLOGICAL_UNIT: MONOMER
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTERIOPHAGE T7;
SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 4 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: BACTERIOPHAGE T7;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS TRANSCRIPTION, DNA-DIRECTED RNA POLYMERASE, HYDROLASE,
KEYWDS 2 GLYCOSIDASE, COMPLEX (POLYMERASE/HYDROLASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR T.STEITZ,D.JERUZALMI
REVDAT 1 21-OCT-98 1ARO 0
JRNL AUTH D.JERUZALMI,T.A.STEITZ
JRNL TITL STRUCTURE OF T7 RNA POLYMERASE COMPLEXED TO THE
JRNL TITL 2 TRANSCRIPTIONAL INHIBITOR T7 LYSOZYME
JRNL REF EMBO J. V. 17 4101 1998
JRNL REFN ASTM EMJODG UK ISSN 0261-4189 0897
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.8 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,
REMARK 3 GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,
REMARK 3 PANNU,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) : 2.8
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 38310
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.262
REMARK 3 FREE R VALUE : 0.309
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 7599
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ARO COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : OCT-1993 TO MAY-1996
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1, F1, F2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.908
REMARK 200 MONOCHROMATOR : SILICON
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE CCD
REMARK 200 DETECTOR MANUFACTURER : FUJI HOME-BUILT
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38310
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.8
REMARK 200 RESOLUTION RANGE LOW (A) : 100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 200 DATA REDUNDANCY : 2.2
REMARK 200 R MERGE (I) : 0.096
REMARK 200 R SYM (I) : 0.096
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.37
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.8
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.9
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2
REMARK 200 R MERGE FOR SHELL (I) : 0.44
REMARK 200 R SYM FOR SHELL (I) : 0.44
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: CCP4, RAVE, X-PLOR, CNS, DEMON-ANGEL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 1/2+X,1/2+Y,Z
REMARK 290 4555 1/2-X,1/2+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 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 136.68671
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.80572
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 136.68671
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 47.80572
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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 LYS P 164 O
REMARK 470 ASN P 233 O
REMARK 470 TRP P 344 O
REMARK 470 GLY P 589 O
REMARK 470 ASP P 879 O
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS P 8 ASN P 9 0 137.12
REMARK 500 GLN P 58 LEU P 59 0 148.06
REMARK 500 LEU P 497 GLU P 498 0 226.60
REMARK 500 ASN P 499 THR P 500 0 218.60
REMARK 500 VAL P 559 ASN P 560 0 112.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 850
REMARK 850 CORRECTION BEFORE RELEASE
REMARK 850 ORIGINAL DEPOSITION REVISED PRIOR TO RELEASE
REMARK 850 DATE REVISED: 24-APR-1998 TRACKING NUMBER: T12554
REMARK 850 DATE REVISED: 22-JUL-1998 TRACKING NUMBER: T15001
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1ARO P SWS P00573 1 - 7 NOT IN ATOMS LIST
REMARK 999 1ARO P SWS P00573 880 - 883 NOT IN ATOMS LIST
REMARK 999 1ARO L GB 431190 1 - 2 NOT IN ATOMS LIST
REMARK 999
REMARK 999 REFERENCE: THE SEQUENCE PRESENTED BELOW IS THAT OF MOFFATT,
REMARK 999 DUNN AND STUDIER, J. MOL. BIOL. V. 173, 265-269 (1984).
DBREF 1ARO P 8 59 SWS P00573 RPOL_BPT7 8 59
DBREF 1ARO P 73 164 SWS P00573 RPOL_BPT7 73 164
DBREF 1ARO P 182 233 SWS P00573 RPOL_BPT7 182 233
DBREF 1ARO P 241 344 SWS P00573 RPOL_BPT7 241 344
DBREF 1ARO P 384 589 SWS P00573 RPOL_BPT7 384 589
DBREF 1ARO P 612 879 SWS P00573 RPOL_BPT7 612 879
DBREF 1ARO L 1002 1150 GB 431190 V01146 3 151
SEQADV 1ARO P SWS P00573 LYS 60 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ALA 61 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 GLY 62 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 GLU 63 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 VAL 64 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ALA 65 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ASP 66 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ASN 67 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ALA 68 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ALA 69 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ALA 70 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 LYS 71 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 PRO 72 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ASN 165 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 VAL 166 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 GLU 167 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 GLU 168 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 GLN 169 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 LEU 170 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ASN 171 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 LYS 172 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ARG 173 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 VAL 174 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 GLY 175 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 HIS 176 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 VAL 177 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 TYR 178 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 LYS 179 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 LYS 180 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ALA 181 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ALA 234 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 GLY 235 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 VAL 236 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 VAL 237 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 GLY 238 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 GLN 239 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ASP 240 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 LYS 345 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 HIS 346 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 CYS 347 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 PRO 348 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 VAL 349 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 GLU 350 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ASP 351 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ILE 352 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 PRO 353 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ALA 354 GAP IN PDB ENTRY
SEQADV 1ARO VAL P 384 SWS P00573 ILE 355 CONFLICT
SEQADV 1ARO TYR P 385 SWS P00573 GLU 356 CONFLICT
SEQADV 1ARO LYS P 387 SWS P00573 GLU 358 CONFLICT
SEQADV 1ARO ASP P 388 SWS P00573 GLU 359 CORRECTION
SEQADV 1ARO P SWS P00573 LEU 360 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 PRO 361 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 MET 362 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 LYS 363 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 PRO 364 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 GLU 365 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ASP 366 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ILE 367 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ASP 368 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 MET 369 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ASN 370 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 PRO 371 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 GLU 372 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ALA 373 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 LEU 374 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 THR 375 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ALA 376 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 TRP 377 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 LYS 378 GAP IN PDB ENTRY
SEQADV 1ARO LYS P 389 SWS P00573 ARG 379 CORRECTION
SEQADV 1ARO P SWS P00573 ALA 381 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ALA 382 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ALA 383 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 VAL 384 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 TYR 385 GAP IN PDB ENTRY
SEQADV 1ARO SER P 393 SWS P00573 THR 388 CORRECTION
SEQADV 1ARO ARG P 395 SWS P00573 LEU 390 CORRECTION
SEQADV 1ARO ILE P 396 SWS P00573 ALA 391 CORRECTION
SEQADV 1ARO P SWS P00573 VAL 395 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 SER 396 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ALA 397 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 LEU 398 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 SER 399 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 SER 400 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 CYS 401 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 LEU 402 GAP IN PDB ENTRY
SEQADV 1ARO ASN P 406 SWS P00573 SER 403 CORRECTION
SEQADV 1ARO TYR P 418 SWS P00573 ILE 406 CORRECTION
SEQADV 1ARO ASN P 419 SWS P00573 SER 407 CORRECTION
SEQADV 1ARO MET P 420 SWS P00573 LEU 408 CORRECTION
SEQADV 1ARO P SWS P00573 LEU 409 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 THR 410 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ILE 411 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ARG 412 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 PRO 413 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 SER 414 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 GLY 415 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 SER 416 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 LEU 417 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 THR 418 GAP IN PDB ENTRY
SEQADV 1ARO ASP P 421 SWS P00573 THR 419 CORRECTION
SEQADV 1ARO ARG P 423 SWS P00573 THR 421 CORRECTION
SEQADV 1ARO P SWS P00573 ALA 423 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 VAL 424 GAP IN PDB ENTRY
SEQADV 1ARO LEU P 443 SWS P00573 ARG 443 CORRECTION
SEQADV 1ARO PRO P 474 SWS P00573 SER 474 CORRECTION
SEQADV 1ARO P SWS P00573 THR 590 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ASP 591 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ASN 592 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 GLU 593 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 VAL 594 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 VAL 595 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 THR 596 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 VAL 597 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 THR 598 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ASP 599 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 GLU 600 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ASN 601 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 THR 602 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 GLY 603 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 GLU 604 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 ILE 605 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 SER 606 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 GLU 607 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 LYS 608 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 VAL 609 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 LYS 610 GAP IN PDB ENTRY
SEQADV 1ARO P SWS P00573 LEU 611 GAP IN PDB ENTRY
SEQADV 1ARO SER P 723 SWS P00573 CYS 723 ENGINEERED
SEQADV 1ARO SER P 839 SWS P00573 CYS 839 ENGINEERED
SEQRES 1 P 883 MET ASN THR ILE ASN ILE ALA LYS ASN ASP PHE SER ASP
SEQRES 2 P 883 ILE GLU LEU ALA ALA ILE PRO PHE ASN THR LEU ALA ASP
SEQRES 3 P 883 HIS TYR GLY GLU ARG LEU ALA ARG GLU GLN LEU ALA LEU
SEQRES 4 P 883 GLU HIS GLU SER TYR GLU MET GLY GLU ALA ARG PHE ARG
SEQRES 5 P 883 LYS MET PHE GLU ARG GLN LEU LYS ALA GLY GLU VAL ALA
SEQRES 6 P 883 ASP ASN ALA ALA ALA LYS PRO LEU ILE THR THR LEU LEU
SEQRES 7 P 883 PRO LYS MET ILE ALA ARG ILE ASN ASP TRP PHE GLU GLU
SEQRES 8 P 883 VAL LYS ALA LYS ARG GLY LYS ARG PRO THR ALA PHE GLN
SEQRES 9 P 883 PHE LEU GLN GLU ILE LYS PRO GLU ALA VAL ALA TYR ILE
SEQRES 10 P 883 THR ILE LYS THR THR LEU ALA CYS LEU THR SER ALA ASP
SEQRES 11 P 883 ASN THR THR VAL GLN ALA VAL ALA SER ALA ILE GLY ARG
SEQRES 12 P 883 ALA ILE GLU ASP GLU ALA ARG PHE GLY ARG ILE ARG ASP
SEQRES 13 P 883 LEU GLU ALA LYS HIS PHE LYS LYS ASN VAL GLU GLU GLN
SEQRES 14 P 883 LEU ASN LYS ARG VAL GLY HIS VAL TYR LYS LYS ALA PHE
SEQRES 15 P 883 MET GLN VAL VAL GLU ALA ASP MET LEU SER LYS GLY LEU
SEQRES 16 P 883 LEU GLY GLY GLU ALA TRP SER SER TRP HIS LYS GLU ASP
SEQRES 17 P 883 SER ILE HIS VAL GLY VAL ARG CYS ILE GLU MET LEU ILE
SEQRES 18 P 883 GLU SER THR GLY MET VAL SER LEU HIS ARG GLN ASN ALA
SEQRES 19 P 883 GLY VAL VAL GLY GLN ASP SER GLU THR ILE GLU LEU ALA
SEQRES 20 P 883 PRO GLU TYR ALA GLU ALA ILE ALA THR ARG ALA GLY ALA
SEQRES 21 P 883 LEU ALA GLY ILE SER PRO MET PHE GLN PRO CYS VAL VAL
SEQRES 22 P 883 PRO PRO LYS PRO TRP THR GLY ILE THR GLY GLY GLY TYR
SEQRES 23 P 883 TRP ALA ASN GLY ARG ARG PRO LEU ALA LEU VAL ARG THR
SEQRES 24 P 883 HIS SER LYS LYS ALA LEU MET ARG TYR GLU ASP VAL TYR
SEQRES 25 P 883 MET PRO GLU VAL TYR LYS ALA ILE ASN ILE ALA GLN ASN
SEQRES 26 P 883 THR ALA TRP LYS ILE ASN LYS LYS VAL LEU ALA VAL ALA
SEQRES 27 P 883 ASN VAL ILE THR LYS TRP LYS HIS SER PRO VAL GLU ASP
SEQRES 28 P 883 ILE PRO ALA ILE GLU ARG GLU GLU LEU PRO MET LYS PRO
SEQRES 29 P 883 GLU ASP ILE ASP MET ASN PRO GLU ALA LEU THR ALA TRP
SEQRES 30 P 883 LYS ARG ALA ALA ALA ALA VAL TYR ARG LYS ASP LYS ALA
SEQRES 31 P 883 ARG LYS SER ARG ARG ILE SER LEU GLU PHE MET LEU GLU
SEQRES 32 P 883 GLN ALA ASN LYS PHE ALA ASN HIS LYS ALA ILE TRP PHE
SEQRES 33 P 883 PRO TYR ASN MET ASP TRP ARG GLY ARG VAL TYR ALA VAL
SEQRES 34 P 883 SER MET PHE ASN PRO GLN GLY ASN ASP MET THR LYS GLY
SEQRES 35 P 883 LEU LEU THR LEU ALA LYS GLY LYS PRO ILE GLY LYS GLU
SEQRES 36 P 883 GLY TYR TYR TRP LEU LYS ILE HIS GLY ALA ASN CYS ALA
SEQRES 37 P 883 GLY VAL ASP LYS VAL PRO PHE PRO GLU ARG ILE LYS PHE
SEQRES 38 P 883 ILE GLU GLU ASN HIS GLU ASN ILE MET ALA CYS ALA LYS
SEQRES 39 P 883 SER PRO LEU GLU ASN THR TRP TRP ALA GLU GLN ASP SER
SEQRES 40 P 883 PRO PHE CYS PHE LEU ALA PHE CYS PHE GLU TYR ALA GLY
SEQRES 41 P 883 VAL GLN HIS HIS GLY LEU SER TYR ASN CYS SER LEU PRO
SEQRES 42 P 883 LEU ALA PHE ASP GLY SER CYS SER GLY ILE GLN HIS PHE
SEQRES 43 P 883 SER ALA MET LEU ARG ASP GLU VAL GLY GLY ARG ALA VAL
SEQRES 44 P 883 ASN LEU LEU PRO SER GLU THR VAL GLN ASP ILE TYR GLY
SEQRES 45 P 883 ILE VAL ALA LYS LYS VAL ASN GLU ILE LEU GLN ALA ASP
SEQRES 46 P 883 ALA ILE ASN GLY THR ASP ASN GLU VAL VAL THR VAL THR
SEQRES 47 P 883 ASP GLU ASN THR GLY GLU ILE SER GLU LYS VAL LYS LEU
SEQRES 48 P 883 GLY THR LYS ALA LEU ALA GLY GLN TRP LEU ALA TYR GLY
SEQRES 49 P 883 VAL THR ARG SER VAL THR LYS ARG SER VAL MET THR LEU
SEQRES 50 P 883 ALA TYR GLY SER LYS GLU PHE GLY PHE ARG GLN GLN VAL
SEQRES 51 P 883 LEU GLU ASP THR ILE GLN PRO ALA ILE ASP SER GLY LYS
SEQRES 52 P 883 GLY LEU MET PHE THR GLN PRO ASN GLN ALA ALA GLY TYR
SEQRES 53 P 883 MET ALA LYS LEU ILE TRP GLU SER VAL SER VAL THR VAL
SEQRES 54 P 883 VAL ALA ALA VAL GLU ALA MET ASN TRP LEU LYS SER ALA
SEQRES 55 P 883 ALA LYS LEU LEU ALA ALA GLU VAL LYS ASP LYS LYS THR
SEQRES 56 P 883 GLY GLU ILE LEU ARG LYS ARG SER ALA VAL HIS TRP VAL
SEQRES 57 P 883 THR PRO ASP GLY PHE PRO VAL TRP GLN GLU TYR LYS LYS
SEQRES 58 P 883 PRO ILE GLN THR ARG LEU ASN LEU MET PHE LEU GLY GLN
SEQRES 59 P 883 PHE ARG LEU GLN PRO THR ILE ASN THR ASN LYS ASP SER
SEQRES 60 P 883 GLU ILE ASP ALA HIS LYS GLN GLU SER GLY ILE ALA PRO
SEQRES 61 P 883 ASN PHE VAL HIS SER GLN ASP GLY SER HIS LEU ARG LYS
SEQRES 62 P 883 THR VAL VAL TRP ALA HIS GLU LYS TYR GLY ILE GLU SER
SEQRES 63 P 883 PHE ALA LEU ILE HIS ASP SER PHE GLY THR ILE PRO ALA
SEQRES 64 P 883 ASP ALA ALA ASN LEU PHE LYS ALA VAL ARG GLU THR MET
SEQRES 65 P 883 VAL ASP THR TYR GLU SER SER ASP VAL LEU ALA ASP PHE
SEQRES 66 P 883 TYR ASP GLN PHE ALA ASP GLN LEU HIS GLU SER GLN LEU
SEQRES 67 P 883 ASP LYS MET PRO ALA LEU PRO ALA LYS GLY ASN LEU ASN
SEQRES 68 P 883 LEU ARG ASP ILE LEU GLU SER ASP PHE ALA PHE ALA
SEQRES 1 L 151 MET ALA ARG VAL GLN PHE LYS GLN ARG GLU SER THR ASP
SEQRES 2 L 151 ALA ILE PHE VAL HIS CYS SER ALA THR LYS PRO SER GLN
SEQRES 3 L 151 ASN VAL GLY VAL ARG GLU ILE ARG GLN TRP HIS LYS GLU
SEQRES 4 L 151 GLN GLY TRP LEU ASP VAL GLY TYR HIS PHE ILE ILE LYS
SEQRES 5 L 151 ARG ASP GLY THR VAL GLU ALA GLY ARG ASP GLU MET ALA
SEQRES 6 L 151 VAL GLY SER HIS ALA LYS GLY TYR ASN HIS ASN SER ILE
SEQRES 7 L 151 GLY VAL CYS LEU VAL GLY GLY ILE ASP ASP LYS GLY LYS
SEQRES 8 L 151 PHE ASP ALA ASN PHE THR PRO ALA GLN MET GLN SER LEU
SEQRES 9 L 151 ARG SER LEU LEU VAL THR LEU LEU ALA LYS TYR GLU GLY
SEQRES 10 L 151 ALA VAL LEU ARG ALA HIS HIS GLU VAL ALA PRO LYS ALA
SEQRES 11 L 151 CYS PRO SER PHE ASP LEU LYS ARG TRP TRP GLU LYS ASN
SEQRES 12 L 151 GLU LEU VAL THR SER ASP ARG GLY
HET HG 903 1
HET HG 904 1
HET HG 905 1
HET HG 906 1
HET HG 907 1
HET HG 908 1
HET HG 909 1
HETNAM HG MERCURY (II) ION
FORMUL 3 HG 7(HG1 2+)
HELIX 1 1 GLU P 15 HIS P 27 1 13
HELIX 2 2 GLU P 30 SER P 43 1 14
HELIX 3 3 GLU P 48 GLN P 58 1 11
HELIX 4 4 LEU P 77 VAL P 92 1 16
HELIX 5 5 PHE P 103 GLN P 107 1 5
HELIX 6 6 PRO P 111 THR P 127 1 17
HELIX 7 7 VAL P 134 LYS P 160 1 27
HELIX 8 8 LYS P 206 SER P 223 1 18
HELIX 9 9 PRO P 248 THR P 256 1 9
HELIX 10 10 ALA P 260 GLY P 263 5 4
HELIX 11 11 LYS P 302 ARG P 307 1 6
HELIX 12 12 PRO P 314 ASN P 325 1 12
HELIX 13 13 LYS P 332 ILE P 341 1 10
HELIX 14 14 LYS P 389 LYS P 407 1 19
HELIX 15 15 ASP P 438 LEU P 443 1 6
HELIX 16 16 GLY P 453 ALA P 468 1 16
HELIX 17 17 PHE P 475 ALA P 491 1 17
HELIX 18 18 TRP P 502 GLU P 504 5 3
HELIX 19 19 PHE P 509 HIS P 524 1 16
HELIX 20 20 HIS P 545 LEU P 550 1 6
HELIX 21 21 GLU P 553 VAL P 559 1 7
HELIX 22 22 ILE P 570 ALA P 586 1 17
HELIX 23 23 GLN P 619 TYR P 623 1 5
HELIX 24 24 GLU P 643 ASP P 653 5 11
HELIX 25 25 GLN P 656 ILE P 659 1 4
HELIX 26 26 ASN P 671 THR P 688 1 18
HELIX 27 27 VAL P 690 LEU P 706 1 17
HELIX 28 28 ALA P 771 SER P 776 1 6
HELIX 29 29 ILE P 778 TRP P 797 1 20
HELIX 30 30 PRO P 818 GLU P 837 1 20
HELIX 31 31 VAL P 841 GLN P 852 1 12
HELIX 32 32 ARG P 873 ILE P 875 5 3
HELIX 33 33 VAL L 1029 GLU L 1038 1 10
HELIX 34 34 ASN L 1073 ASN L 1075 5 3
HELIX 35 35 PRO L 1097 LYS L 1113 1 17
HELIX 36 36 HIS L 1122 GLU L 1124 5 3
HELIX 37 37 LEU L 1135 GLU L 1140 1 6
SHEET 1 A 2 TRP P 328 ILE P 330 0
SHEET 2 A 2 LEU P 444 LEU P 446 -1 N THR P 445 O LYS P 329
SHEET 1 B 2 TYR P 418 MET P 420 0
SHEET 2 B 2 VAL P 426 ALA P 428 -1 N TYR P 427 O ASN P 419
SHEET 1 C 2 VAL P 725 VAL P 728 0
SHEET 2 C 2 PRO P 734 GLN P 737 -1 N GLN P 737 O VAL P 725
SHEET 1 D 5 VAL L1118 ALA L1121 0
SHEET 2 D 5 ALA L1013 CYS L1018 1 N ILE L1014 O VAL L1118
SHEET 3 D 5 SER L1076 LEU L1081 1 N ILE L1077 O ALA L1013
SHEET 4 D 5 PHE L1048 ILE L1050 1 N PHE L1048 O CYS L1080
SHEET 5 D 5 VAL L1056 ALA L1058 -1 N GLU L1057 O ILE L1049
LINK HG HG 903 SG CYS L1018
LINK HG HG 903 SG CYS L1130
LINK HG HG 904 SG CYS P 125
LINK HG HG 905 SG CYS P 530
CISPEP 1 CYS L 1130 PRO L 1131 0 -0.45
CRYST1 273.385 95.612 63.582 90.00 101.40 90.00 C 1 2 1 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 0.003658 0.000000 0.000738 0.00000
SCALE2 0.000000 0.010459 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016044 0.00000
ATOM 1 N LYS P 8 25.806 77.382 9.089 1.00 96.41 N
ATOM 2 CA LYS P 8 26.017 76.714 7.789 1.00 96.02 C
ATOM 3 C LYS P 8 25.994 77.732 6.672 1.00 97.38 C
ATOM 4 O LYS P 8 25.039 77.847 5.815 1.00 99.32 O
ATOM 5 CB LYS P 8 24.983 75.621 7.557 1.00 94.11 C
ATOM 6 CG LYS P 8 25.282 74.406 8.429 1.00 90.10 C
ATOM 7 CD LYS P 8 24.324 73.315 8.048 0.00 88.62 C
ATOM 8 CE LYS P 8 24.487 72.108 8.949 0.00 86.88 C
ATOM 9 NZ LYS P 8 23.511 71.041 8.574 0.00 85.71 N
ATOM 10 N ASN P 9 26.223 78.899 6.589 1.00 96.85 N
ATOM 11 CA ASN P 9 26.810 80.032 5.908 1.00 95.48 C
ATOM 12 C ASN P 9 26.958 81.207 6.852 1.00 94.73 C
ATOM 13 O ASN P 9 27.935 81.972 6.500 1.00 95.73 O
ATOM 14 CB ASN P 9 26.009 80.359 4.653 1.00 96.45 C
ATOM 15 CG ASN P 9 26.006 79.193 3.682 1.00 96.28 C
ATOM 16 OD1 ASN P 9 27.030 78.533 3.486 0.00 96.15 O
ATOM 17 ND2 ASN P 9 24.858 78.930 3.071 0.00 96.15 N
ATOM 18 N ASP P 10 26.527 81.408 7.923 1.00 93.98 N
ATOM 19 CA ASP P 10 26.149 82.550 8.691 1.00 91.00 C
ATOM 20 C ASP P 10 26.959 83.772 8.309 1.00 89.06 C
ATOM 21 O ASP P 10 26.330 84.883 8.278 1.00 89.42 O
ATOM 22 CB ASP P 10 26.921 82.241 9.965 1.00 92.79 C
ATOM 23 CG ASP P 10 26.788 80.769 10.325 1.00 90.63 C
ATOM 24 OD1 ASP P 10 25.827 80.129 9.841 0.00 97.30 O
ATOM 25 OD2 ASP P 10 27.641 80.251 11.074 0.00 97.30 O
ATOM 26 N PHE P 11 28.256 83.733 8.018 1.00 85.92 N
ATOM 27 CA PHE P 11 29.055 84.925 7.772 1.00 83.50 C
ATOM 28 C PHE P 11 29.514 84.977 6.324 1.00 84.26 C
ATOM 29 O PHE P 11 29.550 84.055 5.539 1.00 87.54 O
ATOM 30 CB PHE P 11 30.410 84.518 8.351 1.00 79.03 C
ATOM 31 CG PHE P 11 30.348 84.101 9.788 1.00 76.13 C
ATOM 32 CD1 PHE P 11 30.502 85.035 10.795 0.00 78.01 C
ATOM 33 CD2 PHE P 11 30.135 82.776 10.128 0.00 78.01 C
ATOM 34 CE1 PHE P 11 30.444 84.655 12.123 0.00 74.10 C
ATOM 35 CE2 PHE P 11 30.076 82.389 11.453 0.00 74.10 C
ATOM 36 CZ PHE P 11 30.232 83.331 12.453 0.00 73.02 C
ATOM 37 N SER P 12 29.804 86.223 5.941 1.00 83.70 N
ATOM 38 CA SER P 12 30.171 86.569 4.556 1.00 83.23 C
ATOM 39 C SER P 12 31.383 85.875 4.011 1.00 84.67 C
ATOM 40 O SER P 12 32.140 85.272 4.770 1.00 88.26 O
ATOM 41 CB SER P 12 30.403 88.073 4.398 1.00 79.82 C
ATOM 42 OG SER P 12 31.528 88.488 5.157 0.00 84.77 O
ATOM 43 N ASP P 13 31.579 85.959 2.694 1.00 82.89 N
ATOM 44 CA ASP P 13 32.757 85.327 2.095 1.00 82.87 C
ATOM 45 C ASP P 13 34.047 86.065 2.464 1.00 83.90 C
ATOM 46 O ASP P 13 35.078 85.881 1.823 1.00 87.57 O
ATOM 47 CB ASP P 13 32.674 85.223 0.559 1.00 80.52 C
ATOM 48 CG ASP P 13 31.789 84.084 0.086 1.00 81.97 C
ATOM 49 OD1 ASP P 13 31.419 83.244 0.930 0.00 80.18 O
ATOM 50 OD2 ASP P 13 31.482 84.030 -1.126 0.00 80.18 O
ATOM 51 N ILE P 14 33.988 86.937 3.467 1.00 83.72 N
ATOM 52 CA ILE P 14 35.201 87.614 3.911 1.00 85.74 C
ATOM 53 C ILE P 14 35.475 87.241 5.360 1.00 87.93 C
ATOM 54 O ILE P 14 36.571 86.776 5.671 1.00 93.66 O
ATOM 55 CB ILE P 14 35.148 89.147 3.733 1.00 86.99 C
ATOM 56 CG1 ILE P 14 35.265 89.467 2.235 1.00 90.46 C
ATOM 57 CG2 ILE P 14 36.282 89.784 4.509 1.00 86.91 C
ATOM 58 CD1 ILE P 14 35.168 90.860 1.910 1.00 92.43 C
ATOM 59 N GLU P 15 34.501 87.421 6.252 1.00 88.02 N
ATOM 60 CA GLU P 15 34.754 87.028 7.642 1.00 89.25 C
ATOM 61 C GLU P 15 35.356 85.596 7.498 1.00 89.67 C
ATOM 62 O GLU P 15 36.415 85.265 8.072 1.00 90.97 O
ATOM 63 CB GLU P 15 33.457 87.088 8.502 1.00 87.91 C
ATOM 64 CG GLU P 15 32.858 88.509 8.600 1.00 92.51 C
ATOM 65 CD GLU P 15 31.751 88.598 9.631 1.00 93.30 C
ATOM 66 OE1 GLU P 15 31.176 87.543 10.015 1.00 92.32 O
ATOM 67 OE2 GLU P 15 31.400 89.727 10.046 1.00 91.74 O
....
ATOM 7306 C GLY L1150 -5.466 69.185 15.574 1.00101.33 C
ATOM 7307 O GLY L1150 -5.455 68.082 16.160 1.00100.09 O
ATOM 7308 OXT GLY L1150 -4.433 69.835 15.328 1.00102.38 O
TER 7309 GLY L1150
HETATM 7310 HG HG 903 0.546 58.674 10.452 1.00113.10 HG
HETATM 7311 HG HG 904 43.856 58.181 -8.808 1.00 87.64 HG
HETATM 7312 HG HG 905 69.467 59.800 21.875 1.00 83.11 HG
HETATM 7313 HG HG 906 62.354 49.250 13.389 1.00136.57 HG
HETATM 7314 HG HG 907 31.644 59.819 17.056 1.00159.44 HG
HETATM 7315 HG HG 908 56.936 59.010 0.827 1.00199.92 HG
HETATM 7316 HG HG 909 47.298 38.436 14.347 1.00199.92 HG
CONECT 864 863 7311
CONECT 3581 3580 7312
CONECT 6269 6268 7310
CONECT 7133 7132 7310
CONECT 7310 6269 7133
CONECT 7311 864
CONECT 7312 3581
MASTER 227 0 7 37 11 0 0 6 7314 2 7 80
END