HEADER CONTRACTILE PROTEIN 03-JAN-03 1NKN
TITLE VISUALIZING AN UNSTABLE COILED COIL: THE CRYSTAL STRUCTURE OF AN N-
TITLE 2 TERMINAL SEGMENT OF THE SCALLOP MYOSIN ROD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S2N51-GCN4;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARGOPECTEN IRRADIANS, SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: , BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 31199,4932;
SOURCE 5 STRAIN: ,;
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 ALPHA HELIX, COILED COIL, CONTRACTILE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.LI,J.H.BROWN,L.RESHETNIKOVA,A.BLAZSEK,L.FARKAS,L.NYITRAY,C.COHEN
REVDAT 3 14-FEB-24 1NKN 1 REMARK
REVDAT 2 24-FEB-09 1NKN 1 VERSN
REVDAT 1 22-JUL-03 1NKN 0
JRNL AUTH Y.LI,J.H.BROWN,L.RESHETNIKOVA,A.BLAZSEK,L.FARKAS,L.NYITRAY,
JRNL AUTH 2 C.COHEN
JRNL TITL VISUALIZATION OF AN UNSTABLE COILED COIL FROM THE SCALLOP
JRNL TITL 2 MYOSIN ROD
JRNL REF NATURE V. 424 341 2003
JRNL REFN ISSN 0028-0836
JRNL PMID 12867988
JRNL DOI 10.1038/NATURE01801
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.4
REMARK 3 NUMBER OF REFLECTIONS : 12880
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) : 0.244
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 911
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3224
REMARK 3 BIN FREE R VALUE : 0.4153
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 95
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 : 2495
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 82
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.40
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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.012
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 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NKN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000017954.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.939
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13342
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.4
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.76
REMARK 200 R MERGE FOR SHELL (I) : 0.20300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.280
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CHLORIDE, SODIUM AZIDE, MOPS,
REMARK 280 PEG 200 MME, PH 6.9, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 289K
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 27.01700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.48750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.65150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.48750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.01700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.65150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 4050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 831
REMARK 465 SER A 832
REMARK 465 HIS A 833
REMARK 465 MET A 834
REMARK 465 PRO A 835
REMARK 465 LEU A 836
REMARK 465 LEU A 837
REMARK 465 SER A 838
REMARK 465 ILE A 839
REMARK 465 ALA A 840
REMARK 465 ARG A 841
REMARK 465 GLN A 842
REMARK 465 GLU A 843
REMARK 465 GLU A 844
REMARK 465 GLU A 845
REMARK 465 GLY B 831
REMARK 465 SER B 832
REMARK 465 HIS B 833
REMARK 465 MET B 834
REMARK 465 PRO B 835
REMARK 465 LEU B 836
REMARK 465 LEU B 837
REMARK 465 SER B 838
REMARK 465 ILE B 839
REMARK 465 ALA B 840
REMARK 465 ARG B 841
REMARK 465 GLN B 842
REMARK 465 ARG B 919
REMARK 465 GLY C 831
REMARK 465 SER C 832
REMARK 465 HIS C 833
REMARK 465 MET C 834
REMARK 465 PRO C 835
REMARK 465 LEU C 836
REMARK 465 LEU C 837
REMARK 465 SER C 838
REMARK 465 ILE C 839
REMARK 465 ALA C 840
REMARK 465 ARG C 841
REMARK 465 GLN C 842
REMARK 465 GLU C 843
REMARK 465 GLU C 844
REMARK 465 GLY D 831
REMARK 465 SER D 832
REMARK 465 HIS D 833
REMARK 465 MET D 834
REMARK 465 PRO D 835
REMARK 465 LEU D 836
REMARK 465 LEU D 837
REMARK 465 SER D 838
REMARK 465 ILE D 839
REMARK 465 ALA D 840
REMARK 465 ARG D 841
REMARK 465 GLN D 842
REMARK 465 ARG D 919
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 ARG A 919 CB CG CD NE CZ NH1 NH2
REMARK 470 ARG C 919 CB CG CD NE CZ NH1 NH2
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 GLU C 918 -48.99 -155.00
REMARK 500 GLU D 844 -8.74 -44.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE AN APPROPRIATE SEQUENCE DATABASE REFERENCE WAS NOT
REMARK 999 AVAILABLE AT THE TIME OF PROCESSING.
DBREF 1NKN A 888 919 UNP P03069 GCN4_YEAST 250 281
DBREF 1NKN B 888 919 UNP P03069 GCN4_YEAST 250 281
DBREF 1NKN C 888 919 UNP P03069 GCN4_YEAST 250 281
DBREF 1NKN D 888 919 UNP P03069 GCN4_YEAST 250 281
SEQRES 1 A 89 GLY SER HIS MET PRO LEU LEU SER ILE ALA ARG GLN GLU
SEQRES 2 A 89 GLU GLU MET LYS GLU GLN LEU LYS GLN MET ASP LYS MET
SEQRES 3 A 89 LYS GLU ASP LEU ALA LYS THR GLU ARG ILE LYS LYS GLU
SEQRES 4 A 89 LEU GLU GLU GLN ASN VAL THR LEU LEU GLU GLN LYS ASN
SEQRES 5 A 89 ASP LEU PHE GLY SER MET LYS GLN LEU GLU ASP LYS VAL
SEQRES 6 A 89 GLU GLU LEU LEU SER LYS ASN TYR HIS LEU GLU ASN GLU
SEQRES 7 A 89 VAL ALA ARG LEU LYS LYS LEU VAL GLY GLU ARG
SEQRES 1 B 89 GLY SER HIS MET PRO LEU LEU SER ILE ALA ARG GLN GLU
SEQRES 2 B 89 GLU GLU MET LYS GLU GLN LEU LYS GLN MET ASP LYS MET
SEQRES 3 B 89 LYS GLU ASP LEU ALA LYS THR GLU ARG ILE LYS LYS GLU
SEQRES 4 B 89 LEU GLU GLU GLN ASN VAL THR LEU LEU GLU GLN LYS ASN
SEQRES 5 B 89 ASP LEU PHE GLY SER MET LYS GLN LEU GLU ASP LYS VAL
SEQRES 6 B 89 GLU GLU LEU LEU SER LYS ASN TYR HIS LEU GLU ASN GLU
SEQRES 7 B 89 VAL ALA ARG LEU LYS LYS LEU VAL GLY GLU ARG
SEQRES 1 C 89 GLY SER HIS MET PRO LEU LEU SER ILE ALA ARG GLN GLU
SEQRES 2 C 89 GLU GLU MET LYS GLU GLN LEU LYS GLN MET ASP LYS MET
SEQRES 3 C 89 LYS GLU ASP LEU ALA LYS THR GLU ARG ILE LYS LYS GLU
SEQRES 4 C 89 LEU GLU GLU GLN ASN VAL THR LEU LEU GLU GLN LYS ASN
SEQRES 5 C 89 ASP LEU PHE GLY SER MET LYS GLN LEU GLU ASP LYS VAL
SEQRES 6 C 89 GLU GLU LEU LEU SER LYS ASN TYR HIS LEU GLU ASN GLU
SEQRES 7 C 89 VAL ALA ARG LEU LYS LYS LEU VAL GLY GLU ARG
SEQRES 1 D 89 GLY SER HIS MET PRO LEU LEU SER ILE ALA ARG GLN GLU
SEQRES 2 D 89 GLU GLU MET LYS GLU GLN LEU LYS GLN MET ASP LYS MET
SEQRES 3 D 89 LYS GLU ASP LEU ALA LYS THR GLU ARG ILE LYS LYS GLU
SEQRES 4 D 89 LEU GLU GLU GLN ASN VAL THR LEU LEU GLU GLN LYS ASN
SEQRES 5 D 89 ASP LEU PHE GLY SER MET LYS GLN LEU GLU ASP LYS VAL
SEQRES 6 D 89 GLU GLU LEU LEU SER LYS ASN TYR HIS LEU GLU ASN GLU
SEQRES 7 D 89 VAL ALA ARG LEU LYS LYS LEU VAL GLY GLU ARG
FORMUL 5 HOH *82(H2 O)
HELIX 1 1 MET A 846 GLY A 917 1 72
HELIX 2 2 GLU B 845 GLY B 917 1 73
HELIX 3 3 GLU C 845 GLY C 917 1 73
HELIX 4 4 GLU D 845 VAL D 916 1 72
CRYST1 54.034 73.303 102.975 90.00 90.00 90.00 P 21 21 21 16
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 0.018507 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013642 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009711 0.00000
(ATOM LINES ARE NOT SHOWN.)
END