HEADER ENDOCYTOSIS/EXOCYTOSIS 21-AUG-01 1JTH
TITLE CRYSTAL STRUCTURE AND BIOPHYSICAL PROPERTIES OF A COMPLEX BETWEEN THE
TITLE 2 N-TERMINAL REGION OF SNAP25 AND THE SNARE REGION OF SYNTAXIN 1A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SNAP25;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: N-TERMINAL SNARE MOTIF;
COMPND 5 SYNONYM: SYNAPTOSOMAL-ASSOCIATED PROTEIN SNAP-25;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: SYNTAXIN 1A;
COMPND 9 CHAIN: B, D;
COMPND 10 FRAGMENT: H3, SNARE MOTIF;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE9;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 12 ORGANISM_COMMON: NORWAY RAT;
SOURCE 13 ORGANISM_TAXID: 10116;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: JM190;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PGEX-KG
KEYWDS COILED-COIL, POLAR LAYER, ENDOCYTOSIS-EXOCYTOSIS COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.M.S.MISURA,L.C.GONZALEZ JR.,A.P.MAY,R.H.SCHELLER,W.I.WEIS
REVDAT 8 13-MAR-24 1JTH 1 REMARK
REVDAT 7 23-OCT-19 1JTH 1 REMARK
REVDAT 6 16-APR-14 1JTH 1 REMARK
REVDAT 5 16-NOV-11 1JTH 1 VERSN HETATM
REVDAT 4 24-FEB-09 1JTH 1 VERSN
REVDAT 3 01-APR-03 1JTH 1 JRNL
REVDAT 2 18-DEC-02 1JTH 1 REMARK
REVDAT 1 28-NOV-01 1JTH 0
JRNL AUTH K.M.MISURA,L.C.GONZALEZ JR.,A.P.MAY,R.H.SCHELLER,W.I.WEIS
JRNL TITL CRYSTAL STRUCTURE AND BIOPHYSICAL PROPERTIES OF A COMPLEX
JRNL TITL 2 BETWEEN THE N-TERMINAL SNARE REGION OF SNAP25 AND SYNTAXIN
JRNL TITL 3 1A.
JRNL REF J.BIOL.CHEM. V. 276 41301 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11533035
JRNL DOI 10.1074/JBC.M106853200
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 549679.840
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.8
REMARK 3 NUMBER OF REFLECTIONS : 18147
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) : 0.266
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 12.200
REMARK 3 FREE R VALUE TEST SET COUNT : 2206
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 69.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2080
REMARK 3 BIN R VALUE (WORKING SET) : 0.3550
REMARK 3 BIN FREE R VALUE : 0.3670
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 12.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 304
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2005
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 52
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.03000
REMARK 3 B22 (A**2) : 17.26000
REMARK 3 B33 (A**2) : -15.23000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -7.12000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.34
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) : 0.37
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.37
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 0.900
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 14.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.620
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) : 1.410 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.210 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.750 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.240 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 46.65
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JTH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-AUG-01.
REMARK 100 THE DEPOSITION ID IS D_1000014164.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JAN-01
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9292, 0.9795, 0.9797, 1.005
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
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 : 18147
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.8
REMARK 200 DATA REDUNDANCY : 2.200
REMARK 200 R MERGE (I) : 0.03900
REMARK 200 R SYM (I) : 0.02000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 30.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.32700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, MES, PH 6.5, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 294K
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 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 29.70000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.89000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 29.70000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.89000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 93 LIES ON A SPECIAL POSITION.
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 ALA A 2
REMARK 465 GLU A 3
REMARK 465 ASP A 4
REMARK 465 ALA A 5
REMARK 465 ASP A 6
REMARK 465 MET A 7
REMARK 465 ARG A 8
REMARK 465 ASN A 9
REMARK 465 GLU A 10
REMARK 465 GLU A 73
REMARK 465 ALA A 74
REMARK 465 GLU A 75
REMARK 465 LYS A 76
REMARK 465 ASN A 77
REMARK 465 LEU A 78
REMARK 465 THR A 79
REMARK 465 ASP A 80
REMARK 465 LEU A 81
REMARK 465 GLY A 82
REMARK 465 GLN B 258
REMARK 465 SER B 259
REMARK 465 LYS B 260
REMARK 465 ALA B 261
REMARK 465 ARG B 262
REMARK 465 ARG B 263
REMARK 465 LYS B 264
REMARK 465 LYS B 265
REMARK 465 ILE B 266
REMARK 465 MET B 267
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 GLU C 3
REMARK 465 ASP C 4
REMARK 465 ALA C 5
REMARK 465 ASP C 6
REMARK 465 MET C 7
REMARK 465 ARG C 8
REMARK 465 ASN C 9
REMARK 465 THR C 79
REMARK 465 ASP C 80
REMARK 465 LEU C 81
REMARK 465 GLY C 82
REMARK 465 ALA D 191
REMARK 465 LEU D 192
REMARK 465 SER D 193
REMARK 465 GLU D 194
REMARK 465 ARG D 246
REMARK 465 ALA D 247
REMARK 465 VAL D 248
REMARK 465 SER D 249
REMARK 465 ASP D 250
REMARK 465 THR D 251
REMARK 465 LYS D 252
REMARK 465 LYS D 253
REMARK 465 ALA D 254
REMARK 465 VAL D 255
REMARK 465 LYS D 256
REMARK 465 TYR D 257
REMARK 465 GLN D 258
REMARK 465 SER D 259
REMARK 465 LYS D 260
REMARK 465 ALA D 261
REMARK 465 ARG D 262
REMARK 465 ARG D 263
REMARK 465 LYS D 264
REMARK 465 LYS D 265
REMARK 465 ILE D 266
REMARK 465 MET D 267
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 LEU A 11 CG CD1 CD2
REMARK 470 GLU A 12 CG CD OE1 OE2
REMARK 470 GLU A 13 CG CD OE1 OE2
REMARK 470 LYS A 72 CG CD CE NZ
REMARK 470 GLU C 10 CG CD OE1 OE2
REMARK 470 GLU C 12 CG CD OE1 OE2
REMARK 470 ARG C 16 CG CD NE CZ NH1 NH2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SFC RELATED DB: PDB
REMARK 900 1SFC CONTAINS THE SYNTAXIN 1A H3 AND SNAP-25 N-TERMINAL PEPTIDES
REMARK 900 RELATED ID: 1DN1 RELATED DB: PDB
REMARK 900 1DN1 CONTAINS THE SYNTAXIN 1A H3 PEPTIDE
REMARK 900 RELATED ID: 1HVV RELATED DB: PDB
REMARK 900 1HVV CONTAINS A HOMO-TETRAMERIC ASSEMBLY OF THE SYNTAXIN 1A H3
REMARK 900 PEPTIDE
DBREF 1JTH A 1 82 UNP P60881 SNP25_RAT 1 82
DBREF 1JTH C 1 82 UNP P60881 SNP25_RAT 1 82
DBREF 1JTH B 191 267 UNP P32851 STX1A_RAT 191 267
DBREF 1JTH D 191 267 UNP P32851 STX1A_RAT 191 267
SEQRES 1 A 82 MET ALA GLU ASP ALA ASP MET ARG ASN GLU LEU GLU GLU
SEQRES 2 A 82 MET GLN ARG ARG ALA ASP GLN LEU ALA ASP GLU SER LEU
SEQRES 3 A 82 GLU SER THR ARG ARG MET LEU GLN LEU VAL GLU GLU SER
SEQRES 4 A 82 LYS ASP ALA GLY ILE ARG THR LEU VAL MET LEU ASP GLU
SEQRES 5 A 82 GLN GLY GLU GLN LEU GLU ARG ILE GLU GLU GLY MET ASP
SEQRES 6 A 82 GLN ILE ASN LYS ASP MET LYS GLU ALA GLU LYS ASN LEU
SEQRES 7 A 82 THR ASP LEU GLY
SEQRES 1 B 77 ALA LEU SER GLU ILE GLU THR ARG HIS SER GLU ILE ILE
SEQRES 2 B 77 LYS LEU GLU ASN SER ILE ARG GLU LEU HIS ASP MET PHE
SEQRES 3 B 77 MET ASP MET ALA MET LEU VAL GLU SER GLN GLY GLU MET
SEQRES 4 B 77 ILE ASP ARG ILE GLU TYR ASN VAL GLU HIS ALA VAL ASP
SEQRES 5 B 77 TYR VAL GLU ARG ALA VAL SER ASP THR LYS LYS ALA VAL
SEQRES 6 B 77 LYS TYR GLN SER LYS ALA ARG ARG LYS LYS ILE MET
SEQRES 1 C 82 MET ALA GLU ASP ALA ASP MET ARG ASN GLU LEU GLU GLU
SEQRES 2 C 82 MET GLN ARG ARG ALA ASP GLN LEU ALA ASP GLU SER LEU
SEQRES 3 C 82 GLU SER THR ARG ARG MET LEU GLN LEU VAL GLU GLU SER
SEQRES 4 C 82 LYS ASP ALA GLY ILE ARG THR LEU VAL MET LEU ASP GLU
SEQRES 5 C 82 GLN GLY GLU GLN LEU GLU ARG ILE GLU GLU GLY MET ASP
SEQRES 6 C 82 GLN ILE ASN LYS ASP MET LYS GLU ALA GLU LYS ASN LEU
SEQRES 7 C 82 THR ASP LEU GLY
SEQRES 1 D 77 ALA LEU SER GLU ILE GLU THR ARG HIS SER GLU ILE ILE
SEQRES 2 D 77 LYS LEU GLU ASN SER ILE ARG GLU LEU HIS ASP MET PHE
SEQRES 3 D 77 MET ASP MET ALA MET LEU VAL GLU SER GLN GLY GLU MET
SEQRES 4 D 77 ILE ASP ARG ILE GLU TYR ASN VAL GLU HIS ALA VAL ASP
SEQRES 5 D 77 TYR VAL GLU ARG ALA VAL SER ASP THR LYS LYS ALA VAL
SEQRES 6 D 77 LYS TYR GLN SER LYS ALA ARG ARG LYS LYS ILE MET
FORMUL 5 HOH *52(H2 O)
HELIX 1 1 LEU A 11 LYS A 72 1 62
HELIX 2 2 ALA B 191 TYR B 257 1 67
HELIX 3 3 GLU C 10 LEU C 78 1 69
HELIX 4 4 ILE D 195 GLU D 245 1 51
CRYST1 59.400 65.780 80.100 90.00 99.50 90.00 C 1 2 1 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 0.016835 0.000000 0.002817 0.00000
SCALE2 0.000000 0.015202 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012658 0.00000
(ATOM LINES ARE NOT SHOWN.)
END