Header list of 1msf.pdb file
Complete list - b 23 2 Bytes
HEADER DNA BINDING PROTEIN/DNA 24-JAN-95 1MSF
TITLE SOLUTION STRUCTURE OF A SPECIFIC DNA COMPLEX OF THE MYB DNA-BINDING
TITLE 2 DOMAIN WITH COOPERATIVE RECOGNITION HELICES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-D(*CP*CP*TP*AP*AP*CP*TP*GP*AP*CP*AP*CP*AP*CP*AP*T)-
COMPND 3 3');
COMPND 4 CHAIN: A;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DNA (5'-D(*AP*TP*GP*TP*GP*TP*GP*TP*CP*AP*GP*TP*TP*AP*GP*G)-
COMPND 8 3');
COMPND 9 CHAIN: B;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: C-MYB DNA-BINDING DOMAIN;
COMPND 13 CHAIN: C;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 7 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 8 ORGANISM_TAXID: 10090;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PAR2156NCO1R23 (VECTOR:PAR2156NCO1)
KEYWDS DNA BINDING PROTEIN/DNA, DNA BINDING PROTEIN-DNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR K.OGATA,S.MORIKAWA,H.NAKAMURA,A.SEKIKAWA,T.INOUE,H.KANAI,A.SARAI,
AUTHOR 2 S.ISHII,Y.NISHIMURA
REVDAT 3 23-FEB-22 1MSF 1 REMARK
REVDAT 2 24-FEB-09 1MSF 1 VERSN
REVDAT 1 31-MAR-95 1MSF 0
JRNL AUTH K.OGATA,S.MORIKAWA,H.NAKAMURA,A.SEKIKAWA,T.INOUE,H.KANAI,
JRNL AUTH 2 A.SARAI,S.ISHII,Y.NISHIMURA
JRNL TITL SOLUTION STRUCTURE OF A SPECIFIC DNA COMPLEX OF THE MYB
JRNL TITL 2 DNA-BINDING DOMAIN WITH COOPERATIVE RECOGNITION HELICES.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 79 639 1994
JRNL REFN ISSN 0092-8674
JRNL PMID 7954830
JRNL DOI 10.1016/0092-8674(94)90549-5
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.OGATA,H.HOJO,S.AIMOTO,T.NAKAI,H.NAKAMURA,A.SARAI,S.ISHII,
REMARK 1 AUTH 2 Y.NISHIMURA
REMARK 1 TITL SOLUTION STRUCTURE OF A DNA-BINDING UNIT OF MYB: A
REMARK 1 TITL 2 HELIX-TURN-HELIX-RELATED MOTIF WITH CONSERVED TRYPTOPHANS
REMARK 1 TITL 3 FORMING A HYDROPHOBIC CORE
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 89 6428 1992
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MSF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175145.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-25
REMARK 465 RES C SSSEQI
REMARK 465 DC A 12
REMARK 465 DA A 13
REMARK 465 DC A 14
REMARK 465 DA A 15
REMARK 465 DT A 16
REMARK 465 DA B 17
REMARK 465 DT B 18
REMARK 465 DG B 19
REMARK 465 DT B 20
REMARK 465 DG B 21
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 DC A 1 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DC A 2 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 1 DT A 3 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 1 DT A 3 C4 - C5 - C6 ANGL. DEV. = 4.7 DEGREES
REMARK 500 1 DT A 3 C4 - C5 - C7 ANGL. DEV. = 4.2 DEGREES
REMARK 500 1 DT A 3 C6 - C5 - C7 ANGL. DEV. = -8.8 DEGREES
REMARK 500 1 DA A 4 O4' - C1' - N9 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 DA A 5 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 1 DT A 7 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 1 DT A 7 C4 - C5 - C6 ANGL. DEV. = 4.9 DEGREES
REMARK 500 1 DT A 7 C4 - C5 - C7 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 DT A 7 C6 - C5 - C7 ANGL. DEV. = -8.6 DEGREES
REMARK 500 1 DG A 8 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 1 DA A 9 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 1 DC A 10 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 1 DA A 11 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 1 DT B 22 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DT B 22 C4 - C5 - C6 ANGL. DEV. = 4.8 DEGREES
REMARK 500 1 DT B 22 C4 - C5 - C7 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 DT B 22 C6 - C5 - C7 ANGL. DEV. = -9.3 DEGREES
REMARK 500 1 DG B 23 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 1 DT B 24 O4' - C1' - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 1 DT B 24 C4 - C5 - C6 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 DT B 24 C4 - C5 - C7 ANGL. DEV. = 4.7 DEGREES
REMARK 500 1 DT B 24 C6 - C5 - C7 ANGL. DEV. = -9.2 DEGREES
REMARK 500 1 DC B 25 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 1 DA B 26 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 1 DG B 27 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DT B 28 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 1 DT B 28 C4 - C5 - C6 ANGL. DEV. = 4.7 DEGREES
REMARK 500 1 DT B 28 C4 - C5 - C7 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 DT B 28 C6 - C5 - C7 ANGL. DEV. = -9.2 DEGREES
REMARK 500 1 DT B 29 O4' - C1' - N1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 1 DT B 29 C4 - C5 - C6 ANGL. DEV. = 4.7 DEGREES
REMARK 500 1 DT B 29 C4 - C5 - C7 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 DT B 29 C6 - C5 - C7 ANGL. DEV. = -9.1 DEGREES
REMARK 500 1 DA B 30 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 1 DG B 31 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 1 DG B 32 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 2 DC A 1 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 2 DC A 2 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 2 DT A 3 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 2 DT A 3 C4 - C5 - C6 ANGL. DEV. = 4.8 DEGREES
REMARK 500 2 DT A 3 C4 - C5 - C7 ANGL. DEV. = 4.6 DEGREES
REMARK 500 2 DT A 3 C6 - C5 - C7 ANGL. DEV. = -9.3 DEGREES
REMARK 500 2 DA A 4 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 2 DA A 5 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 2 DC A 6 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 2 DT A 7 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 2 DT A 7 C4 - C5 - C6 ANGL. DEV. = 4.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 949 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
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 1 LYS C 92 -133.57 64.41
REMARK 500 1 LYS C 97 112.35 67.91
REMARK 500 1 GLU C 99 -61.98 -127.46
REMARK 500 1 ARG C 102 -64.20 -95.84
REMARK 500 1 TYR C 110 -62.90 -96.19
REMARK 500 1 LYS C 113 46.55 -169.19
REMARK 500 1 ARG C 114 31.31 -167.49
REMARK 500 1 LYS C 123 -91.59 62.39
REMARK 500 1 TRP C 134 -158.03 -80.63
REMARK 500 1 HIS C 135 75.66 30.82
REMARK 500 1 ASN C 136 -84.45 -166.79
REMARK 500 1 HIS C 137 27.92 -159.73
REMARK 500 1 ASN C 139 106.32 -31.98
REMARK 500 1 SER C 146 178.93 69.74
REMARK 500 1 THR C 148 -67.51 -159.75
REMARK 500 1 GLU C 149 -59.42 -150.29
REMARK 500 1 GLN C 157 -63.04 -104.59
REMARK 500 1 THR C 177 -174.08 -69.74
REMARK 500 1 ASN C 179 -47.67 -173.92
REMARK 500 1 ASN C 186 47.59 -74.20
REMARK 500 1 SER C 187 -43.52 -167.96
REMARK 500 1 MET C 189 40.74 -98.85
REMARK 500 1 ARG C 191 -3.90 -145.50
REMARK 500 2 PRO C 94 -81.70 -66.43
REMARK 500 2 TRP C 95 103.68 139.43
REMARK 500 2 THR C 96 144.44 172.43
REMARK 500 2 LYS C 97 114.23 74.65
REMARK 500 2 GLU C 99 -56.53 -129.28
REMARK 500 2 LYS C 113 45.09 -166.87
REMARK 500 2 ARG C 114 -43.99 -151.88
REMARK 500 2 TRP C 115 18.58 44.58
REMARK 500 2 SER C 116 -55.51 -120.86
REMARK 500 2 LYS C 123 -69.63 64.32
REMARK 500 2 ASN C 136 -86.54 -167.89
REMARK 500 2 HIS C 137 18.50 -156.79
REMARK 500 2 VAL C 142 -139.47 -85.75
REMARK 500 2 SER C 146 -146.34 57.47
REMARK 500 2 THR C 148 -49.99 -164.51
REMARK 500 2 GLU C 149 -37.26 -164.70
REMARK 500 2 ASP C 178 -108.57 41.33
REMARK 500 2 LYS C 182 -70.79 -63.17
REMARK 500 2 ASN C 186 25.11 -78.19
REMARK 500 2 SER C 187 -39.68 -163.89
REMARK 500 2 MET C 189 -89.74 -83.25
REMARK 500 2 ARG C 190 -68.08 -143.53
REMARK 500 2 ARG C 191 -61.92 -164.90
REMARK 500 2 LYS C 192 15.49 -148.81
REMARK 500 3 ILE C 91 27.66 -158.32
REMARK 500 3 LYS C 92 -35.12 -138.32
REMARK 500 3 GLU C 98 41.65 -86.29
REMARK 500
REMARK 500 THIS ENTRY HAS 532 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 DA A 4 0.11 SIDE CHAIN
REMARK 500 1 DG A 8 0.08 SIDE CHAIN
REMARK 500 1 DA A 9 0.06 SIDE CHAIN
REMARK 500 1 DC A 10 0.07 SIDE CHAIN
REMARK 500 1 DA A 11 0.07 SIDE CHAIN
REMARK 500 1 DT B 24 0.10 SIDE CHAIN
REMARK 500 1 DC B 25 0.07 SIDE CHAIN
REMARK 500 1 ARG C 133 0.23 SIDE CHAIN
REMARK 500 2 DC A 1 0.07 SIDE CHAIN
REMARK 500 2 DT B 22 0.11 SIDE CHAIN
REMARK 500 2 DC B 25 0.07 SIDE CHAIN
REMARK 500 2 ARG C 133 0.13 SIDE CHAIN
REMARK 500 3 DG A 8 0.08 SIDE CHAIN
REMARK 500 3 DA A 9 0.07 SIDE CHAIN
REMARK 500 3 DC A 10 0.12 SIDE CHAIN
REMARK 500 3 DC B 25 0.10 SIDE CHAIN
REMARK 500 3 DA B 30 0.07 SIDE CHAIN
REMARK 500 3 ARG C 114 0.11 SIDE CHAIN
REMARK 500 3 ARG C 165 0.10 SIDE CHAIN
REMARK 500 4 DT A 3 0.09 SIDE CHAIN
REMARK 500 4 DA A 4 0.09 SIDE CHAIN
REMARK 500 4 DC A 6 0.06 SIDE CHAIN
REMARK 500 4 DC B 25 0.07 SIDE CHAIN
REMARK 500 4 DA B 30 0.09 SIDE CHAIN
REMARK 500 4 DG B 31 0.06 SIDE CHAIN
REMARK 500 5 DC A 1 0.06 SIDE CHAIN
REMARK 500 5 DT A 7 0.07 SIDE CHAIN
REMARK 500 5 DG A 8 0.06 SIDE CHAIN
REMARK 500 5 DC A 10 0.09 SIDE CHAIN
REMARK 500 5 DC B 25 0.07 SIDE CHAIN
REMARK 500 5 ARG C 133 0.12 SIDE CHAIN
REMARK 500 6 DT A 3 0.06 SIDE CHAIN
REMARK 500 6 DA A 11 0.08 SIDE CHAIN
REMARK 500 6 DT B 22 0.07 SIDE CHAIN
REMARK 500 6 DT B 24 0.06 SIDE CHAIN
REMARK 500 6 DC B 25 0.07 SIDE CHAIN
REMARK 500 6 DA B 30 0.05 SIDE CHAIN
REMARK 500 6 ARG C 131 0.08 SIDE CHAIN
REMARK 500 6 ARG C 133 0.11 SIDE CHAIN
REMARK 500 7 DA A 4 0.07 SIDE CHAIN
REMARK 500 7 DC A 10 0.09 SIDE CHAIN
REMARK 500 7 DA B 30 0.08 SIDE CHAIN
REMARK 500 7 DG B 31 0.07 SIDE CHAIN
REMARK 500 8 DA A 4 0.07 SIDE CHAIN
REMARK 500 8 DT A 7 0.10 SIDE CHAIN
REMARK 500 8 DG A 8 0.10 SIDE CHAIN
REMARK 500 8 DG B 31 0.06 SIDE CHAIN
REMARK 500 9 DG A 8 0.06 SIDE CHAIN
REMARK 500 9 DC A 10 0.10 SIDE CHAIN
REMARK 500 9 DA A 11 0.10 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 173 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MSE RELATED DB: PDB
DBREF 1MSF C 90 193 UNP P06876 MYB_MOUSE 90 193
DBREF 1MSF A 1 16 PDB 1MSF 1MSF 1 16
DBREF 1MSF B 17 32 PDB 1MSF 1MSF 17 32
SEQRES 1 A 16 DC DC DT DA DA DC DT DG DA DC DA DC DA
SEQRES 2 A 16 DC DA DT
SEQRES 1 B 16 DA DT DG DT DG DT DG DT DC DA DG DT DT
SEQRES 2 B 16 DA DG DG
SEQRES 1 C 105 MET LEU ILE LYS GLY PRO TRP THR LYS GLU GLU ASP GLN
SEQRES 2 C 105 ARG VAL ILE LYS LEU VAL GLN LYS TYR GLY PRO LYS ARG
SEQRES 3 C 105 TRP SER VAL ILE ALA LYS HIS LEU LYS GLY ARG ILE GLY
SEQRES 4 C 105 LYS GLN CYS ARG GLU ARG TRP HIS ASN HIS LEU ASN PRO
SEQRES 5 C 105 GLU VAL LYS LYS THR SER TRP THR GLU GLU GLU ASP ARG
SEQRES 6 C 105 ILE ILE TYR GLN ALA HIS LYS ARG LEU GLY ASN ARG TRP
SEQRES 7 C 105 ALA GLU ILE ALA LYS LEU LEU PRO GLY ARG THR ASP ASN
SEQRES 8 C 105 ALA ILE LYS ASN HIS TRP ASN SER THR MET ARG ARG LYS
SEQRES 9 C 105 VAL
HELIX 1 H1 LYS C 97 TYR C 110 1 14
HELIX 2 H2 TRP C 115 HIS C 121 1 7
HELIX 3 H3 GLY C 127 HIS C 135 1 9
HELIX 4 H4 GLU C 149 LEU C 162 1 14
HELIX 5 H5 TRP C 166 LEU C 172 1 7
HELIX 6 H6 ASN C 179 ASN C 186 1 8
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - b 23 2 Bytes