Header list of 1osl.pdb file
Complete list - t 27 2 Bytes
HEADER TRANSCRIPTION/DNA 20-MAR-03 1OSL
TITLE SOLUTION STRUCTURE OF A DIMERIC LACTOSE DNA-BINDING DOMAIN COMPLEXED
TITLE 2 TO A NONSPECIFIC DNA SEQUENCE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*CP*GP*AP*TP*AP*AP*GP*AP*TP*AP*TP*CP*TP*TP*AP*TP*CP*G)
COMPND 3 -3';
COMPND 4 CHAIN: C, D;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: LACTOSE OPERON REPRESSOR;
COMPND 8 CHAIN: A, B;
COMPND 9 FRAGMENT: N-TERMINAL DNA-BINDING DOMAIN, RESIDUES 1-62;
COMPND 10 ENGINEERED: YES;
COMPND 11 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 5 ORGANISM_TAXID: 562;
SOURCE 6 GENE: LACI;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: DH9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET-HP62-V52C
KEYWDS PROTEIN-DNA COMPLEX, LAC REPRESSOR, NONSPECIFIC INTERACTION,
KEYWDS 2 TRANSCRIPTION-DNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.G.KALODIMOS,A.M.J.J.BONVIN,R.BOELENS,R.KAPTEIN
REVDAT 4 27-OCT-21 1OSL 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1OSL 1 VERSN
REVDAT 2 20-JUL-04 1OSL 1 JRNL
REVDAT 1 04-MAY-04 1OSL 0
JRNL AUTH C.G.KALODIMOS,N.BIRIS,A.M.BONVIN,M.M.LEVANDOSKI,
JRNL AUTH 2 M.GUENNUEGUES,R.BOELENS,R.KAPTEIN
JRNL TITL STRUCTURE AND FLEXIBILITY ADAPTATION IN NONSPECIFIC AND
JRNL TITL 2 SPECIFIC PROTEIN-DNA COMPLEXES.
JRNL REF SCIENCE V. 305 386 2004
JRNL REFN ISSN 0036-8075
JRNL PMID 15256668
JRNL DOI 10.1126/SCIENCE.1097064
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.0, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE OF THE COMPLEX WAS SOLVED
REMARK 3 ON THE BASIS OF 70 INTERMOLECULAR RESTRAINTS
REMARK 4
REMARK 4 1OSL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018627.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 5.8
REMARK 210 IONIC STRENGTH : 400MM KCL, 60MM KPI
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM LAC-HP62-V52C U-15N,13C,
REMARK 210 60MM KPI, 400MM KCL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 13C-15N DOUBLE-
REMARK 210 HALF NOESY FILTER
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, NMRVIEW 5.0.3, CNS
REMARK 210 1.1
REMARK 210 METHOD USED : THE STRUCTURE OF THE COMPLEX WAS
REMARK 210 CALCULATED AS FOLLOWS. FIRST THE
REMARK 210 STRUCTURE OF THE DIMERIC LACHP62-
REMARK 210 V52C WAS CALCULATED USING ONLY
REMARK 210 PROTEIN NMR RESTRAINTS. THE 100
REMARK 210 BEST STRUCTURES WERE SELECTED
REMARK 210 AND DOCKED ONTO THE NONSPECIFIC
REMARK 210 LAC OPERATOR B-DNA USING
REMARK 210 SIMULATED ANNEALING. DISTANCE
REMARK 210 AND PLANARITY RESTRAINTS FOR THE
REMARK 210 DNA WERE INCORPORATED IN ORDER
REMARK 210 TO KEEP DNA CLOSE TO B-DNA
REMARK 210 CONFORMATION.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D AND 3D
REMARK 210 HOMO- AND HETERONUCLEAR TECHNIQUES. 13C-15N LABELED PROTEIN AND
REMARK 210 UNLABELED NUCLEOTIDE WERE USED. IN ADDITION ISOTOPE FILTER
REMARK 210 EXPERIMENTS WERE APPLIED TO OBTAIN ADDITIONAL ASSIGNMENTS AND TO
REMARK 210 ASSIGN INTER-MOLECULAR NOES. FOR FURTHER DETAILS SEE THE
REMARK 210 REFERENCE DESCRIBING THE STRUCTURES.
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-20
REMARK 470 RES CSSEQI ATOMS
REMARK 470 ILE B 48 O
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 HA VAL A 23 HB1 ALA A 27 1.19
REMARK 500 HG11 VAL A 23 HG22 VAL A 38 1.21
REMARK 500 HH11 ARG A 22 HG23 VAL A 30 1.34
REMARK 500 HA VAL B 23 HB1 ALA B 27 1.34
REMARK 500 O TYR B 17 H SER B 21 1.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 2 TYR B 7 CE1 TYR B 7 CZ 0.135
REMARK 500 2 TYR B 7 CZ TYR B 7 CE2 -0.132
REMARK 500 3 TYR B 7 CE1 TYR B 7 CZ 0.123
REMARK 500 3 TYR B 7 CZ TYR B 7 CE2 -0.131
REMARK 500 3 TYR B 17 CE1 TYR B 17 CZ -0.166
REMARK 500 3 TYR B 17 CZ TYR B 17 CE2 0.147
REMARK 500 4 TYR A 12 CE1 TYR A 12 CZ 0.088
REMARK 500 4 TYR A 12 CZ TYR A 12 CE2 -0.091
REMARK 500 5 TYR B 7 CE1 TYR B 7 CZ 0.155
REMARK 500 5 TYR B 7 CZ TYR B 7 CE2 -0.155
REMARK 500 5 TYR B 47 CZ TYR B 47 CE2 0.085
REMARK 500 6 TYR A 17 CE1 TYR A 17 CZ -0.084
REMARK 500 6 TYR A 17 CZ TYR A 17 CE2 0.079
REMARK 500 6 TYR B 7 CE1 TYR B 7 CZ 0.220
REMARK 500 6 TYR B 7 CZ TYR B 7 CE2 -0.204
REMARK 500 6 TYR B 17 CE1 TYR B 17 CZ -0.168
REMARK 500 6 TYR B 17 CZ TYR B 17 CE2 0.160
REMARK 500 8 TYR A 17 CE1 TYR A 17 CZ -0.090
REMARK 500 8 TYR A 17 CZ TYR A 17 CE2 0.080
REMARK 500 8 TYR B 17 CE1 TYR B 17 CZ -0.127
REMARK 500 8 TYR B 17 CZ TYR B 17 CE2 0.117
REMARK 500 9 TYR B 7 CE1 TYR B 7 CZ 0.209
REMARK 500 9 TYR B 7 CZ TYR B 7 CE2 -0.213
REMARK 500 9 TYR B 17 CE1 TYR B 17 CZ -0.184
REMARK 500 9 TYR B 17 CZ TYR B 17 CE2 0.180
REMARK 500 10 TYR B 7 CE1 TYR B 7 CZ 0.160
REMARK 500 10 TYR B 7 CZ TYR B 7 CE2 -0.163
REMARK 500 10 TYR B 17 CE1 TYR B 17 CZ -0.127
REMARK 500 10 TYR B 17 CZ TYR B 17 CE2 0.120
REMARK 500 11 TYR A 12 CE1 TYR A 12 CZ 0.080
REMARK 500 11 TYR A 12 CZ TYR A 12 CE2 -0.080
REMARK 500 11 TYR B 7 CE1 TYR B 7 CZ 0.142
REMARK 500 11 TYR B 7 CZ TYR B 7 CE2 -0.133
REMARK 500 12 TYR B 17 CE1 TYR B 17 CZ -0.095
REMARK 500 12 TYR B 17 CZ TYR B 17 CE2 0.086
REMARK 500 13 TYR B 7 CE1 TYR B 7 CZ 0.182
REMARK 500 13 TYR B 7 CZ TYR B 7 CE2 -0.184
REMARK 500 13 TYR B 17 CE1 TYR B 17 CZ -0.105
REMARK 500 13 TYR B 17 CZ TYR B 17 CE2 0.095
REMARK 500 14 TYR B 12 CE1 TYR B 12 CZ 0.095
REMARK 500 14 TYR B 12 CZ TYR B 12 CE2 -0.095
REMARK 500 15 TYR B 7 CE1 TYR B 7 CZ 0.111
REMARK 500 15 TYR B 7 CZ TYR B 7 CE2 -0.112
REMARK 500 16 TYR B 7 CE1 TYR B 7 CZ 0.178
REMARK 500 16 TYR B 7 CZ TYR B 7 CE2 -0.161
REMARK 500 16 TYR B 17 CE1 TYR B 17 CZ -0.146
REMARK 500 16 TYR B 17 CZ TYR B 17 CE2 0.171
REMARK 500 17 TYR B 7 CE1 TYR B 7 CZ 0.093
REMARK 500 17 TYR B 7 CZ TYR B 7 CE2 -0.095
REMARK 500 18 TYR B 7 CE1 TYR B 7 CZ 0.130
REMARK 500
REMARK 500 THIS ENTRY HAS 55 BOND DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
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 4 DA D 3 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 6 TYR B 7 CD1 - CE1 - CZ ANGL. DEV. = -5.4 DEGREES
REMARK 500 6 TYR B 7 CE1 - CZ - OH ANGL. DEV. = -17.1 DEGREES
REMARK 500 8 DT C 11 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 18 DA D 3 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 19 DT C 11 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 19 THR B 19 N - CA - CB ANGL. DEV. = 11.7 DEGREES
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 PRO A 3 -173.73 -67.20
REMARK 500 1 GLN A 26 -55.63 176.79
REMARK 500 1 HIS A 29 75.19 -101.56
REMARK 500 1 ASN A 46 -47.85 74.48
REMARK 500 1 TYR A 47 96.60 59.58
REMARK 500 1 PRO A 49 -70.45 -61.93
REMARK 500 1 CYS A 52 -91.59 -111.87
REMARK 500 1 ALA A 53 72.86 -173.37
REMARK 500 1 GLN A 54 -67.90 -106.72
REMARK 500 1 ALA A 57 -76.21 -83.42
REMARK 500 1 LYS A 59 -65.92 -130.01
REMARK 500 1 GLN B 26 -44.48 163.63
REMARK 500 1 ASN B 46 -51.81 74.64
REMARK 500 1 TYR B 47 98.45 51.21
REMARK 500 1 ASN B 50 72.71 -153.86
REMARK 500 1 CYS B 52 -100.14 -95.85
REMARK 500 1 ALA B 53 82.27 -161.88
REMARK 500 2 PRO A 3 -109.13 -86.82
REMARK 500 2 GLN A 26 -41.09 86.77
REMARK 500 2 ALA A 27 -121.34 63.50
REMARK 500 2 SER A 28 -50.05 -166.22
REMARK 500 2 HIS A 29 -131.53 -99.89
REMARK 500 2 VAL A 30 150.40 73.93
REMARK 500 2 ASN A 46 -45.82 73.33
REMARK 500 2 TYR A 47 87.09 54.09
REMARK 500 2 ARG A 51 48.27 -99.71
REMARK 500 2 GLN A 55 -49.02 -140.56
REMARK 500 2 LEU A 56 -78.54 -179.76
REMARK 500 2 LYS A 59 -140.66 64.86
REMARK 500 2 LYS B 2 116.27 -160.25
REMARK 500 2 GLN B 26 74.16 87.94
REMARK 500 2 ASN B 46 -57.23 75.30
REMARK 500 2 TYR B 47 107.86 53.01
REMARK 500 2 ARG B 51 81.70 -157.52
REMARK 500 2 ALA B 53 -157.51 64.73
REMARK 500 2 GLN B 55 19.43 -161.33
REMARK 500 2 LYS B 59 -75.54 -129.26
REMARK 500 3 GLN A 26 -58.44 178.42
REMARK 500 3 ASN A 46 -48.00 74.25
REMARK 500 3 TYR A 47 76.01 49.90
REMARK 500 3 ASN A 50 -68.49 -153.49
REMARK 500 3 ARG A 51 -71.94 -90.36
REMARK 500 3 CYS A 52 -70.60 178.33
REMARK 500 3 ALA A 53 -160.14 -179.99
REMARK 500 3 GLN A 54 -77.73 -64.76
REMARK 500 3 GLN A 55 27.69 -143.01
REMARK 500 3 LYS B 2 -59.84 -124.10
REMARK 500 3 GLN B 26 -46.21 161.99
REMARK 500 3 ALA B 53 -169.62 74.66
REMARK 500 3 GLN B 54 -92.70 -84.01
REMARK 500
REMARK 500 THIS ENTRY HAS 365 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 2 TYR B 47 0.07 SIDE CHAIN
REMARK 500 5 TYR B 47 0.06 SIDE CHAIN
REMARK 500 6 TYR B 7 0.07 SIDE CHAIN
REMARK 500 7 TYR B 47 0.06 SIDE CHAIN
REMARK 500 9 TYR B 17 0.06 SIDE CHAIN
REMARK 500 11 TYR B 7 0.05 SIDE CHAIN
REMARK 500 16 TYR B 7 0.07 SIDE CHAIN
REMARK 500 16 TYR B 17 0.09 SIDE CHAIN
REMARK 500 19 TYR B 47 0.06 SIDE CHAIN
REMARK 500 20 TYR A 47 0.06 SIDE CHAIN
REMARK 500 20 TYR B 7 0.05 SIDE CHAIN
REMARK 500 20 TYR B 47 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1L1M RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED TO A NONSPECIFIC DNA OPERATOR
DBREF 1OSL A 1 62 UNP P03023 LACI_ECOLI 1 62
DBREF 1OSL B 1 62 UNP P03023 LACI_ECOLI 1 62
DBREF 1OSL C 1 18 PDB 1OSL 1OSL 1 18
DBREF 1OSL D 1 18 PDB 1OSL 1OSL 1 18
SEQADV 1OSL CYS A 52 UNP P03023 VAL 52 ENGINEERED MUTATION
SEQADV 1OSL CYS B 52 UNP P03023 VAL 52 ENGINEERED MUTATION
SEQRES 1 C 18 DC DG DA DT DA DA DG DA DT DA DT DC DT
SEQRES 2 C 18 DT DA DT DC DG
SEQRES 1 D 18 DC DG DA DT DA DA DG DA DT DA DT DC DT
SEQRES 2 D 18 DT DA DT DC DG
SEQRES 1 A 62 MET LYS PRO VAL THR LEU TYR ASP VAL ALA GLU TYR ALA
SEQRES 2 A 62 GLY VAL SER TYR GLN THR VAL SER ARG VAL VAL ASN GLN
SEQRES 3 A 62 ALA SER HIS VAL SER ALA LYS THR ARG GLU LYS VAL GLU
SEQRES 4 A 62 ALA ALA MET ALA GLU LEU ASN TYR ILE PRO ASN ARG CYS
SEQRES 5 A 62 ALA GLN GLN LEU ALA GLY LYS GLN SER LEU
SEQRES 1 B 62 MET LYS PRO VAL THR LEU TYR ASP VAL ALA GLU TYR ALA
SEQRES 2 B 62 GLY VAL SER TYR GLN THR VAL SER ARG VAL VAL ASN GLN
SEQRES 3 B 62 ALA SER HIS VAL SER ALA LYS THR ARG GLU LYS VAL GLU
SEQRES 4 B 62 ALA ALA MET ALA GLU LEU ASN TYR ILE PRO ASN ARG CYS
SEQRES 5 B 62 ALA GLN GLN LEU ALA GLY LYS GLN SER LEU
HELIX 1 1 THR A 5 GLY A 14 1 10
HELIX 2 2 SER A 16 GLN A 26 1 11
HELIX 3 3 SER A 31 LEU A 45 1 15
HELIX 4 4 THR B 5 GLY B 14 1 10
HELIX 5 5 SER B 16 GLN B 26 1 11
HELIX 6 6 SER B 31 LEU B 45 1 15
SSBOND 1 CYS A 52 CYS B 52 1555 1555 2.03
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 - t 27 2 Bytes