Header list of 1c7u.pdb file
Complete list - 16 20 Bytes
HEADER TRANSCRIPTION/DNA 17-MAR-00 1C7U
TITLE COMPLEX OF THE DNA BINDING CORE DOMAIN OF THE TRANSCRIPTION FACTOR
TITLE 2 MEF2A WITH A 20MER OLIGONUCLEOTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*CP*TP*CP*GP*GP*CP*TP*AP*TP*TP*AP*AP*TP*AP*GP*CP*CP*GP
COMPND 3 *AP*G)-3';
COMPND 4 CHAIN: C, D;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: MYOCYTE-SPECIFIC ENHANCER FACTOR 2A, C4 FORM;
COMPND 8 CHAIN: A, B;
COMPND 9 FRAGMENT: RESIDUES 2-86;
COMPND 10 SYNONYM: TRANSCRIPTION FACTOR MEF2A;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 5 ORGANISM_COMMON: HUMAN;
SOURCE 6 ORGANISM_TAXID: 9606;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BE23;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS DNA BINDING PROTEIN, TRANSCRIPTION FACTOR, MADS-BOX, SAM DOMAIN,
KEYWDS 2 TRANSCRIPTION-DNA COMPLEX
EXPDTA SOLUTION NMR
AUTHOR G.M.CLORE,K.HUANG
REVDAT 5 16-FEB-22 1C7U 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1C7U 1 VERSN
REVDAT 3 05-APR-05 1C7U 1 JRNL COMPND REMARK
REVDAT 2 14-JUN-00 1C7U 1 JRNL
REVDAT 1 27-MAR-00 1C7U 0
JRNL AUTH K.HUANG,J.M.LOUIS,L.DONALDSON,F.L.LIM,A.D.SHARROCKS,
JRNL AUTH 2 G.M.CLORE
JRNL TITL SOLUTION STRUCTURE OF THE MEF2A-DNA COMPLEX: STRUCTURAL
JRNL TITL 2 BASIS FOR THE MODULATION OF DNA BENDING AND SPECIFICITY BY
JRNL TITL 3 MADS-BOX TRANSCRIPTION FACTORS
JRNL REF EMBO J. V. 19 2615 2000
JRNL REFN ISSN 0261-4189
JRNL PMID 10835359
JRNL DOI 10.1093/EMBOJ/19.11.2615
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR/CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS, CLORE, DELANO, GROS, GROSSE
REMARK 3 -KUNSTLEVE, JIANG, KUSZEWSKI, NILGES, PANNU, READ,
REMARK 3 RICE WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING
REMARK 3 PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229, 129-136 USING THE
REMARK 3 PROGRAM XPLOR/CNS MODIFIED TO INCORPORATE COUPLING CONSTANT
REMARK 3 RESTRAINTS (GARRETT ET AL. (1984) J. MAGN. RESON. SERIES B 104, 99-
REMARK 3 103), CARBON CHEMICAL SHIFT RESTRAINTS, (KUSZEWSKI ET AL. (1995)
REMARK 3 J. MAGN. RESON. SERIES B 106, 92-96) RESTRAINTS, RESIDUAL DIPOLAR
REMARK 3 COUPLING RESTRAINTS (CLORE ET AL. J. MAGN. RESON 131, 159-162
REMARK 3 (1998); J. MAGN 133, 216-221 (1998)), AND A CONFORMATIONAL
REMARK 3 DATABASE POTENTIAL FOR PROTEINS AND NUCLEIC ACIDS (KUSZEWSKI ET
REMARK 3 AL. PROTEIN SCI. 5, 1067-1080 (1996); J. MAGN. RESON 125, 171-177
REMARK 3 (1997)).
REMARK 3
REMARK 3 IN THIS ENTRY THE LAST NUMERICAL COLUMN IS THE RMS OF THE
REMARK 3 35 INDIVIDUAL SIMULATED ANNEALING STRUCTURES ABOUT THE
REMARK 3 MEAN COORDINATE POSITIONS. THE LATTER ARE OBTAINED
REMARK 3 BY TAKING THE AVERAGE OF THE 35 SIMULATED ANNEALING
REMARK 3 STRUCTURES BEST-FITTED TO RESIDUES 1-73 AND 101-173
REMARK 3 OF THE PROTEIN AND RESIDUES 201-240 OF THE DNA.
REMARK 3 RESIDUES 74-85 AND 174-185 ARE DISORDERED IN SOLUTION
REMARK 3 AND ARE THEREFORE NOT INCLUDED IN THE COORDINATES.
REMARK 3 THE RESTRAINED MINIMIZED MEAN STRUCTURE IS OBTAINED
REMARK 3 BY RESTRAINED REGULARIZATION OF THE AVERAGE COORDINATES
REMARK 3 AGAINST THE SAME TARGET FUNCTION USED TO CALCULATE THE
REMARK 3 SIMULATED ANNEALING STRUCTURES.
REMARK 4
REMARK 4 1C7U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-00.
REMARK 100 THE DEPOSITION ID IS D_1000001443.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : (1) TRIPLE RESONANCE FOR
REMARK 210 ASSIGNMENT OF PROTEIN. (2)
REMARK 210 QUANTITATIVE J CORRELATION FOR
REMARK 210 COUPLING CONSTANTS. (3) 3D AND
REMARK 210 4D HETERONUCLEAR SEPARATED AND
REMARK 210 FILTERED NOE EXPTS. (4) 2D 12C-
REMARK 210 FILTERED EXPERIMENTS FOR DNA
REMARK 210 ASSIGNMENTS. (5) IPAP EXPTS FOR
REMARK 210 DIPOLAR COUPLINGS DIPOLAR
REMARK 210 COUPLINGS WERE MEASURED IN A
REMARK 210 BICELLE LIQUID CRYSTALLINE
REMARK 210 MEDIUM.
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS/X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 35
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : REGULARIZED MEAN STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: SOLVED BY MULTI HETERONUCLEAR NMR AND IS BASED ON 4560
REMARK 210 EXPERIMENTAL NMR RESTRAINTS (I.E. 2280 UNIQUE ONES SINCE PROTEIN
REMARK 210 IS A HOMODIMER AND DNA IS PALINDROMIC). NOE RESTRAINTS: (A)
REMARK 210 PROTEIN: 664 SEQUENTIAL, 504 MEDIUM RANGE, 212 LONG RANGE, 616
REMARK 210 INTRARESIDUE, 174 INTERSUBUNIT. (B) DNA: 428 INTRARESIDUE, 196
REMARK 210 SEQUENTIAL INTRASTRAND, 24 INTERSTRAND. (C) PROTEIN- DNA 168. H-
REMARK 210 BOND RESTRAINTS: PROTEIN 138, DNA 120. TORSION ANGLE RESTRAINTS:
REMARK 210 PROTEIN 480 (142 PHI, 142 PSI, 112 CHI1, 68 CHI2, 16 CHI3), DNA
REMARK 210 228. THREE-BOND HN-HALPHA COUPLING CONSTANTS: 72. SECONDARY 13C
REMARK 210 SHIFTS: 140 13CALPHA, 140 13CBETA. DIPOLAR COUPLINGS: 1DNH
REMARK 210 PROTEIN: 70, 1DCH DNA 70. REPULSIVE RESTRAINTS: 106
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 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 RES C SSSEQI
REMARK 465 HIS A 75
REMARK 465 GLU A 76
REMARK 465 SER A 77
REMARK 465 ARG A 78
REMARK 465 THR A 79
REMARK 465 ASN A 80
REMARK 465 SER A 81
REMARK 465 ASP A 82
REMARK 465 ILE A 83
REMARK 465 VAL A 84
REMARK 465 GLU A 85
REMARK 465 HIS B 175
REMARK 465 GLU B 176
REMARK 465 SER B 177
REMARK 465 ARG B 178
REMARK 465 THR B 179
REMARK 465 ASN B 180
REMARK 465 SER B 181
REMARK 465 ASP B 182
REMARK 465 ILE B 183
REMARK 465 VAL B 184
REMARK 465 GLU B 185
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 O LYS B 163 H LYS B 167 1.53
REMARK 500 O LYS A 63 H LYS A 67 1.53
REMARK 500 O ARG B 123 H LEU B 127 1.55
REMARK 500 O ARG A 23 H LEU A 27 1.55
REMARK 500 O LEU B 127 H LYS B 130 1.60
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 DT C 209 C5 DT C 209 C7 0.038
REMARK 500 DT C 210 C5 DT C 210 C7 0.037
REMARK 500 DT D 229 C5 DT D 229 C7 0.038
REMARK 500 DT D 230 C5 DT D 230 C7 0.037
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 DC C 201 C4' - C3' - C2' ANGL. DEV. = 7.6 DEGREES
REMARK 500 DC C 201 O4' - C1' - C2' ANGL. DEV. = 3.7 DEGREES
REMARK 500 DT C 202 C4' - C3' - C2' ANGL. DEV. = 6.4 DEGREES
REMARK 500 DC C 203 C4' - C3' - C2' ANGL. DEV. = 7.0 DEGREES
REMARK 500 DG C 204 C4' - C3' - C2' ANGL. DEV. = 7.7 DEGREES
REMARK 500 DG C 204 O4' - C1' - C2' ANGL. DEV. = 3.7 DEGREES
REMARK 500 DG C 205 C4' - C3' - C2' ANGL. DEV. = 6.2 DEGREES
REMARK 500 DG C 205 O4' - C1' - C2' ANGL. DEV. = 3.4 DEGREES
REMARK 500 DC C 206 C4' - C3' - C2' ANGL. DEV. = 7.2 DEGREES
REMARK 500 DC C 206 O4' - C1' - C2' ANGL. DEV. = 3.1 DEGREES
REMARK 500 DT C 207 C4' - C3' - C2' ANGL. DEV. = 7.0 DEGREES
REMARK 500 DA C 208 C4' - C3' - C2' ANGL. DEV. = 5.9 DEGREES
REMARK 500 DA C 208 O4' - C1' - C2' ANGL. DEV. = 3.1 DEGREES
REMARK 500 DT C 209 C4' - C3' - C2' ANGL. DEV. = 7.1 DEGREES
REMARK 500 DT C 209 O4' - C1' - C2' ANGL. DEV. = 3.5 DEGREES
REMARK 500 DT C 210 C4' - C3' - C2' ANGL. DEV. = 8.0 DEGREES
REMARK 500 DT C 210 O4' - C1' - C2' ANGL. DEV. = 3.7 DEGREES
REMARK 500 DA C 211 C4' - C3' - C2' ANGL. DEV. = 8.4 DEGREES
REMARK 500 DA C 211 O4' - C1' - C2' ANGL. DEV. = 3.2 DEGREES
REMARK 500 DA C 212 C4' - C3' - C2' ANGL. DEV. = 7.8 DEGREES
REMARK 500 DT C 213 C4' - C3' - C2' ANGL. DEV. = 7.3 DEGREES
REMARK 500 DT C 213 O4' - C1' - C2' ANGL. DEV. = 3.9 DEGREES
REMARK 500 DA C 214 C4' - C3' - C2' ANGL. DEV. = 6.8 DEGREES
REMARK 500 DG C 215 C4' - C3' - C2' ANGL. DEV. = 7.1 DEGREES
REMARK 500 DC C 216 C4' - C3' - C2' ANGL. DEV. = 6.5 DEGREES
REMARK 500 DC C 217 C4' - C3' - C2' ANGL. DEV. = 6.8 DEGREES
REMARK 500 DG C 218 C4' - C3' - C2' ANGL. DEV. = 6.5 DEGREES
REMARK 500 DA C 219 C4' - C3' - C2' ANGL. DEV. = 6.2 DEGREES
REMARK 500 DG C 220 C4' - C3' - C2' ANGL. DEV. = 5.5 DEGREES
REMARK 500 DC D 221 C4' - C3' - C2' ANGL. DEV. = 7.5 DEGREES
REMARK 500 DC D 221 O4' - C1' - C2' ANGL. DEV. = 3.7 DEGREES
REMARK 500 DT D 222 C4' - C3' - C2' ANGL. DEV. = 6.4 DEGREES
REMARK 500 DC D 223 C4' - C3' - C2' ANGL. DEV. = 7.0 DEGREES
REMARK 500 DG D 224 C4' - C3' - C2' ANGL. DEV. = 7.8 DEGREES
REMARK 500 DG D 224 O4' - C1' - C2' ANGL. DEV. = 3.7 DEGREES
REMARK 500 DG D 225 C4' - C3' - C2' ANGL. DEV. = 6.3 DEGREES
REMARK 500 DG D 225 O4' - C1' - C2' ANGL. DEV. = 3.4 DEGREES
REMARK 500 DC D 226 C4' - C3' - C2' ANGL. DEV. = 7.2 DEGREES
REMARK 500 DC D 226 O4' - C1' - C2' ANGL. DEV. = 3.1 DEGREES
REMARK 500 DT D 227 C4' - C3' - C2' ANGL. DEV. = 7.0 DEGREES
REMARK 500 DA D 228 C4' - C3' - C2' ANGL. DEV. = 5.9 DEGREES
REMARK 500 DA D 228 O4' - C1' - C2' ANGL. DEV. = 3.1 DEGREES
REMARK 500 DT D 229 C4' - C3' - C2' ANGL. DEV. = 7.2 DEGREES
REMARK 500 DT D 229 O4' - C1' - C2' ANGL. DEV. = 3.5 DEGREES
REMARK 500 DT D 230 C4' - C3' - C2' ANGL. DEV. = 8.0 DEGREES
REMARK 500 DT D 230 O4' - C1' - C2' ANGL. DEV. = 3.7 DEGREES
REMARK 500 DA D 231 C4' - C3' - C2' ANGL. DEV. = 8.5 DEGREES
REMARK 500 DA D 232 C4' - C3' - C2' ANGL. DEV. = 7.8 DEGREES
REMARK 500 DT D 233 C4' - C3' - C2' ANGL. DEV. = 7.4 DEGREES
REMARK 500 DT D 233 O4' - C1' - C2' ANGL. DEV. = 3.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 57 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 ARG A 2 -9.41 -57.91
REMARK 500 ASN A 51 74.26 67.48
REMARK 500 ASP A 60 107.37 49.99
REMARK 500 ARG B 102 -9.31 -57.92
REMARK 500 ASN B 151 74.19 66.50
REMARK 500 ASP B 160 107.40 50.25
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1C7U A 1 85 UNP Q02078 MEF2A_HUMAN 2 86
DBREF 1C7U B 101 185 UNP Q02078 MEF2A_HUMAN 2 86
DBREF 1C7U C 201 220 PDB 1C7U 1C7U 201 220
DBREF 1C7U D 221 240 PDB 1C7U 1C7U 221 240
SEQADV 1C7U ALA A 38 UNP Q02078 CYS 39 CONFLICT
SEQADV 1C7U ALA A 40 UNP Q02078 CYS 41 CONFLICT
SEQADV 1C7U ALA B 138 UNP Q02078 CYS 39 CONFLICT
SEQADV 1C7U ALA B 140 UNP Q02078 CYS 41 CONFLICT
SEQRES 1 C 20 DC DT DC DG DG DC DT DA DT DT DA DA DT
SEQRES 2 C 20 DA DG DC DC DG DA DG
SEQRES 1 D 20 DC DT DC DG DG DC DT DA DT DT DA DA DT
SEQRES 2 D 20 DA DG DC DC DG DA DG
SEQRES 1 A 85 GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP GLU
SEQRES 2 A 85 ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE GLY
SEQRES 3 A 85 LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU ALA ASP
SEQRES 4 A 85 ALA GLU ILE ALA LEU ILE ILE PHE ASN SER SER ASN LYS
SEQRES 5 A 85 LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL LEU
SEQRES 6 A 85 LEU LYS TYR THR GLU TYR ASN GLU PRO HIS GLU SER ARG
SEQRES 7 A 85 THR ASN SER ASP ILE VAL GLU
SEQRES 1 B 85 GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP GLU
SEQRES 2 B 85 ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE GLY
SEQRES 3 B 85 LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU ALA ASP
SEQRES 4 B 85 ALA GLU ILE ALA LEU ILE ILE PHE ASN SER SER ASN LYS
SEQRES 5 B 85 LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL LEU
SEQRES 6 B 85 LEU LYS TYR THR GLU TYR ASN GLU PRO HIS GLU SER ARG
SEQRES 7 B 85 THR ASN SER ASP ILE VAL GLU
HELIX 1 1 ASP A 12 ASP A 39 1 28
HELIX 2 2 ASP A 60 ASN A 72 1 13
HELIX 3 3 ASP B 112 ASP B 139 1 28
HELIX 4 4 ASP B 160 ASN B 172 1 13
SHEET 1 A 4 LYS A 52 TYR A 56 0
SHEET 2 A 4 ILE A 42 ASN A 48 -1 N LEU A 44 O TYR A 56
SHEET 3 A 4 GLU B 141 ASN B 148 -1 O GLU B 141 N PHE A 47
SHEET 4 A 4 LYS B 152 TYR B 156 -1 O LYS B 152 N ASN B 148
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
Complete list - 16 20 Bytes