Header list of 2hdc.pdb file
Complete list - r 9 2 Bytes
HEADER PROTEIN/DNA 05-MAY-99 2HDC
TITLE STRUCTURE OF TRANSCRIPTION FACTOR GENESIS/DNA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-
COMPND 3 D(P*GP*CP*TP*TP*AP*AP*AP*AP*TP*AP*AP*CP*AP*AP*TP*AP*C)-3');
COMPND 4 CHAIN: B;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DNA (5'-
COMPND 8 D(P*GP*TP*AP*TP*TP*GP*TP*TP*AP*TP*TP*TP*TP*AP*AP*GP*C)-3');
COMPND 9 CHAIN: C;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: PROTEIN (TRANSCRIPTION FACTOR);
COMPND 13 CHAIN: A;
COMPND 14 FRAGMENT: DNA BINDING DOMAIN;
COMPND 15 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: RATTUS NORVEGICUS;
SOURCE 7 ORGANISM_COMMON: NORWAY RAT;
SOURCE 8 ORGANISM_TAXID: 10116;
SOURCE 9 ORGANELLE: NUCLEUS;
SOURCE 10 GENE: GENESIS
KEYWDS DYANAMICS, GENESIS, WINGED HELIX PROTEIN, PROTEIN-DNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.JIN,I.MARSDEN,X.CHEN,X.LIAO
REVDAT 3 09-MAR-22 2HDC 1 REMARK
REVDAT 2 24-FEB-09 2HDC 1 VERSN
REVDAT 1 05-JUL-99 2HDC 0
JRNL AUTH C.JIN,I.MARSDEN,X.CHEN,X.LIAO
JRNL TITL DYNAMIC DNA CONTACTS OBSERVED IN THE NMR STRUCTURE OF WINGED
JRNL TITL 2 HELIX PROTEIN-DNA COMPLEX.
JRNL REF J.MOL.BIOL. V. 289 683 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10369754
JRNL DOI 10.1006/JMBI.1999.2819
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5
REMARK 3 AUTHORS : GUNTERT, PETER, ET AL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HDC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAY-99.
REMARK 100 THE DEPOSITION ID IS D_1000001006.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; HNCA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N (AND 2H)-LABELED SAMPLE
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: B, C, A
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 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 LEU A 24 H TRP A 77 1.54
REMARK 500 O4 DT B 251 H61 DA C 363 1.54
REMARK 500 H61 DA B 261 O4 DT C 353 1.54
REMARK 500 O4 DT B 252 H61 DA C 362 1.55
REMARK 500 H61 DA B 259 O4 DT C 355 1.57
REMARK 500 O ILE A 33 H PHE A 37 1.57
REMARK 500 O ALA A 10 HG1 THR A 13 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 1 DG B 249 O4' DG B 249 C4' -0.297
REMARK 500 1 DT B 251 O4' DT B 251 C4' 0.145
REMARK 500 1 DA B 253 O4' DA B 253 C4' 0.091
REMARK 500 1 DA B 254 O4' DA B 254 C4' -0.365
REMARK 500 1 DA B 255 O4' DA B 255 C4' -0.280
REMARK 500 1 DA B 256 O4' DA B 256 C4' 0.181
REMARK 500 1 DT B 257 O4' DT B 257 C4' -0.074
REMARK 500 1 DA B 259 O4' DA B 259 C4' 0.093
REMARK 500 1 DC B 260 O4' DC B 260 C4' 0.249
REMARK 500 1 DA B 261 O4' DA B 261 C4' 0.123
REMARK 500 1 DA B 262 O4' DA B 262 C4' 0.077
REMARK 500 1 DT B 263 O4' DT B 263 C4' 0.310
REMARK 500 1 DC B 265 O4' DC B 265 C4' 0.118
REMARK 500 1 DT C 350 O4' DT C 350 C4' 0.123
REMARK 500 1 DT C 353 O4' DT C 353 C4' 0.123
REMARK 500 1 DG C 354 O4' DG C 354 C4' 0.156
REMARK 500 1 DA C 357 O4' DA C 357 C4' -0.334
REMARK 500 1 DT C 359 O4' DT C 359 C4' 0.251
REMARK 500 1 DA C 362 O4' DA C 362 C4' -0.137
REMARK 500 1 DG C 364 O4' DG C 364 C4' 0.154
REMARK 500 1 DC C 365 O4' DC C 365 C4' -0.197
REMARK 500 2 DT B 251 O4' DT B 251 C4' 0.158
REMARK 500 2 DT B 252 O4' DT B 252 C4' 0.141
REMARK 500 2 DA B 253 O4' DA B 253 C4' 0.128
REMARK 500 2 DA B 254 O4' DA B 254 C4' -0.378
REMARK 500 2 DA B 255 O4' DA B 255 C4' 0.233
REMARK 500 2 DA B 256 O4' DA B 256 C4' 0.299
REMARK 500 2 DT B 257 O4' DT B 257 C4' 0.151
REMARK 500 2 DA B 259 O4' DA B 259 C4' 0.068
REMARK 500 2 DC B 260 O4' DC B 260 C4' 0.314
REMARK 500 2 DA B 261 O4' DA B 261 C4' 0.158
REMARK 500 2 DA B 262 O4' DA B 262 C4' 0.066
REMARK 500 2 DT B 263 O4' DT B 263 C4' 0.326
REMARK 500 2 DG C 349 O4' DG C 349 C4' -0.069
REMARK 500 2 DT C 350 O4' DT C 350 C4' 0.082
REMARK 500 2 DA C 351 O4' DA C 351 C4' 0.094
REMARK 500 2 DT C 352 O4' DT C 352 C4' -0.358
REMARK 500 2 DG C 354 O4' DG C 354 C4' 0.100
REMARK 500 2 DA C 357 O4' DA C 357 C4' 0.131
REMARK 500 2 DT C 361 O4' DT C 361 C4' 0.055
REMARK 500 2 DA C 362 O4' DA C 362 C4' 0.076
REMARK 500 2 DG C 364 O4' DG C 364 C4' 0.164
REMARK 500 2 DC C 365 O4' DC C 365 C4' -0.226
REMARK 500 3 DT B 251 O4' DT B 251 C4' 0.200
REMARK 500 3 DA B 253 O4' DA B 253 C4' 0.129
REMARK 500 3 DA B 254 O4' DA B 254 C4' -0.370
REMARK 500 3 DA B 255 O4' DA B 255 C4' -0.303
REMARK 500 3 DA B 256 O4' DA B 256 C4' 0.255
REMARK 500 3 DA B 258 O4' DA B 258 C4' 0.071
REMARK 500 3 DA B 259 O4' DA B 259 C4' 0.191
REMARK 500
REMARK 500 THIS ENTRY HAS 488 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 1 DG B 249 C5' - C4' - O4' ANGL. DEV. = -16.6 DEGREES
REMARK 500 1 DG B 249 C1' - O4' - C4' ANGL. DEV. = 9.1 DEGREES
REMARK 500 1 DG B 249 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DG B 249 C6 - N1 - C2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 1 DG B 249 N1 - C2 - N3 ANGL. DEV. = 5.2 DEGREES
REMARK 500 1 DG B 249 C5 - C6 - N1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 1 DC B 250 O4' - C4' - C3' ANGL. DEV. = -8.5 DEGREES
REMARK 500 1 DC B 250 C1' - O4' - C4' ANGL. DEV. = 6.8 DEGREES
REMARK 500 1 DC B 250 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DT B 251 O4' - C4' - C3' ANGL. DEV. = -15.3 DEGREES
REMARK 500 1 DT B 251 C5' - C4' - O4' ANGL. DEV. = 45.4 DEGREES
REMARK 500 1 DT B 251 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DT B 251 C2 - N3 - C4 ANGL. DEV. = -3.6 DEGREES
REMARK 500 1 DT B 252 O4' - C4' - C3' ANGL. DEV. = -8.7 DEGREES
REMARK 500 1 DT B 252 C5' - C4' - O4' ANGL. DEV. = 34.5 DEGREES
REMARK 500 1 DT B 252 C1' - O4' - C4' ANGL. DEV. = 6.3 DEGREES
REMARK 500 1 DT B 252 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DT B 252 C2 - N3 - C4 ANGL. DEV. = -3.6 DEGREES
REMARK 500 1 DA B 253 O4' - C4' - C3' ANGL. DEV. = -14.4 DEGREES
REMARK 500 1 DA B 253 C5' - C4' - O4' ANGL. DEV. = 42.9 DEGREES
REMARK 500 1 DA B 253 C1' - O4' - C4' ANGL. DEV. = 4.4 DEGREES
REMARK 500 1 DA B 253 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DA B 254 C5' - C4' - O4' ANGL. DEV. = 28.6 DEGREES
REMARK 500 1 DA B 254 C1' - O4' - C4' ANGL. DEV. = 12.9 DEGREES
REMARK 500 1 DA B 254 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DA B 255 C5' - C4' - O4' ANGL. DEV. = 31.8 DEGREES
REMARK 500 1 DA B 255 C1' - O4' - C4' ANGL. DEV. = 8.4 DEGREES
REMARK 500 1 DA B 255 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DA B 256 O4' - C4' - C3' ANGL. DEV. = -19.2 DEGREES
REMARK 500 1 DA B 256 C5' - C4' - O4' ANGL. DEV. = 47.2 DEGREES
REMARK 500 1 DA B 256 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DT B 257 O4' - C4' - C3' ANGL. DEV. = -6.9 DEGREES
REMARK 500 1 DT B 257 C5' - C4' - O4' ANGL. DEV. = 34.9 DEGREES
REMARK 500 1 DT B 257 C1' - O4' - C4' ANGL. DEV. = 8.0 DEGREES
REMARK 500 1 DT B 257 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DA B 258 O4' - C4' - C3' ANGL. DEV. = -4.5 DEGREES
REMARK 500 1 DA B 258 C5' - C4' - O4' ANGL. DEV. = 14.2 DEGREES
REMARK 500 1 DA B 258 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DA B 259 O4' - C4' - C3' ANGL. DEV. = -5.5 DEGREES
REMARK 500 1 DA B 259 C5' - C4' - O4' ANGL. DEV. = 26.4 DEGREES
REMARK 500 1 DA B 259 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DC B 260 O4' - C4' - C3' ANGL. DEV. = -18.7 DEGREES
REMARK 500 1 DC B 260 C5' - C4' - O4' ANGL. DEV. = 47.0 DEGREES
REMARK 500 1 DC B 260 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DA B 261 O4' - C4' - C3' ANGL. DEV. = -10.1 DEGREES
REMARK 500 1 DA B 261 C5' - C4' - O4' ANGL. DEV. = 30.9 DEGREES
REMARK 500 1 DA B 261 C1' - O4' - C4' ANGL. DEV. = 4.3 DEGREES
REMARK 500 1 DA B 261 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DA B 262 O4' - C4' - C3' ANGL. DEV. = -9.6 DEGREES
REMARK 500 1 DA B 262 C5' - C4' - O4' ANGL. DEV. = 37.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 2702 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 A 3 140.40 69.80
REMARK 500 1 SER A 19 78.62 -115.77
REMARK 500 1 LYS A 22 64.97 67.34
REMARK 500 1 LYS A 23 152.13 179.10
REMARK 500 1 PHE A 44 61.74 36.07
REMARK 500 1 PRO A 45 43.82 -75.03
REMARK 500 1 ALA A 46 66.04 91.43
REMARK 500 1 LEU A 57 80.19 -68.44
REMARK 500 1 ASN A 58 -68.38 160.28
REMARK 500 1 CYS A 60 64.86 68.46
REMARK 500 1 PHE A 61 -163.13 -115.86
REMARK 500 1 ARG A 66 101.18 -41.05
REMARK 500 1 LYS A 73 54.07 -141.27
REMARK 500 1 GLN A 82 -43.35 -130.68
REMARK 500 1 SER A 91 45.76 -149.45
REMARK 500 1 ARG A 94 62.63 -101.79
REMARK 500 1 ARG A 95 -60.79 169.58
REMARK 500 1 LYS A 97 64.79 37.36
REMARK 500 2 LYS A 3 -65.19 -108.73
REMARK 500 2 SER A 7 -100.17 -114.75
REMARK 500 2 GLN A 21 -94.56 -70.11
REMARK 500 2 LYS A 22 68.23 178.79
REMARK 500 2 LYS A 23 143.80 -176.43
REMARK 500 2 PHE A 44 68.95 -176.95
REMARK 500 2 ALA A 46 59.86 171.50
REMARK 500 2 ASN A 58 -41.09 160.37
REMARK 500 2 PHE A 61 -152.10 -127.31
REMARK 500 2 PRO A 65 -169.99 -75.03
REMARK 500 2 ARG A 66 73.34 -61.13
REMARK 500 2 LYS A 73 58.73 -142.76
REMARK 500 2 GLN A 82 40.36 168.39
REMARK 500 2 SER A 91 -60.40 176.94
REMARK 500 2 LEU A 93 90.67 -59.78
REMARK 500 2 ARG A 94 143.16 -179.09
REMARK 500 2 ARG A 96 -59.55 79.29
REMARK 500 3 LYS A 3 -66.94 -139.48
REMARK 500 3 SER A 7 -158.60 -105.54
REMARK 500 3 THR A 13 -36.03 -39.70
REMARK 500 3 SER A 19 77.57 -119.08
REMARK 500 3 GLN A 21 -91.71 -71.42
REMARK 500 3 LYS A 22 73.96 173.25
REMARK 500 3 THR A 25 110.14 179.59
REMARK 500 3 PHE A 44 73.21 43.15
REMARK 500 3 PRO A 45 36.76 -75.01
REMARK 500 3 ASN A 58 -54.24 165.42
REMARK 500 3 CYS A 60 62.98 76.28
REMARK 500 3 PHE A 61 -162.15 -119.22
REMARK 500 3 PRO A 65 -161.77 -74.99
REMARK 500 3 ARG A 66 116.39 -33.58
REMARK 500 3 LYS A 73 55.14 -141.52
REMARK 500
REMARK 500 THIS ENTRY HAS 334 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2HDC A 2 98 UNP Q63245 FOXD3_RAT 2 98
DBREF 2HDC B 249 265 PDB 2HDC 2HDC 249 265
DBREF 2HDC C 349 365 PDB 2HDC 2HDC 349 365
SEQRES 1 B 17 DG DC DT DT DA DA DA DA DT DA DA DC DA
SEQRES 2 B 17 DA DT DA DC
SEQRES 1 C 17 DG DT DA DT DT DG DT DT DA DT DT DT DT
SEQRES 2 C 17 DA DA DG DC
SEQRES 1 A 97 VAL LYS PRO PRO TYR SER TYR ILE ALA LEU ILE THR MET
SEQRES 2 A 97 ALA ILE LEU GLN SER PRO GLN LYS LYS LEU THR LEU SER
SEQRES 3 A 97 GLY ILE CYS GLU PHE ILE SER ASN ARG PHE PRO TYR TYR
SEQRES 4 A 97 ARG GLU LYS PHE PRO ALA TRP GLN ASN SER ILE ARG HIS
SEQRES 5 A 97 ASN LEU SER LEU ASN ASP CYS PHE VAL LYS ILE PRO ARG
SEQRES 6 A 97 GLU PRO GLY ASN PRO GLY LYS GLY ASN TYR TRP THR LEU
SEQRES 7 A 97 ASP PRO GLN SER GLU ASP MET PHE ASP ASN GLY SER PHE
SEQRES 8 A 97 LEU ARG ARG ARG LYS ARG
HELIX 1 1 SER A 7 GLN A 18 1 12
HELIX 2 2 THR A 25 PHE A 37 1 13
HELIX 3 3 PHE A 37 PHE A 44 1 8
HELIX 4 4 ALA A 46 CYS A 60 1 15
HELIX 5 5 GLN A 82 GLY A 90 1 9
SHEET 1 A 2 VAL A 62 ILE A 64 0
SHEET 2 A 2 TYR A 76 THR A 78 -1 O TYR A 76 N ILE A 64
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 - r 9 2 Bytes