Header list of 2stt.pdb file
Complete list - r 16 2 Bytes
HEADER DNA BINDING PROTEIN/DNA 05-AUG-96 2STT
TITLE SOLUTION NMR STRUCTURE OF THE HUMAN ETS1/DNA COMPLEX, 25 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-
COMPND 3 D(*TP*CP*GP*AP*GP*CP*CP*GP*GP*AP*AP*GP*TP*TP*CP*GP*A)-3');
COMPND 4 CHAIN: B;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DNA (5'-
COMPND 8 D(*TP*CP*GP*AP*AP*CP*TP*TP*CP*CP*GP*GP*CP*TP*CP*GP*A)-3');
COMPND 9 CHAIN: C;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: ETS1;
COMPND 13 CHAIN: A
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: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606
KEYWDS DEOXYRIBONUCLEIC ACID, COMPLEX (DNA-BINDING PROTEIN-DNA), DNA BINDING
KEYWDS 2 PROTEIN-DNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR G.M.CLORE,M.H.WERNER,A.M.GRONENBORN
REVDAT 3 16-MAR-22 2STT 1 REMARK
REVDAT 2 24-FEB-09 2STT 1 VERSN
REVDAT 1 12-MAR-97 2STT 0
SPRSDE 12-MAR-97 2STT 1STT
JRNL AUTH M.H.WERNER,G.M.CLORE,C.L.FISHER,R.J.FISHER,L.TRINH,
JRNL AUTH 2 J.SHILOACH,A.M.GRONENBORN
JRNL TITL CORRECTION OF THE NMR STRUCTURE OF THE ETS1/DNA COMPLEX.
JRNL REF J.BIOMOL.NMR V. 10 317 1997
JRNL REFN ISSN 0925-2738
JRNL PMID 9460239
JRNL DOI 10.1023/A:1018399711996
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE RESTRAINED REGULARIZED MEAN STRUCTURE IS PRESENTED IN
REMARK 3 ENTRY 2STW AND 25 STRUCTURES ARE PRESENTED IN ENTRY 2STT.
REMARK 3 IN 2STW THE LAST COLUMN REPRESENTS THE RMS OF THE 25
REMARK 3 INDIVIDUAL SIMULATED ANNEALING STRUCTURES ABOUT THE MEAN
REMARK 3 COORDINATE POSITIONS. THE LAST COLUMN IN THE INDIVIDUAL SA
REMARK 3 STRUCTURES HAS NO MEANING. BEST FITTING TO GENERATE THE
REMARK 3 AVERAGE STRUCTURE IS WITH RESPECT TO RESIDUES 24 - 105 OF
REMARK 3 THE PROTEIN AND BASE PAIRS 1 - 17 OF THE DNA (RESIDUES 10 -
REMARK 3 24 ARE DISORDERED IN SOLUTION). RESIDUE 10 CORRESPONDS TO
REMARK 3 RESIDUE 320 OF THE NATURAL SEQUENCE. NOTE THE OCCUPANCY
REMARK 3 FIELD HAS NO MEANING.
REMARK 4
REMARK 4 2STT 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_1000178655.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 305.00
REMARK 210 PH : 6.80
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 : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500; AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
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: 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 HH12 ARG A 63 HZ3 LYS A 73 1.33
REMARK 500 OH TYR A 87 H LYS A 94 1.51
REMARK 500 O LEU A 35 HE1 TRP A 46 1.55
REMARK 500 OE1 GLN A 26 H TRP A 28 1.55
REMARK 500 O TYR A 86 H ASP A 88 1.56
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 DT C 25 C5 DT C 25 C7 0.038
REMARK 500 1 DT C 31 C5 DT C 31 C7 0.038
REMARK 500 3 DT B 13 C5 DT B 13 C7 0.036
REMARK 500 3 DT C 25 C5 DT C 25 C7 0.042
REMARK 500 3 DT C 31 C5 DT C 31 C7 0.040
REMARK 500 4 DT C 31 C5 DT C 31 C7 0.037
REMARK 500 5 DT C 24 C5 DT C 24 C7 0.037
REMARK 500 5 DT C 31 C5 DT C 31 C7 0.042
REMARK 500 6 DT B 14 C5 DT B 14 C7 0.037
REMARK 500 7 DT B 14 C5 DT B 14 C7 0.039
REMARK 500 7 DT C 25 C5 DT C 25 C7 0.038
REMARK 500 7 DT C 31 C5 DT C 31 C7 0.037
REMARK 500 8 DT C 24 C5 DT C 24 C7 0.036
REMARK 500 8 DT C 31 C5 DT C 31 C7 0.040
REMARK 500 9 DT B 14 C5 DT B 14 C7 0.039
REMARK 500 10 DT C 25 C5 DT C 25 C7 0.039
REMARK 500 10 DT C 31 C5 DT C 31 C7 0.038
REMARK 500 11 DT B 14 C5 DT B 14 C7 0.036
REMARK 500 11 DT C 31 C5 DT C 31 C7 0.038
REMARK 500 12 DT B 14 C5 DT B 14 C7 0.038
REMARK 500 12 DT C 31 C5 DT C 31 C7 0.043
REMARK 500 13 DT B 14 C5 DT B 14 C7 0.039
REMARK 500 14 DT B 13 C5 DT B 13 C7 0.037
REMARK 500 14 DT C 25 C5 DT C 25 C7 0.038
REMARK 500 14 DT C 31 C5 DT C 31 C7 0.038
REMARK 500 16 DT B 13 C5 DT B 13 C7 0.042
REMARK 500 16 DT C 24 C5 DT C 24 C7 0.036
REMARK 500 16 DT C 25 C5 DT C 25 C7 0.037
REMARK 500 16 DT C 31 C5 DT C 31 C7 0.039
REMARK 500 17 DT B 14 C5 DT B 14 C7 0.037
REMARK 500 17 DT C 25 C5 DT C 25 C7 0.038
REMARK 500 18 DT B 13 C5 DT B 13 C7 0.040
REMARK 500 18 DT B 14 C5 DT B 14 C7 0.037
REMARK 500 18 DT C 18 C5 DT C 18 C7 0.040
REMARK 500 18 DT C 24 C5 DT C 24 C7 0.037
REMARK 500 18 DT C 31 C5 DT C 31 C7 0.041
REMARK 500 20 DT C 31 C5 DT C 31 C7 0.038
REMARK 500 21 DT C 24 C5 DT C 24 C7 0.039
REMARK 500 21 DT C 25 C5 DT C 25 C7 0.036
REMARK 500 21 DT C 31 C5 DT C 31 C7 0.039
REMARK 500 22 DT C 31 C5 DT C 31 C7 0.041
REMARK 500 23 DT B 13 C5 DT B 13 C7 0.036
REMARK 500 23 DT B 14 C5 DT B 14 C7 0.037
REMARK 500 23 DT C 25 C5 DT C 25 C7 0.038
REMARK 500 23 DT C 31 C5 DT C 31 C7 0.036
REMARK 500 25 DT B 13 C5 DT B 13 C7 0.036
REMARK 500 25 DT C 25 C5 DT C 25 C7 0.042
REMARK 500 25 DT C 31 C5 DT C 31 C7 0.040
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 DT B 1 O4' - C1' - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 1 DT B 1 C6 - C5 - C7 ANGL. DEV. = -3.7 DEGREES
REMARK 500 1 DC B 2 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 1 DG B 3 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 1 DA B 4 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 1 DG B 5 O4' - C1' - N9 ANGL. DEV. = 3.5 DEGREES
REMARK 500 1 DC B 6 O4' - C1' - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 1 DC B 7 O4' - C1' - N1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 DG B 8 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 1 DG B 9 O4' - C1' - N9 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 DA B 10 O4' - C1' - N9 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 DA B 11 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 1 DG B 12 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 1 DT B 13 O4' - C1' - N1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 1 DT B 14 O4' - C1' - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 1 DC B 15 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 1 DG B 16 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 1 DA B 17 O4' - C1' - N9 ANGL. DEV. = 3.5 DEGREES
REMARK 500 1 DT C 18 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 1 DC C 19 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 1 DG C 20 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 1 DA C 21 O4' - C1' - N9 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 DA C 22 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 1 DC C 23 O4' - C1' - N1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 DT C 24 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 1 DT C 25 O4' - C1' - N1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 1 DC C 26 O4' - C1' - N1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 DC C 27 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 1 DG C 28 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 1 DG C 29 O4' - C1' - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 DC C 30 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 1 DT C 31 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 1 DC C 32 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 1 DG C 33 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 1 DA C 34 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 2 DT B 1 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 2 DC B 2 O4' - C1' - N1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 2 DG B 3 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 2 DA B 4 O4' - C1' - N9 ANGL. DEV. = 4.1 DEGREES
REMARK 500 2 DG B 5 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 2 DC B 6 O4' - C1' - N1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 2 DC B 7 O4' - C1' - N1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 2 DG B 8 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 2 DG B 9 O4' - C1' - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 DA B 10 O4' - C1' - N9 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 DA B 11 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 2 DG B 12 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 2 DT B 13 O4' - C1' - N1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 DT B 14 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 2 DC B 15 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 849 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 PRO A 12 4.56 -68.08
REMARK 500 1 ALA A 13 -91.79 -71.33
REMARK 500 1 ASP A 49 -112.16 -115.92
REMARK 500 1 LYS A 89 -93.43 -126.05
REMARK 500 1 ASN A 90 92.98 -160.51
REMARK 500 1 ILE A 91 -91.62 -144.92
REMARK 500 2 THR A 20 -112.11 -126.31
REMARK 500 2 SER A 22 40.58 -106.74
REMARK 500 2 ASP A 37 -84.64 -106.53
REMARK 500 2 ASP A 49 -108.49 -107.60
REMARK 500 2 PRO A 72 -86.61 -57.09
REMARK 500 2 TYR A 86 7.03 -69.25
REMARK 500 2 TYR A 87 98.06 -62.11
REMARK 500 2 ASP A 88 -77.62 -87.24
REMARK 500 2 LYS A 89 -66.52 -126.91
REMARK 500 2 ASN A 90 84.92 -154.42
REMARK 500 2 ILE A 91 -100.77 -139.39
REMARK 500 3 PRO A 12 29.47 -60.91
REMARK 500 3 ALA A 13 -169.64 -103.77
REMARK 500 3 THR A 20 -158.12 -94.64
REMARK 500 3 THR A 36 52.45 -108.30
REMARK 500 3 ASP A 37 -80.16 -128.50
REMARK 500 3 LYS A 38 -169.13 -76.93
REMARK 500 3 SER A 39 -131.60 -74.12
REMARK 500 3 CYS A 40 -44.79 -174.62
REMARK 500 3 ASP A 49 -45.19 -138.10
REMARK 500 3 TRP A 51 50.25 -159.47
REMARK 500 3 PRO A 58 57.37 -67.53
REMARK 500 3 ILE A 91 -49.19 -136.03
REMARK 500 3 ALA A 96 6.63 -68.61
REMARK 500 4 THR A 36 70.44 -113.44
REMARK 500 4 ASP A 37 -135.46 -115.31
REMARK 500 4 LYS A 38 -143.12 -59.55
REMARK 500 4 CYS A 40 -19.05 70.43
REMARK 500 4 ASP A 49 -153.48 -122.43
REMARK 500 4 TRP A 51 69.99 -150.66
REMARK 500 4 PRO A 72 -159.05 -52.84
REMARK 500 4 ILE A 91 -46.78 -136.19
REMARK 500 4 ALA A 96 26.83 -75.96
REMARK 500 4 LYS A 98 -133.79 -113.32
REMARK 500 5 ALA A 17 -89.08 -79.83
REMARK 500 5 THR A 47 -158.84 -58.11
REMARK 500 5 TRP A 51 35.44 -155.34
REMARK 500 5 PRO A 58 38.54 -72.17
REMARK 500 5 PRO A 72 -83.66 -60.40
REMARK 500 5 TYR A 87 3.80 -67.22
REMARK 500 5 ILE A 91 -48.19 -136.63
REMARK 500 5 ALA A 96 33.13 -84.11
REMARK 500 5 LYS A 98 -119.81 -111.62
REMARK 500 5 ARG A 99 -39.52 -131.95
REMARK 500
REMARK 500 THIS ENTRY HAS 265 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2STW RELATED DB: PDB
REMARK 900 RESTRAINED REGULARIZED MEAN STRUCTURE
DBREF 2STT A 10 105 UNP P14921 ETS1_HUMAN 320 415
DBREF 2STT B 1 17 PDB 2STT 2STT 1 17
DBREF 2STT C 18 34 PDB 2STT 2STT 18 34
SEQRES 1 B 17 DT DC DG DA DG DC DC DG DG DA DA DG DT
SEQRES 2 B 17 DT DC DG DA
SEQRES 1 C 17 DT DC DG DA DA DC DT DT DC DC DG DG DC
SEQRES 2 C 17 DT DC DG DA
SEQRES 1 A 96 VAL ILE PRO ALA ALA ALA LEU ALA GLY TYR THR GLY SER
SEQRES 2 A 96 GLY PRO ILE GLN LEU TRP GLN PHE LEU LEU GLU LEU LEU
SEQRES 3 A 96 THR ASP LYS SER CYS GLN SER PHE ILE SER TRP THR GLY
SEQRES 4 A 96 ASP GLY TRP GLU PHE LYS LEU SER ASP PRO ASP GLU VAL
SEQRES 5 A 96 ALA ARG ARG TRP GLY LYS ARG LYS ASN LYS PRO LYS MET
SEQRES 6 A 96 ASN TYR GLU LYS LEU SER ARG GLY LEU ARG TYR TYR TYR
SEQRES 7 A 96 ASP LYS ASN ILE ILE HIS LYS THR ALA GLY LYS ARG TYR
SEQRES 8 A 96 VAL TYR ARG PHE VAL
HELIX 1 H1 LEU A 27 THR A 36 1 10
HELIX 2 H2 SER A 39 GLN A 41 5 3
HELIX 3 H3 ASP A 59 LYS A 67 5 9
HELIX 4 H4 TYR A 76 TYR A 85 5 10
SHEET 1 A 2 SER A 45 THR A 47 0
SHEET 2 A 2 GLU A 52 LYS A 54 -1 N LYS A 54 O SER A 45
SHEET 1 B 2 ILE A 92 LYS A 94 0
SHEET 2 B 2 TYR A 102 PHE A 104 -1 N ARG A 103 O HIS A 93
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 16 2 Bytes