Header list of 2ezg.pdb file
Complete list - r 9 2 Bytes
HEADER DNA BINDING PROTEIN/DNA 04-JUN-97 2EZG
TITLE SOLUTION STRUCTURE OF A COMPLEX OF THE THIRD DNA BINDING DOMAIN OF
TITLE 2 HUMAN HMG-I(Y) BOUND TO DNA DODECAMER CONTAINING THE PRDII SITE OF
TITLE 3 THE INTERFERON-BETA PROMOTER, NMR, 35 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-D(*GP*GP*GP*AP*AP*AP*TP*TP*CP*CP*TP*C)-3');
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA (5'-D(*GP*AP*GP*GP*AP*AP*TP*TP*TP*CP*CP*C)-3');
COMPND 7 CHAIN: C;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: HIGH MOBILITY GROUP PROTEIN HMG-I/HMG-Y;
COMPND 11 CHAIN: A;
COMPND 12 SYNONYM: HIGH MOBILITY GROUP PROTEIN HMG;
COMPND 13 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: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DNA BINDING PROTEIN, MINOR GROOVE DNA BINDING, TRANSCRIPTIONAL CO-
KEYWDS 2 ACTIVATOR, ARCHITECTURAL FACTOR, COMPLEX (DNA-BINDING PROTEIN-DNA),
KEYWDS 3 DNA BINDING PROTEIN-DNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 35
AUTHOR G.M.CLORE,J.R.HUTH,C.BEWLEY,A.M.GRONENBORN
REVDAT 3 09-MAR-22 2EZG 1 REMARK
REVDAT 2 24-FEB-09 2EZG 1 VERSN
REVDAT 1 15-OCT-97 2EZG 0
JRNL AUTH J.R.HUTH,C.A.BEWLEY,M.S.NISSEN,J.N.EVANS,R.REEVES,
JRNL AUTH 2 A.M.GRONENBORN,G.M.CLORE
JRNL TITL THE SOLUTION STRUCTURE OF AN HMG-I(Y)-DNA COMPLEX DEFINES A
JRNL TITL 2 NEW ARCHITECTURAL MINOR GROOVE BINDING MOTIF.
JRNL REF NAT.STRUCT.BIOL. V. 4 657 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9253416
JRNL DOI 10.1038/NSB0897-657
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES WERE CALCULATED USING THE SIMULATED
REMARK 3 ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT.
REMARK 3 229, 129 - 136 USING THE PROGRAM X-PLOR 3.1 (BRUNGER)
REMARK 3 MODIFIED TO INCORPORATE COUPLING CONSTANT (GARRETT ET AL.
REMARK 3 (1984) J. MAGN RESON. SERIES B 104, 99 - 103), CARBON
REMARK 3 CHEMICAL SHIFT (KUSZEWSKI ET AL. (1995) J. MAGN. RESON.
REMARK 3 SERIES B 106, 92 - 96) RESTRAINTS AND A CONFORMATIONAL
REMARK 3 DATABASE
REMARK 3 POTENTIAL (KUSZEWSKI ET AL. (1996) PROTEIN SCI 5, 1067 -
REMARK 3 1080
REMARK 3 AND (1997) J. MAGN. RESON. 125, 171-177)
REMARK 3 THE 3D STRUCTURE OF THE COMPLEX OF THE THIRD DNA BINDING
REMARK 3 DOMAIN OF HMG-I(Y)
REMARK 3 COMPLEXED TO DNA WAS SOLVED BY
REMARK 3 MULTI-DIMENSIONAL HETERONUCLEAR-EDITED AND -FILTERED NMR
REMARK 3 (A) PROTEIN: 31 SEQUENTIAL (|I-J|=1), 2 MEDIUM
REMARK 3 RANGE (1 < |I-J| >=5) AND 22 INTRARESIDUE
REMARK 3 APPROXIMATE INTERPROTON DISTANCE RESTRAINTS; NULL
REMARK 3 17 TORSION ANGLE RESTRAINTS
REMARK 3 6 THREE-BOND HN-HA AND 3 THREE_BOND COCO COUPLING
REMARK 3 CONSTANT RESTRAINTS; 17 (9 CALPHA AND 8 CBETA) 13C
REMARK 3 SHIFT RESTRAINTS.
REMARK 3 (B) DNA: 249 INTRARESIDUE, 119 SEQUENTIAL INTRASTRAND AND
REMARK 3 33 INTERSTRAND INTERPROTON DISTANCE RESTRAINTS; 42
REMARK 3 DISTANCES FOR WATSON-CRICK BASE PAIR HYDROGEN BONDS;
REMARK 3 136 TORSION ANGLE RESTRAINTS
REMARK 3 (C) 34 INTERMOLECULAR INTERPROTON DISTANCE RESTRAINTS
REMARK 3 (D) 4 INTERMOLECULAR DISTANCE RESTRAINTS TO PHOSPHATES
REMARK 3 (E) 28 'REPULSIVE' RESTRAINTS
REMARK 3
REMARK 3 THE STRUCTURES IN THIS ENTRY ARE THE 35 INDIVIDUAL
REMARK 3 SIMULATED ANNEALING STRUCTURES. THE RESTRAINTS REGULARIZED
REMARK 3 MEAN STRUCTURE IS FOUND IN PDB ENTRY 2EZF. THE LAST
REMARK 3 NUMERIC COLUMN IN THE INDIVIDUAL SA STRUCTURES HAS NO
REMARK 3 MEANING.
REMARK 3
REMARK 3 RESIDUES 32 - 41 OF THE PROTEIN CORRESPOND TO RESIDUES 79 -
REMARK 3 88 OF INTACT HMG-I(Y).
REMARK 4
REMARK 4 2EZG 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_1000178058.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 306
REMARK 210 PH : 6.1
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 : 600 MHZ; 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500; AMX600; DMX600; DMX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR MODIFIED MODIFIED
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 35
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 35
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: DATA WERE RECORDED ON A 2:1 COMPLEX OF DNA DODECAMER TO
REMARK 210 HMG-I(Y) 50-91 WHICH CONTAINS THE SECOND AND THIRD DNA
REMARK 210 DNA BINDING DOMAINS. EACH DNA BINDING DOMAIN BINDS TO
REMARK 210 1 MOLECULE OF DNA.
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
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 B 308 C5 DT B 308 C7 0.042
REMARK 500 1 DT C 321 C5 DT C 321 C7 0.039
REMARK 500 2 DT B 311 C5 DT B 311 C7 0.039
REMARK 500 2 DT C 319 C5 DT C 319 C7 0.038
REMARK 500 2 DT C 320 C5 DT C 320 C7 0.037
REMARK 500 3 DT B 311 C5 DT B 311 C7 0.038
REMARK 500 5 DT B 307 C5 DT B 307 C7 0.037
REMARK 500 5 DT C 321 C5 DT C 321 C7 0.040
REMARK 500 6 DT B 311 C5 DT B 311 C7 0.036
REMARK 500 8 DT C 319 C5 DT C 319 C7 0.039
REMARK 500 10 DT C 320 C5 DT C 320 C7 0.036
REMARK 500 11 DT B 308 C5 DT B 308 C7 0.043
REMARK 500 12 DT C 321 C5 DT C 321 C7 0.037
REMARK 500 13 DT B 307 C5 DT B 307 C7 0.037
REMARK 500 15 DT B 307 C5 DT B 307 C7 0.037
REMARK 500 15 DT C 320 C5 DT C 320 C7 0.042
REMARK 500 15 DT C 321 C5 DT C 321 C7 0.043
REMARK 500 16 DT B 307 C5 DT B 307 C7 0.040
REMARK 500 16 DT B 308 C5 DT B 308 C7 0.039
REMARK 500 17 DT B 307 C5 DT B 307 C7 0.039
REMARK 500 17 DT C 320 C5 DT C 320 C7 0.037
REMARK 500 18 DT C 320 C5 DT C 320 C7 0.037
REMARK 500 19 DT B 307 C5 DT B 307 C7 0.040
REMARK 500 19 DT B 311 C5 DT B 311 C7 0.039
REMARK 500 20 DT C 320 C5 DT C 320 C7 0.036
REMARK 500 22 DT B 311 C5 DT B 311 C7 0.037
REMARK 500 22 DT C 321 C5 DT C 321 C7 0.038
REMARK 500 23 DT C 321 C5 DT C 321 C7 0.037
REMARK 500 24 DT C 320 C5 DT C 320 C7 0.039
REMARK 500 25 DT C 319 C5 DT C 319 C7 0.045
REMARK 500 26 DT B 307 C5 DT B 307 C7 0.046
REMARK 500 26 DT C 319 C5 DT C 319 C7 0.037
REMARK 500 27 DT B 308 C5 DT B 308 C7 0.037
REMARK 500 27 DT C 319 C5 DT C 319 C7 0.037
REMARK 500 27 DT C 320 C5 DT C 320 C7 0.037
REMARK 500 28 DT C 320 C5 DT C 320 C7 0.037
REMARK 500 28 DT C 321 C5 DT C 321 C7 0.037
REMARK 500 29 DT B 308 C5 DT B 308 C7 0.038
REMARK 500 29 DT C 320 C5 DT C 320 C7 0.037
REMARK 500 32 DT B 311 C5 DT B 311 C7 0.037
REMARK 500 32 DT C 320 C5 DT C 320 C7 0.038
REMARK 500 33 DT B 311 C5 DT B 311 C7 0.037
REMARK 500 34 DT B 308 C5 DT B 308 C7 0.041
REMARK 500 34 DT C 319 C5 DT C 319 C7 0.037
REMARK 500 35 DT C 319 C5 DT C 319 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 2 DT B 308 C6 - C5 - C7 ANGL. DEV. = -3.6 DEGREES
REMARK 500 2 DT C 319 C6 - C5 - C7 ANGL. DEV. = -4.0 DEGREES
REMARK 500 3 DT C 320 C6 - C5 - C7 ANGL. DEV. = -3.6 DEGREES
REMARK 500 5 DT B 308 C6 - C5 - C7 ANGL. DEV. = -4.0 DEGREES
REMARK 500 5 DT C 319 C6 - C5 - C7 ANGL. DEV. = -3.7 DEGREES
REMARK 500 5 DT C 321 C6 - C5 - C7 ANGL. DEV. = -3.9 DEGREES
REMARK 500 6 DT B 308 C6 - C5 - C7 ANGL. DEV. = -3.7 DEGREES
REMARK 500 6 DT B 311 C6 - C5 - C7 ANGL. DEV. = -3.9 DEGREES
REMARK 500 6 DT C 319 C6 - C5 - C7 ANGL. DEV. = -3.9 DEGREES
REMARK 500 7 DT B 308 C6 - C5 - C7 ANGL. DEV. = -3.8 DEGREES
REMARK 500 7 DT C 320 C4 - C5 - C6 ANGL. DEV. = 3.6 DEGREES
REMARK 500 7 DT C 320 C6 - C5 - C7 ANGL. DEV. = -3.6 DEGREES
REMARK 500 8 DT B 311 C6 - C5 - C7 ANGL. DEV. = -3.7 DEGREES
REMARK 500 9 DT B 308 C6 - C5 - C7 ANGL. DEV. = -3.9 DEGREES
REMARK 500 9 DT B 311 C6 - C5 - C7 ANGL. DEV. = -3.7 DEGREES
REMARK 500 10 DT B 307 C6 - C5 - C7 ANGL. DEV. = -4.1 DEGREES
REMARK 500 10 DT B 308 C6 - C5 - C7 ANGL. DEV. = -3.9 DEGREES
REMARK 500 10 DT C 319 C6 - C5 - C7 ANGL. DEV. = -3.9 DEGREES
REMARK 500 10 DT C 320 C6 - C5 - C7 ANGL. DEV. = -3.7 DEGREES
REMARK 500 11 DT C 319 C4 - C5 - C6 ANGL. DEV. = 3.6 DEGREES
REMARK 500 11 DT C 321 C6 - C5 - C7 ANGL. DEV. = -3.8 DEGREES
REMARK 500 12 DT C 320 C6 - C5 - C7 ANGL. DEV. = -3.8 DEGREES
REMARK 500 14 DT B 311 C6 - C5 - C7 ANGL. DEV. = -4.2 DEGREES
REMARK 500 14 DT C 319 C6 - C5 - C7 ANGL. DEV. = -3.7 DEGREES
REMARK 500 16 DT B 311 C6 - C5 - C7 ANGL. DEV. = -3.9 DEGREES
REMARK 500 16 DT C 320 C6 - C5 - C7 ANGL. DEV. = -3.6 DEGREES
REMARK 500 16 DT C 321 C6 - C5 - C7 ANGL. DEV. = -3.6 DEGREES
REMARK 500 17 DT C 319 C6 - C5 - C7 ANGL. DEV. = -3.6 DEGREES
REMARK 500 18 DT B 308 C6 - C5 - C7 ANGL. DEV. = -3.9 DEGREES
REMARK 500 18 DT B 311 C6 - C5 - C7 ANGL. DEV. = -3.7 DEGREES
REMARK 500 18 DT C 320 C6 - C5 - C7 ANGL. DEV. = -3.9 DEGREES
REMARK 500 19 DT C 319 C4 - C5 - C6 ANGL. DEV. = 3.9 DEGREES
REMARK 500 19 DT C 319 C6 - C5 - C7 ANGL. DEV. = -3.6 DEGREES
REMARK 500 20 DT C 321 C6 - C5 - C7 ANGL. DEV. = -3.7 DEGREES
REMARK 500 21 DT B 311 C6 - C5 - C7 ANGL. DEV. = -3.6 DEGREES
REMARK 500 21 DT C 319 C6 - C5 - C7 ANGL. DEV. = -3.6 DEGREES
REMARK 500 22 DT B 308 C6 - C5 - C7 ANGL. DEV. = -3.7 DEGREES
REMARK 500 24 DT C 319 C6 - C5 - C7 ANGL. DEV. = -3.8 DEGREES
REMARK 500 24 DT C 320 C6 - C5 - C7 ANGL. DEV. = -3.7 DEGREES
REMARK 500 26 DG B 301 O4' - C1' - C2' ANGL. DEV. = 3.0 DEGREES
REMARK 500 26 DT B 311 C6 - C5 - C7 ANGL. DEV. = -4.0 DEGREES
REMARK 500 26 DT C 319 C6 - C5 - C7 ANGL. DEV. = -3.7 DEGREES
REMARK 500 27 DT B 307 C6 - C5 - C7 ANGL. DEV. = -3.8 DEGREES
REMARK 500 27 DT B 311 C6 - C5 - C7 ANGL. DEV. = -3.7 DEGREES
REMARK 500 27 DT C 319 C6 - C5 - C7 ANGL. DEV. = -3.8 DEGREES
REMARK 500 28 DT C 319 C6 - C5 - C7 ANGL. DEV. = -3.8 DEGREES
REMARK 500 29 DG C 313 O4' - C1' - C2' ANGL. DEV. = 3.1 DEGREES
REMARK 500 30 DT B 308 C6 - C5 - C7 ANGL. DEV. = -4.1 DEGREES
REMARK 500 31 DT B 311 C6 - C5 - C7 ANGL. DEV. = -3.7 DEGREES
REMARK 500 32 DT B 307 C6 - C5 - C7 ANGL. DEV. = -3.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 53 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 35 171.66 -46.82
REMARK 500 1 PRO A 39 159.56 -45.40
REMARK 500 3 PRO A 35 158.54 -43.27
REMARK 500 3 PRO A 39 177.88 -46.44
REMARK 500 4 PRO A 39 151.73 -41.24
REMARK 500 5 PRO A 35 -167.69 -47.29
REMARK 500 6 PRO A 39 152.00 -43.57
REMARK 500 7 PRO A 35 -164.35 -76.55
REMARK 500 9 PRO A 35 -175.75 -44.83
REMARK 500 9 PRO A 39 142.31 -39.07
REMARK 500 10 PRO A 35 -176.32 -46.47
REMARK 500 10 PRO A 39 147.55 -38.59
REMARK 500 11 PRO A 39 -178.03 -64.95
REMARK 500 12 PRO A 39 154.63 -38.49
REMARK 500 13 PRO A 39 167.46 -41.36
REMARK 500 14 PRO A 39 158.23 -38.73
REMARK 500 15 PRO A 35 178.05 -43.58
REMARK 500 16 PRO A 39 150.40 -43.47
REMARK 500 17 PRO A 35 -160.92 -64.53
REMARK 500 19 PRO A 35 -171.97 -48.19
REMARK 500 19 PRO A 39 153.50 -39.10
REMARK 500 20 PRO A 35 -159.70 -80.04
REMARK 500 21 PRO A 35 177.19 -46.34
REMARK 500 21 PRO A 39 157.60 -45.53
REMARK 500 22 PRO A 35 -170.50 -49.40
REMARK 500 22 PRO A 39 -163.79 -71.89
REMARK 500 23 PRO A 35 -167.06 -68.67
REMARK 500 23 PRO A 39 146.09 -39.16
REMARK 500 25 PRO A 39 159.65 -42.62
REMARK 500 26 PRO A 35 -162.37 -52.39
REMARK 500 26 PRO A 39 165.13 -41.99
REMARK 500 28 PRO A 35 -169.92 -64.91
REMARK 500 28 PRO A 39 152.59 -42.78
REMARK 500 29 PRO A 35 169.08 -40.77
REMARK 500 29 PRO A 39 155.22 -44.86
REMARK 500 30 PRO A 35 -162.62 -78.10
REMARK 500 30 PRO A 39 155.85 -39.51
REMARK 500 32 PRO A 35 -159.90 -69.50
REMARK 500 34 PRO A 35 -179.61 -47.10
REMARK 500 34 PRO A 39 141.22 -38.92
REMARK 500 35 PRO A 39 146.39 -38.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2EZF RELATED DB: PDB
REMARK 900 MINIMIZED AVERAGE STRUCTURE
DBREF 2EZG A 32 41 UNP P17096 HMGIY_HUMAN 68 77
DBREF 2EZG B 301 312 PDB 2EZG 2EZG 301 312
DBREF 2EZG C 313 324 PDB 2EZG 2EZG 313 324
SEQRES 1 B 12 DG DG DG DA DA DA DT DT DC DC DT DC
SEQRES 1 C 12 DG DA DG DG DA DA DT DT DT DC DC DC
SEQRES 1 A 10 GLY ARG LYS PRO ARG GLY ARG PRO LYS LYS
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