Header list of 1gau.pdb file
Complete list - p 12 2 Bytes
HEADER TRANSCRIPTION/DNA 28-JUN-93 1GAU TITLE SOLUTION STRUCTURE OF THE SPECIFIC DNA COMPLEX OF THE ZINC TITLE 2 CONTAINING DNA BINDING DOMAIN OF THE ERYTHROID TITLE 3 TRANSCRIPTION FACTOR GATA-1 BY MULTIDIMENSIONAL NMR COMPND MOL_ID: 1; COMPND 2 MOLECULE: DNA (5'-D(P*AP*GP*AP*TP*AP*AP*AP*C)-3'); COMPND 3 CHAIN: B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: DNA (5'-D(P*GP*TP*TP*TP*AP*TP*CP*T)-3'); COMPND 7 CHAIN: C; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ERYTHROID TRANSCRIPTION FACTOR GATA-1; COMPND 11 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: GALLUS GALLUS; SOURCE 7 ORGANISM_COMMON: CHICKEN; SOURCE 8 ORGANISM_TAXID: 9031 KEYWDS TRANSCRIPTION/DNA EXPDTA SOLUTION NMR NUMMDL 30 AUTHOR G.M.CLORE,J.G.OMICHINSKI,A.M.GRONENBORN REVDAT 2 24-FEB-09 1GAU 1 VERSN REVDAT 1 31-OCT-93 1GAU 0 JRNL AUTH J.G.OMICHINSKI,G.M.CLORE,M.ROBIEN,K.SAKAGUCHI, JRNL AUTH 2 E.APPELLA,A.M.GRONENBORN JRNL TITL HIGH-RESOLUTION SOLUTION STRUCTURE OF THE DOUBLE JRNL TITL 2 CYS2HIS2 ZINC FINGER FROM THE HUMAN ENHANCER JRNL TITL 3 BINDING PROTEIN MBP-1. JRNL REF BIOCHEMISTRY V. 31 3907 1992 JRNL REFN ISSN 0006-2960 JRNL PMID 1567844 JRNL DOI 10.1021/BI00131A004 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NULL REMARK 3 AUTHORS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 DETAILS OF THE STRUCTURE DETERMINATION AND ALL STRUCTURAL REMARK 3 STATISTICS ARE GIVEN IN THE REFERENCE CITED ON THE *JRNL* REMARK 3 RECORDS ABOVE (I.E. AGREEMENT WITH EXPERIMENTAL RESTRAINTS, REMARK 3 DEVIATIONS FROM IDEALITY FOR BOND LENGTHS, ANGLES, PLANES REMARK 3 AND CHIRALITY, NON-BONDED CONTACTS, ATOMIC RMS DIFFERENCES REMARK 3 BETWEEN THE CALCULATED STRUCTURES). THE STRUCTURES ARE REMARK 3 BASED ON A TOTAL OF 1740 EXPERIMENTAL NMR RESTRAINTS REMARK 3 COMPRISING: 1444 INTERPROTON DISTANCE RESTRAINTS DERIVED REMARK 3 FROM NOE MEASUREMENTS; AND 296 TORSION ANGLE RESTRAINTS. REMARK 3 THE NOE RESTRAINTS ARE SUBDIVIDED AS FOLLOWS: (A) WITHIN REMARK 3 THE PROTEIN: 242 INTERRESIDUE SEQUENTIAL (|I-J|=1); 161 REMARK 3 INTERRESIDUE SHORT RANGE (1(LESS THAN)|I-J|(LESS THAN)=5); REMARK 3 182 INTERRESIDUE LONG RANGE (|I-J|(GREATER THAN)5); AND REMARK 3 334 INTRARESIDUE. (B) WITHIN THE DNA: 157 INTRARESIDUE; REMARK 3 180 SEQUENTIAL INTRASTRAND; 34 INTERSTRAND; AND 37 REMARK 3 H-BONDS (C) BETWEEN PROTEIN AND DNA: 117. THE TORSION REMARK 3 ANGLE RESTRAINTS ARE SUBDIVIDED AS FOLLOWS: 144 ANGLES REMARK 3 FOR THE PROTEIN (58 PHI, 56 PSI, 26 CHI1 AND 4 CHI2) AND REMARK 3 152 FOR THE DNA. THE TORSION ANGLE RESTRAINTS FOR THE REMARK 3 DNA COMPRISE LOOSE RESTRAINTS ON THE BACKBONE TORSION REMARK 3 ANGLES ALPHA, BETA, GAMMA, EPSILON AND ZETA TO PREVENT REMARK 3 PROBLEMS ASSOCIATED WITH LOCAL MIRROR IMAGES. REMARK 3 REMARK 3 THE METHOD USED TO DETERMINE THE STRUCTURES IS THE HYBRID REMARK 3 METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED REMARK 3 ANNEALING METHOD [M.NILGES, G.M.CLORE, AND A.M.GRONENBORN REMARK 3 FEBS LETT. 229, 317-324 (1988)]. REMARK 3 REMARK 3 A TOTAL OF 30 STRUCTURES WERE CALCULATED. THE ATOMIC RMS REMARK 3 DISTRIBUTION ABOUT THE MEAN COORDINATE POSITIONS FOR REMARK 3 RESIDUES 2 - 59 OF THE PROTEIN AND BASE PAIRS 6 - 13 OF THE REMARK 3 DNA IS 0.70 (+/-0.13) A FOR THE BACKBONE ATOMS OF THE REMARK 3 PROTEIN AND ALL ATOMS OF THE DNA, AND 1.13 (+/-0.08) A FOR REMARK 3 ALL ATOMS OF THE PROTEIN AND DNA. THE N-TERMINUS REMARK 3 (RESIDUE 1) AND C-TERMINUS (RESIDUES 60 - 66) ARE REMARK 3 DISORDERED. THE ORIENTATION OF THE FIRST 5 AND LAST 3 BASE REMARK 3 PAIRS OF THE 16MER DNA DUPLEX, WHICH ARE NOT IN CONTACT REMARK 3 WITH THE DNA, IS POORLY DEFINED WITH RESPECT TO THE CORE OF REMARK 3 THE COMPLEX. CONSEQUENTLY, ONLY THE COORDINATES OF THE REMARK 3 COMPLEX PROPER HAVE BEEN DEPOSITED: I.E. RESIDUES 1 - 60 REMARK 3 OF THE PROTEIN AND BASE PAIRS 6 - 13 OF THE DNA. REMARK 3 THE COORDINATES OF THE 30 INDIVIDUAL SA STRUCTURES ARE REMARK 3 PRESENTED AS MODELS 1 TO 30. THE QUANTITY IN COLUMNS 61 - REMARK 3 OF THESE MODELS HAS NO MEANING. REMARK 3 REMARK 3 THE COORDINATES OF THE RESTRAINED MINIMIZED STRUCTURE REMARK 3 ARE PRESENTED IN PROTEIN DATA BANK ENTRY 1GAT. THE (SA)R REMARK 3 RESTRAINED MINIMIZED MEAN STRUCTURE WAS DERIVED BY REMARK 3 AVERAGING THE COORDINATES OF THE INDIVIDUAL SA STRUCTURES REMARK 3 (BEST FITTED TO RESIDUES 2 - 59 OF THE PROTEIN AND BASE REMARK 3 PAIRS 6 - 13 OF THE DNA), AND SUBJECTING THE RESULTING REMARK 3 COORDINATES TO RESTRAINED MINIMIZATION. THE QUANTITY REMARK 3 PRESENTED IN COLUMNS 61 - 66 OF MEAN STRUCTURE, PRESENTED REMARK 3 IN PROTEIN DATA BANK ENTRY 1GAT, REPRESENTS THE ATOMIC RMS REMARK 3 DEVIATIONS OF THE 30 INDIVIDUAL SA STRUCTURES ABOUT THE REMARK 3 MEAN STRUCTURE. REMARK 4 REMARK 4 1GAU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL 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 : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30 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 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 16 DA B 106 C8 DA B 106 N9 -0.049 REMARK 500 18 DA B 106 C8 DA B 106 N9 -0.050 REMARK 500 24 DA B 106 C8 DA B 106 N9 -0.049 REMARK 500 26 DA C 124 C8 DA C 124 N9 -0.048 REMARK 500 28 DA C 124 C8 DA C 124 N9 -0.048 REMARK 500 29 DA B 106 C8 DA B 106 N9 -0.049 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 DA B 106 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES REMARK 500 1 DA B 106 C5 - N7 - C8 ANGL. DEV. = -4.0 DEGREES REMARK 500 1 DA B 106 N7 - C8 - N9 ANGL. DEV. = 6.6 DEGREES REMARK 500 1 DA B 106 C8 - N9 - C4 ANGL. DEV. = -3.1 DEGREES REMARK 500 1 DG B 107 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES REMARK 500 1 DG B 107 C5 - N7 - C8 ANGL. DEV. = -4.0 DEGREES REMARK 500 1 DG B 107 N7 - C8 - N9 ANGL. DEV. = 7.0 DEGREES REMARK 500 1 DG B 107 C8 - N9 - C4 ANGL. DEV. = -3.9 DEGREES REMARK 500 1 DA B 108 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES REMARK 500 1 DA B 108 C5 - N7 - C8 ANGL. DEV. = -3.8 DEGREES REMARK 500 1 DA B 108 N7 - C8 - N9 ANGL. DEV. = 6.2 DEGREES REMARK 500 1 DA B 108 C8 - N9 - C4 ANGL. DEV. = -3.3 DEGREES REMARK 500 1 DT B 109 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES REMARK 500 1 DA B 110 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES REMARK 500 1 DA B 110 C5 - N7 - C8 ANGL. DEV. = -3.7 DEGREES REMARK 500 1 DA B 110 N7 - C8 - N9 ANGL. DEV. = 6.1 DEGREES REMARK 500 1 DA B 110 C8 - N9 - C4 ANGL. DEV. = -3.5 DEGREES REMARK 500 1 DA B 111 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES REMARK 500 1 DA B 111 C5 - N7 - C8 ANGL. DEV. = -3.8 DEGREES REMARK 500 1 DA B 111 N7 - C8 - N9 ANGL. DEV. = 6.3 DEGREES REMARK 500 1 DA B 111 C8 - N9 - C4 ANGL. DEV. = -3.3 DEGREES REMARK 500 1 DA B 112 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES REMARK 500 1 DA B 112 C5 - N7 - C8 ANGL. DEV. = -3.8 DEGREES REMARK 500 1 DA B 112 N7 - C8 - N9 ANGL. DEV. = 6.0 DEGREES REMARK 500 1 DA B 112 C8 - N9 - C4 ANGL. DEV. = -3.2 DEGREES REMARK 500 1 DC B 113 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES REMARK 500 1 DG C 120 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES REMARK 500 1 DG C 120 C5 - N7 - C8 ANGL. DEV. = -3.9 DEGREES REMARK 500 1 DG C 120 N7 - C8 - N9 ANGL. DEV. = 7.2 DEGREES REMARK 500 1 DG C 120 C8 - N9 - C4 ANGL. DEV. = -3.9 DEGREES REMARK 500 1 DT C 121 O4' - C1' - N1 ANGL. DEV. = 3.5 DEGREES REMARK 500 1 DT C 121 C6 - C5 - C7 ANGL. DEV. = -3.8 DEGREES REMARK 500 1 DT C 122 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES REMARK 500 1 DT C 123 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES REMARK 500 1 DA C 124 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES REMARK 500 1 DA C 124 C5 - N7 - C8 ANGL. DEV. = -4.0 DEGREES REMARK 500 1 DA C 124 N7 - C8 - N9 ANGL. DEV. = 6.7 DEGREES REMARK 500 1 DA C 124 C8 - N9 - C4 ANGL. DEV. = -3.1 DEGREES REMARK 500 1 DT C 125 O4' - C1' - N1 ANGL. DEV. = 3.6 DEGREES REMARK 500 1 DC C 126 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES REMARK 500 1 DT C 127 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES REMARK 500 2 DA B 106 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES REMARK 500 2 DA B 106 C5 - N7 - C8 ANGL. DEV. = -4.0 DEGREES REMARK 500 2 DA B 106 N7 - C8 - N9 ANGL. DEV. = 6.5 DEGREES REMARK 500 2 DA B 106 C8 - N9 - C4 ANGL. DEV. = -3.0 DEGREES REMARK 500 2 DG B 107 O4' - C1' - N9 ANGL. DEV. = 3.3 DEGREES REMARK 500 2 DG B 107 C5 - N7 - C8 ANGL. DEV. = -3.9 DEGREES REMARK 500 2 DG B 107 N7 - C8 - N9 ANGL. DEV. = 7.0 DEGREES REMARK 500 2 DG B 107 C8 - N9 - C4 ANGL. DEV. = -4.0 DEGREES REMARK 500 2 DA B 108 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 1220 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 THR A 5 91.69 -63.50 REMARK 500 1 CYS A 10 20.63 -145.41 REMARK 500 1 GLN A 11 20.31 45.05 REMARK 500 1 ASN A 41 -173.81 -62.93 REMARK 500 1 ASN A 55 93.93 -61.40 REMARK 500 1 ARG A 56 150.19 -48.36 REMARK 500 2 CYS A 7 108.05 -47.99 REMARK 500 2 CYS A 10 23.81 -143.25 REMARK 500 2 GLN A 11 22.56 44.61 REMARK 500 2 LEU A 44 41.63 -84.49 REMARK 500 2 ASN A 55 91.83 -62.74 REMARK 500 2 SER A 59 108.72 -53.59 REMARK 500 3 ARG A 2 59.57 -98.06 REMARK 500 3 CYS A 7 107.31 -51.10 REMARK 500 3 CYS A 10 23.02 -142.72 REMARK 500 3 LEU A 44 0.92 -68.60 REMARK 500 4 THR A 5 92.60 -66.56 REMARK 500 4 CYS A 10 18.39 -142.69 REMARK 500 4 GLN A 11 21.34 46.83 REMARK 500 4 PRO A 26 91.96 -64.98 REMARK 500 4 ARG A 54 -154.85 -153.38 REMARK 500 4 ASN A 55 87.05 -62.98 REMARK 500 5 CYS A 10 26.06 -141.51 REMARK 500 5 GLN A 11 20.93 41.82 REMARK 500 5 PRO A 26 91.40 -65.05 REMARK 500 5 GLN A 39 29.07 46.65 REMARK 500 5 LYS A 48 -169.90 -122.41 REMARK 500 5 ASP A 49 -82.33 -47.72 REMARK 500 5 ARG A 54 -157.42 -150.87 REMARK 500 6 THR A 5 93.46 -58.31 REMARK 500 6 CYS A 10 24.31 -154.01 REMARK 500 6 GLN A 11 34.41 33.73 REMARK 500 6 PRO A 26 95.63 -63.47 REMARK 500 6 GLN A 39 26.73 81.87 REMARK 500 6 LYS A 48 -156.25 -106.84 REMARK 500 6 ASP A 49 -73.91 -66.03 REMARK 500 6 ASN A 55 100.13 -56.17 REMARK 500 7 ARG A 2 43.05 -100.50 REMARK 500 7 CYS A 10 25.83 -144.70 REMARK 500 7 GLN A 11 25.60 38.96 REMARK 500 7 ARG A 19 74.47 -116.34 REMARK 500 7 PRO A 26 99.70 -60.70 REMARK 500 7 LEU A 44 40.52 -83.14 REMARK 500 7 ASN A 55 103.63 -54.13 REMARK 500 8 THR A 5 92.16 -60.13 REMARK 500 8 CYS A 10 25.79 -143.16 REMARK 500 8 GLN A 11 35.54 37.15 REMARK 500 8 LEU A 44 37.71 -95.46 REMARK 500 8 ASP A 49 -77.59 -49.67 REMARK 500 9 THR A 5 89.08 -66.53 REMARK 500 9 GLN A 11 25.51 46.82 REMARK 500 9 TRP A 18 103.14 -53.32 REMARK 500 9 ASN A 41 -176.02 -60.81 REMARK 500 9 ARG A 54 -155.67 -152.51 REMARK 500 9 SER A 59 104.38 -54.37 REMARK 500 10 THR A 5 93.97 -66.59 REMARK 500 10 CYS A 10 28.05 -147.90 REMARK 500 10 GLN A 11 40.56 30.69 REMARK 500 10 ARG A 20 99.62 -61.29 REMARK 500 10 PRO A 26 96.44 -68.22 REMARK 500 10 ASP A 49 -80.46 -49.09 REMARK 500 11 THR A 5 91.70 -59.46 REMARK 500 11 CYS A 7 109.50 -48.24 REMARK 500 11 CYS A 10 19.30 -141.03 REMARK 500 11 GLN A 11 25.61 47.50 REMARK 500 11 TRP A 18 99.93 -62.56 REMARK 500 11 ARG A 20 96.14 -63.06 REMARK 500 11 LEU A 44 37.21 -83.93 REMARK 500 11 LYS A 48 -155.42 -131.59 REMARK 500 11 ASP A 49 -84.85 -57.15 REMARK 500 11 SER A 59 100.51 -48.29 REMARK 500 12 GLN A 11 24.93 48.18 REMARK 500 12 TRP A 18 98.62 -59.51 REMARK 500 12 ARG A 20 94.75 -61.08 REMARK 500 12 LEU A 44 29.83 -74.33 REMARK 500 12 ASP A 49 -70.25 -44.43 REMARK 500 12 VAL A 58 122.10 -39.53 REMARK 500 12 SER A 59 103.72 -44.83 REMARK 500 13 GLN A 11 22.13 49.55 REMARK 500 13 ASN A 41 -173.62 -61.69 REMARK 500 13 LYS A 48 -163.99 -119.38 REMARK 500 13 ASP A 49 -89.35 -79.51 REMARK 500 13 ARG A 54 -158.47 -153.16 REMARK 500 13 ASN A 55 106.11 -58.37 REMARK 500 14 THR A 5 96.37 -60.61 REMARK 500 14 CYS A 10 26.28 -154.00 REMARK 500 14 GLN A 11 37.11 31.15 REMARK 500 14 TRP A 18 98.92 -64.96 REMARK 500 14 ARG A 20 95.59 -64.20 REMARK 500 14 PRO A 26 87.59 -66.13 REMARK 500 14 LYS A 48 -166.07 -124.84 REMARK 500 15 GLN A 11 37.57 30.53 REMARK 500 15 TRP A 18 109.27 -54.54 REMARK 500 15 PRO A 26 93.27 -66.63 REMARK 500 15 ASN A 41 -173.20 -66.72 REMARK 500 15 ARG A 54 -157.65 -150.57 REMARK 500 15 ASN A 55 97.18 -62.74 REMARK 500 16 THR A 5 87.84 -69.19 REMARK 500 16 CYS A 7 109.44 -47.44 REMARK 500 16 CYS A 10 17.22 -142.37 REMARK 500 16 GLN A 11 18.65 53.43 REMARK 500 16 GLN A 39 28.35 47.42 REMARK 500 16 ASN A 41 -177.27 -62.47 REMARK 500 16 LYS A 48 -160.52 -106.94 REMARK 500 16 ASP A 49 -73.20 -47.67 REMARK 500 17 THR A 5 99.87 -66.90 REMARK 500 17 CYS A 7 106.88 -40.72 REMARK 500 17 TRP A 18 102.67 -54.70 REMARK 500 17 LEU A 33 -70.10 -76.91 REMARK 500 17 GLN A 39 43.88 36.86 REMARK 500 18 ARG A 2 90.81 -49.95 REMARK 500 18 ALA A 3 90.98 -64.21 REMARK 500 18 THR A 5 94.54 -55.45 REMARK 500 18 CYS A 7 109.44 -44.18 REMARK 500 18 CYS A 10 24.84 -141.86 REMARK 500 18 GLN A 11 26.95 40.36 REMARK 500 18 TRP A 18 94.83 -59.27 REMARK 500 18 GLN A 39 46.09 72.87 REMARK 500 18 LEU A 44 48.01 -78.89 REMARK 500 18 ASP A 49 -74.01 -78.53 REMARK 500 18 ASN A 55 93.05 -63.49 REMARK 500 19 ARG A 2 46.11 -99.27 REMARK 500 19 THR A 5 93.77 -64.68 REMARK 500 19 CYS A 10 19.82 -140.23 REMARK 500 19 GLN A 11 34.81 39.24 REMARK 500 19 ARG A 20 92.42 -63.52 REMARK 500 19 PRO A 26 95.20 -64.35 REMARK 500 19 GLN A 39 27.50 87.40 REMARK 500 19 ASN A 41 175.64 -58.17 REMARK 500 19 ILE A 51 107.77 -46.35 REMARK 500 19 ARG A 54 -152.37 -150.46 REMARK 500 19 LYS A 57 106.90 -50.11 REMARK 500 20 ARG A 2 59.82 -90.21 REMARK 500 20 GLN A 11 23.90 43.04 REMARK 500 20 LEU A 37 -71.14 -66.57 REMARK 500 20 GLN A 39 52.43 73.30 REMARK 500 20 LEU A 44 30.77 -84.67 REMARK 500 20 ASN A 55 89.74 -65.57 REMARK 500 21 THR A 5 89.36 -62.81 REMARK 500 21 CYS A 10 24.87 -141.82 REMARK 500 21 GLN A 11 27.61 42.67 REMARK 500 21 TRP A 18 106.72 -57.44 REMARK 500 21 ASN A 29 -38.50 -39.63 REMARK 500 21 GLN A 39 31.75 77.22 REMARK 500 21 LYS A 48 -156.86 -125.39 REMARK 500 22 ARG A 2 43.77 -91.34 REMARK 500 22 CYS A 10 23.34 -140.63 REMARK 500 22 GLN A 11 29.45 38.75 REMARK 500 22 ARG A 20 95.30 -61.19 REMARK 500 22 LYS A 48 -149.56 -99.16 REMARK 500 22 ASP A 49 -81.90 -50.63 REMARK 500 22 ARG A 54 -153.63 -150.77 REMARK 500 22 SER A 59 109.20 -57.16 REMARK 500 23 THR A 5 90.75 -62.77 REMARK 500 23 CYS A 10 17.40 -140.46 REMARK 500 23 ASN A 55 94.46 -62.37 REMARK 500 24 CYS A 10 28.37 -141.26 REMARK 500 24 GLN A 11 30.19 34.22 REMARK 500 24 TRP A 18 88.72 -69.67 REMARK 500 24 PRO A 26 98.56 -64.02 REMARK 500 24 ASN A 29 -37.24 -37.96 REMARK 500 24 ASN A 41 -175.01 -59.10 REMARK 500 24 LYS A 48 -158.61 -133.36 REMARK 500 24 GLN A 52 79.87 -65.66 REMARK 500 24 ARG A 54 -159.11 -150.64 REMARK 500 24 ASN A 55 103.15 -52.56 REMARK 500 25 THR A 5 92.64 -68.40 REMARK 500 25 CYS A 10 23.43 -142.66 REMARK 500 25 GLN A 11 37.50 38.25 REMARK 500 25 PRO A 26 94.51 -66.40 REMARK 500 25 LEU A 37 -71.82 -74.54 REMARK 500 25 ARG A 54 -158.79 -150.92 REMARK 500 25 ASN A 55 98.47 -55.83 REMARK 500 25 VAL A 58 -167.17 -71.51 REMARK 500 26 THR A 5 88.53 -65.45 REMARK 500 26 GLN A 11 26.17 45.81 REMARK 500 26 TRP A 18 86.34 -64.77 REMARK 500 26 ARG A 19 81.39 -69.33 REMARK 500 26 LEU A 44 37.64 -89.73 REMARK 500 27 CYS A 10 26.16 -140.49 REMARK 500 27 GLN A 11 27.88 40.56 REMARK 500 27 TRP A 18 84.22 -63.49 REMARK 500 27 LYS A 48 -166.18 -127.96 REMARK 500 27 ARG A 54 -158.27 -151.67 REMARK 500 28 THR A 5 100.58 -54.40 REMARK 500 28 CYS A 10 17.22 -142.50 REMARK 500 28 GLN A 11 26.30 47.64 REMARK 500 28 PRO A 26 94.91 -66.50 REMARK 500 28 GLN A 39 47.99 73.20 REMARK 500 28 ILE A 51 104.04 -53.47 REMARK 500 28 GLN A 52 96.76 -46.50 REMARK 500 28 ARG A 54 -154.45 -154.17 REMARK 500 29 GLN A 11 21.02 44.59 REMARK 500 29 ASN A 29 -36.64 -38.12 REMARK 500 30 THR A 5 93.36 -69.13 REMARK 500 30 GLN A 11 25.98 38.45 REMARK 500 30 TRP A 18 86.33 -65.39 REMARK 500 30 PRO A 26 99.69 -63.11 REMARK 500 30 GLN A 39 49.00 76.19 REMARK 500 30 ARG A 54 -152.49 -145.64 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1GAT RELATED DB: PDB REMARK 900 MINIMIZED AVERAGE STRUCTURE DBREF 1GAU B 106 113 PDB 1GAU 1GAU 106 113 DBREF 1GAU C 120 127 PDB 1GAU 1GAU 120 127 DBREF 1GAU A 1 60 UNP P17678 GATA1_CHICK 158 217 SEQRES 1 B 8 DA DG DA DT DA DA DA DC SEQRES 1 C 8 DG DT DT DT DA DT DC DT SEQRES 1 A 60 LYS ARG ALA GLY THR VAL CYS SER ASN CYS GLN THR SER SEQRES 2 A 60 THR THR THR LEU TRP ARG ARG SER PRO MET GLY ASP PRO SEQRES 3 A 60 VAL CYS ASN ALA CYS GLY LEU TYR TYR LYS LEU HIS GLN SEQRES 4 A 60 VAL ASN ARG PRO LEU THR MET ARG LYS ASP GLY ILE GLN SEQRES 5 A 60 THR ARG ASN ARG LYS VAL SER SER HELIX 1 1 ASN A 29 GLN A 39 1 11 SHEET 1 A 2 TRP A 18 SER A 21 0 SHEET 2 A 2 ASP A 25 CYS A 28 -1 O ASP A 25 N SER A 21 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 - p 12 2 Bytes