Header list of 2ff0.pdb file
Complete list - r 9 2 Bytes
HEADER HORMONE/GROWTH FACTOR/DNA 17-DEC-05 2FF0 TITLE SOLUTION STRUCTURE OF STEROIDOGENIC FACTOR 1 DNA BINDING DOMAIN BOUND TITLE 2 TO ITS TARGET SEQUENCE IN THE INHIBIN ALPHA-SUBUNIT PROMOTER COMPND MOL_ID: 1; COMPND 2 MOLECULE: GGCTCAGGGCCACAG; COMPND 3 CHAIN: B; COMPND 4 FRAGMENT: INHIBIN ALPHA-SUBUNIT PROMOTER; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: CTGTGGCCCTGAGCC; COMPND 8 CHAIN: C; COMPND 9 FRAGMENT: INHIBIN ALPHA-SUBUNIT PROMOTER; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: STEROIDOGENIC FACTOR 1; COMPND 13 CHAIN: A; COMPND 14 FRAGMENT: DNA BINDING DOMAIN; COMPND 15 SYNONYM: STF-1, SF-1, ADRENAL 4 BINDING PROTEIN, STEROID HORMONE COMPND 16 RECEPTOR AD4BP, FUSHI TARAZU FACTOR HOMOLOG 1, EMBRYONAL LTR BINDING COMPND 17 PROTEIN, ELP, EMBRYONAL LONG TERMINAL REPEAT- BINDING PROTEIN, COMPND 18 STEROID HYDROXYLASE POSITIVE REGULATOR; COMPND 19 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THE DNA SEQUENCE WAS SYNTHESIZED VIA AUTOMATED SOURCE 4 METHODS; SOURCE 5 MOL_ID: 2; SOURCE 6 SYNTHETIC: YES; SOURCE 7 OTHER_DETAILS: THE DNA SEQUENCE WAS SYNTHESIZED VIA AUTOMATED SOURCE 8 METHODS; SOURCE 9 MOL_ID: 3; SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 11 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 12 ORGANISM_TAXID: 10090; SOURCE 13 GENE: NR5A1, FTZF1; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PMCSG7 KEYWDS NUCLEAR HORMONE RECEPTOR, PROTEIN-DNA COMPLEX, MONOMERIC RECEPTOR-DNA KEYWDS 2 COMPLEX, HORMONE-GROWTH FACTOR-DNA COMPLEX EXPDTA SOLUTION NMR NUMMDL 16 AUTHOR T.H.LITTLE,Y.ZHANG,C.K.MATULIS,J.WECK,Z.ZHANG,A.RAMACHANDRAN, AUTHOR 2 K.E.MAYO,I.RADHAKRISHNAN REVDAT 3 09-MAR-22 2FF0 1 REMARK LINK REVDAT 2 24-FEB-09 2FF0 1 VERSN REVDAT 1 11-APR-06 2FF0 0 JRNL AUTH T.H.LITTLE,Y.ZHANG,C.K.MATULIS,J.WECK,Z.ZHANG, JRNL AUTH 2 A.RAMACHANDRAN,K.E.MAYO,I.RADHAKRISHNAN JRNL TITL SEQUENCE-SPECIFIC DEOXYRIBONUCLEIC ACID (DNA) RECOGNITION BY JRNL TITL 2 STEROIDOGENIC FACTOR 1: A HELIX AT THE CARBOXY TERMINUS OF JRNL TITL 3 THE DNA BINDING DOMAIN IS NECESSARY FOR COMPLEX STABILITY. JRNL REF MOL.ENDOCRINOL. V. 20 831 2006 JRNL REFN ISSN 0888-8809 JRNL PMID 16339274 JRNL DOI 10.1210/ME.2005-0384 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : FELIX 98.0, ARIA 1.2, CNS 1.1 REMARK 3 AUTHORS : ACCELRYS INC (FELIX), NILGES ET AL. (ARIA), REMARK 3 BRUNGER ET AL. (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2FF0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-DEC-05. REMARK 100 THE DEPOSITION ID IS D_1000035799. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 20 MM TRIS ACETATE, 50 UM ZNCL2, REMARK 210 2 MM DTT, 1% GLYCEROL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : U-15N-STEROIDOGENIC FACTOR 1 REMARK 210 DBD:NA-DUPLEX DNA COMPLEX; U-15N, REMARK 210 U-13C-STEROIDOGENIC FACTOR 1 DBD: REMARK 210 NA-DUPLEX DNA COMPLEX; U-15N,U- REMARK 210 13C-STEROIDOGENIC FACTOR 1 DBD: REMARK 210 NA-DUPLEX DNA COMPLEX REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; REMARK 210 3D_ALIPHATIC_13C-SEPARATED_NOESY; 3D_AROMATIC_13C-SEPARATED_ REMARK 210 NOESY; 2D_15N,13C-DOUBLE-HALF-FILTERED_NOESY; 3D_13C-FILTERED_ REMARK 210 13C-EDITED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : VNMR 6.1 REMARK 210 METHOD USED : SIMULATED ANNEALING AND REMARK 210 CARTESIAN MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST RESTRAINT ENERGIES, REMARK 210 RESTRAINT VIOLATIONS, AND RMS REMARK 210 DEVIATIONS FROM IDEAL COVALENT REMARK 210 GEOMETRY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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 HG CYS A 65 ZN ZN A 1002 1.09 REMARK 500 HG CYS A 33 ZN ZN A 1001 1.14 REMARK 500 H1' DC B 3 H5' DT B 4 1.14 REMARK 500 H1' DG C 20 H5' DG C 21 1.31 REMARK 500 H2'' DG B 1 H8 DG B 2 1.33 REMARK 500 HG CYS A 68 ZN ZN A 1002 1.46 REMARK 500 OE1 GLU A 31 HZ2 LYS A 34 1.57 REMARK 500 HG CYS A 16 OD2 ASP A 18 1.59 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 VAL A 15 -81.88 -104.03 REMARK 500 1 SER A 52 86.91 46.81 REMARK 500 1 ASP A 86 -76.47 -55.28 REMARK 500 1 ARG A 87 -34.53 165.82 REMARK 500 2 TYR A 25 -71.60 73.03 REMARK 500 2 GLU A 51 -91.62 59.71 REMARK 500 2 GLN A 53 -28.23 69.86 REMARK 500 2 SER A 54 43.19 -105.32 REMARK 500 2 ARG A 87 -16.08 81.89 REMARK 500 3 GLU A 51 -149.18 -102.06 REMARK 500 3 GLN A 53 -45.80 71.02 REMARK 500 3 ASP A 58 -163.64 -120.93 REMARK 500 3 ASP A 86 -80.42 -65.56 REMARK 500 3 ARG A 87 113.08 -179.67 REMARK 500 3 ASN A 93 -138.59 -110.77 REMARK 500 4 VAL A 15 -69.88 -100.77 REMARK 500 4 TYR A 23 -151.61 57.06 REMARK 500 4 HIS A 24 -29.48 127.06 REMARK 500 4 TYR A 25 -151.69 -138.62 REMARK 500 4 LEU A 27 -178.35 176.55 REMARK 500 4 GLU A 51 -93.08 -91.51 REMARK 500 4 GLN A 53 -38.42 72.32 REMARK 500 4 SER A 54 72.45 -101.85 REMARK 500 4 ARG A 64 -62.63 -90.94 REMARK 500 4 ASP A 86 -73.35 -74.85 REMARK 500 4 ARG A 87 -91.55 -179.75 REMARK 500 4 MET A 88 86.70 45.82 REMARK 500 4 ASN A 93 -70.53 -164.14 REMARK 500 4 GLN A 107 -68.73 -101.33 REMARK 500 4 GLN A 108 -177.39 58.28 REMARK 500 5 TYR A 25 -82.96 65.74 REMARK 500 5 THR A 50 -76.27 65.36 REMARK 500 5 SER A 52 72.39 47.46 REMARK 500 5 SER A 54 79.59 -113.89 REMARK 500 5 ASN A 93 -73.87 -135.57 REMARK 500 6 THR A 50 -43.85 72.29 REMARK 500 6 SER A 52 -27.90 -163.06 REMARK 500 6 GLN A 53 -47.59 77.64 REMARK 500 6 ILE A 57 99.68 -64.13 REMARK 500 6 ASP A 58 -161.71 -125.73 REMARK 500 6 VAL A 83 109.34 -57.13 REMARK 500 6 ASN A 93 -38.57 -157.10 REMARK 500 6 GLN A 108 -72.65 -62.74 REMARK 500 6 LYS A 109 117.76 -174.34 REMARK 500 7 PRO A 14 11.87 -68.90 REMARK 500 7 THR A 50 173.51 53.86 REMARK 500 7 GLU A 51 -59.57 65.70 REMARK 500 7 ARG A 87 85.47 66.44 REMARK 500 7 ASN A 93 -62.42 -120.08 REMARK 500 7 LYS A 109 -0.28 67.08 REMARK 500 REMARK 500 THIS ENTRY HAS 127 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A1001 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 13 SG REMARK 620 2 CYS A 16 SG 116.2 REMARK 620 3 CYS A 30 SG 102.9 109.8 REMARK 620 4 CYS A 33 SG 115.5 99.0 113.9 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A1002 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 49 SG REMARK 620 2 CYS A 55 SG 110.9 REMARK 620 3 CYS A 65 SG 111.5 111.9 REMARK 620 4 CYS A 68 SG 106.9 101.5 113.7 REMARK 620 N 1 2 3 REMARK 650 REMARK 650 HELIX REMARK 650 AUTHOR DETERMINED HELIX RECORDS BASED ON PROCHECK REMARK 650 OUTPUT OF ENTIRE NMR ENSEMBLE REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1001 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1002 DBREF 2FF0 A 10 111 UNP P33242 STF1_MOUSE 10 111 DBREF 2FF0 B 1 15 PDB 2FF0 2FF0 1 15 DBREF 2FF0 C 16 30 PDB 2FF0 2FF0 16 30 SEQRES 1 B 15 DG DG DC DT DC DA DG DG DG DC DC DA DC SEQRES 2 B 15 DA DG SEQRES 1 C 15 DC DT DG DT DG DG DC DC DC DT DG DA DG SEQRES 2 C 15 DC DC SEQRES 1 A 102 ASP GLU LEU CYS PRO VAL CYS GLY ASP LYS VAL SER GLY SEQRES 2 A 102 TYR HIS TYR GLY LEU LEU THR CYS GLU SER CYS LYS GLY SEQRES 3 A 102 PHE PHE LYS ARG THR VAL GLN ASN ASN LYS HIS TYR THR SEQRES 4 A 102 CYS THR GLU SER GLN SER CYS LYS ILE ASP LYS THR GLN SEQRES 5 A 102 ARG LYS ARG CYS PRO PHE CYS ARG PHE GLN LYS CYS LEU SEQRES 6 A 102 THR VAL GLY MET ARG LEU GLU ALA VAL ARG ALA ASP ARG SEQRES 7 A 102 MET ARG GLY GLY ARG ASN LYS PHE GLY PRO MET TYR LYS SEQRES 8 A 102 ARG ASP ARG ALA LEU LYS GLN GLN LYS LYS ALA HET ZN A1001 1 HET ZN A1002 1 HETNAM ZN ZINC ION FORMUL 4 ZN 2(ZN 2+) HELIX 1 1 GLU A 31 GLN A 42 1 12 HELIX 2 2 PRO A 66 VAL A 76 1 11 HELIX 3 3 LEU A 80 ALA A 82 5 3 HELIX 4 4 GLY A 96 GLN A 107 1 12 SHEET 1 A 2 GLY A 22 HIS A 24 0 SHEET 2 A 2 LEU A 27 THR A 29 -1 O LEU A 27 N HIS A 24 LINK SG CYS A 13 ZN ZN A1001 1555 1555 2.18 LINK SG CYS A 16 ZN ZN A1001 1555 1555 2.19 LINK SG CYS A 30 ZN ZN A1001 1555 1555 2.19 LINK SG CYS A 33 ZN ZN A1001 1555 1555 2.18 LINK SG CYS A 49 ZN ZN A1002 1555 1555 2.23 LINK SG CYS A 55 ZN ZN A1002 1555 1555 2.23 LINK SG CYS A 65 ZN ZN A1002 1555 1555 2.22 LINK SG CYS A 68 ZN ZN A1002 1555 1555 2.24 SITE 1 AC1 4 CYS A 13 CYS A 16 CYS A 30 CYS A 33 SITE 1 AC2 5 CYS A 49 SER A 52 CYS A 55 CYS A 65 SITE 2 AC2 5 CYS A 68 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