Header list of 1njq.pdb file
Complete list - b 23 2 Bytes
HEADER METAL BINDING PROTEIN 02-JAN-03 1NJQ TITLE NMR STRUCTURE OF THE SINGLE QALGGH ZINC FINGER DOMAIN FROM ARABIDOPSIS TITLE 2 THALIANA SUPERMAN PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: SUPERMAN PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SUPERMAN SINGLE QALGGH ZINC-FINGER DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED THROUGH FMOC SOURCE 4 SOLID STATE PEPTIDE SYNTHESIS. THE SEQUENCE OF THE PEPTIDE IS SOURCE 5 NATURALLY FOUND IN ARABIDOPSIS THALIANA. KEYWDS ZINC-FINGER, PEPTIDE-ZINC COMPLEX, BETA-BETA-ALFA MOTIF, METAL KEYWDS 2 BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR C.ISERNIA,E.BUCCI,M.LEONE,L.ZACCARO,P.DI LELLO,G.DIGILIO,S.ESPOSITO, AUTHOR 2 M.SAVIANO,B.DI BLASIO,C.PEDONE,P.V.PEDONE,R.FATTORUSSO REVDAT 4 23-FEB-22 1NJQ 1 REMARK LINK REVDAT 3 24-FEB-09 1NJQ 1 VERSN REVDAT 2 02-SEP-03 1NJQ 1 JRNL REVDAT 1 04-MAR-03 1NJQ 0 JRNL AUTH C.ISERNIA,E.BUCCI,M.LEONE,L.ZACCARO,P.DI LELLO,G.DIGILIO, JRNL AUTH 2 S.ESPOSITO,M.SAVIANO,B.DI BLASIO,C.PEDONE,P.V.PEDONE, JRNL AUTH 3 R.FATTORUSSO JRNL TITL NMR STRUCTURE OF THE SINGLE QALGGH ZINC FINGER DOMAIN FROM JRNL TITL 2 THE ARABIDOPSIS THALIANA SUPERMAN PROTEIN. JRNL REF CHEMBIOCHEM V. 4 171 2003 JRNL REFN ISSN 1439-4227 JRNL PMID 12616630 JRNL DOI 10.1002/CBIC.200390028 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1B, OPAL 2.2 REMARK 3 AUTHORS : VARIAN TEAM (VNMR), GUENTERT, P. (OPAL) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: TORSION ANGLE DYNAMICS STRUCTURE REMARK 3 CALCULATIONS CONTAINED 338 UPPER DISTANCE CONSTRAINTS AND 123 REMARK 3 DIHEDRAL ANGLE CONSTRAINTS, NO HYDROGEN BONDING CONSTRAINTS WERE REMARK 3 USED. REMARK 4 REMARK 4 1NJQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-03. REMARK 100 THE DEPOSITION ID IS D_1000017929. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 301 REMARK 210 PH : 6.4 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : 2MM PEPTIDE,2.2MM ZNCL2, REMARK 210 90%H2O;10%D2O; 2MM PEPTIDE,2.2MM REMARK 210 ZNCL2;100%D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : PROSA 3.7, XEASY 1.3.12, DYANA REMARK 210 1.5 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS AND REMARK 210 UNRESTRAINED ENERGY MINIMIZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION 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: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 19 ACE A 0 C TRP A 1 N 0.144 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 ARG A 36 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 2 PHE A 15 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES REMARK 500 3 PHE A 15 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES REMARK 500 5 ARG A 4 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 8 PHE A 15 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES REMARK 500 9 PHE A 15 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES REMARK 500 10 PHE A 15 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES REMARK 500 11 PHE A 15 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES REMARK 500 14 PHE A 15 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES REMARK 500 15 PHE A 15 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES REMARK 500 16 PHE A 15 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES REMARK 500 18 PHE A 15 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES 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 3 -170.94 -67.15 REMARK 500 1 ARG A 4 83.75 60.98 REMARK 500 1 SER A 5 162.49 55.52 REMARK 500 1 PHE A 10 -54.56 -122.85 REMARK 500 1 PHE A 15 109.01 -165.59 REMARK 500 1 HIS A 28 -79.84 -81.51 REMARK 500 1 ASP A 31 179.81 55.68 REMARK 500 1 ARG A 32 -51.39 66.41 REMARK 500 1 ALA A 33 87.22 29.89 REMARK 500 1 ARG A 34 -38.49 71.28 REMARK 500 1 LEU A 35 -47.23 66.72 REMARK 500 1 ARG A 36 -44.74 -157.84 REMARK 500 2 SER A 5 147.68 60.63 REMARK 500 2 PHE A 10 -50.53 -124.39 REMARK 500 2 PHE A 15 101.66 -169.67 REMARK 500 2 HIS A 28 48.38 -82.98 REMARK 500 2 ARG A 29 92.16 -171.73 REMARK 500 2 ARG A 32 -78.01 68.63 REMARK 500 2 ALA A 33 -90.50 -172.39 REMARK 500 2 ARG A 34 113.20 -167.24 REMARK 500 2 LEU A 35 162.06 64.87 REMARK 500 3 PHE A 10 -50.83 -130.96 REMARK 500 3 PHE A 15 109.04 -170.28 REMARK 500 3 HIS A 28 -83.67 -81.03 REMARK 500 3 ARG A 29 103.45 160.01 REMARK 500 3 ARG A 32 100.25 63.85 REMARK 500 3 ARG A 34 -50.06 -167.24 REMARK 500 3 LEU A 35 77.43 55.92 REMARK 500 4 PHE A 15 109.35 -169.08 REMARK 500 4 HIS A 28 48.07 -82.33 REMARK 500 4 ARG A 29 83.51 -173.86 REMARK 500 4 LEU A 35 107.93 61.86 REMARK 500 5 PHE A 10 -50.14 -122.17 REMARK 500 5 PHE A 15 108.31 -170.53 REMARK 500 5 ARG A 29 117.65 -171.02 REMARK 500 5 ARG A 32 89.61 -160.17 REMARK 500 5 ALA A 33 -82.50 -169.48 REMARK 500 5 ARG A 34 174.89 61.11 REMARK 500 5 LEU A 35 78.83 40.91 REMARK 500 6 PRO A 3 32.41 -71.95 REMARK 500 6 ARG A 4 -152.28 -101.51 REMARK 500 6 PHE A 10 -51.37 -120.11 REMARK 500 6 PHE A 15 117.80 -168.33 REMARK 500 6 HIS A 28 45.81 -88.85 REMARK 500 6 ARG A 29 94.25 -171.13 REMARK 500 6 ASP A 31 -92.51 -125.04 REMARK 500 6 ALA A 33 -86.22 -121.55 REMARK 500 6 ARG A 34 99.83 -164.90 REMARK 500 6 LEU A 35 146.40 65.92 REMARK 500 7 SER A 5 160.03 73.52 REMARK 500 REMARK 500 THIS ENTRY HAS 159 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 TYR A 6 0.10 SIDE CHAIN REMARK 500 1 PHE A 15 0.13 SIDE CHAIN REMARK 500 2 TYR A 6 0.12 SIDE CHAIN REMARK 500 2 PHE A 15 0.13 SIDE CHAIN REMARK 500 3 TYR A 6 0.10 SIDE CHAIN REMARK 500 3 PHE A 15 0.14 SIDE CHAIN REMARK 500 4 TYR A 6 0.14 SIDE CHAIN REMARK 500 4 PHE A 15 0.13 SIDE CHAIN REMARK 500 5 TYR A 6 0.09 SIDE CHAIN REMARK 500 5 PHE A 15 0.12 SIDE CHAIN REMARK 500 6 TYR A 6 0.07 SIDE CHAIN REMARK 500 6 PHE A 15 0.12 SIDE CHAIN REMARK 500 7 PHE A 15 0.13 SIDE CHAIN REMARK 500 8 PHE A 15 0.15 SIDE CHAIN REMARK 500 9 TYR A 6 0.08 SIDE CHAIN REMARK 500 9 PHE A 15 0.13 SIDE CHAIN REMARK 500 10 TYR A 6 0.07 SIDE CHAIN REMARK 500 10 PHE A 15 0.13 SIDE CHAIN REMARK 500 11 TYR A 6 0.12 SIDE CHAIN REMARK 500 11 PHE A 15 0.14 SIDE CHAIN REMARK 500 12 TYR A 6 0.08 SIDE CHAIN REMARK 500 12 PHE A 15 0.14 SIDE CHAIN REMARK 500 13 TYR A 6 0.08 SIDE CHAIN REMARK 500 13 PHE A 15 0.14 SIDE CHAIN REMARK 500 14 TYR A 6 0.10 SIDE CHAIN REMARK 500 14 PHE A 15 0.14 SIDE CHAIN REMARK 500 15 TYR A 6 0.09 SIDE CHAIN REMARK 500 15 PHE A 15 0.14 SIDE CHAIN REMARK 500 16 PHE A 15 0.15 SIDE CHAIN REMARK 500 17 TYR A 6 0.09 SIDE CHAIN REMARK 500 17 PHE A 15 0.14 SIDE CHAIN REMARK 500 18 TYR A 6 0.09 SIDE CHAIN REMARK 500 18 PHE A 15 0.13 SIDE CHAIN REMARK 500 19 PHE A 15 0.12 SIDE CHAIN REMARK 500 20 PHE A 15 0.13 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 11 HIS A 28 11.24 REMARK 500 REMARK 500 REMARK: NULL 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 64 DBREF 1NJQ A 1 37 UNP Q38895 SUP_ARATH 42 78 SEQRES 1 A 39 ACE TRP PRO PRO ARG SER TYR THR CYS SER PHE CYS LYS SEQRES 2 A 39 ARG GLU PHE ARG SER ALA GLN ALA LEU GLY GLY HIS MET SEQRES 3 A 39 ASN VAL HIS ARG ARG ASP ARG ALA ARG LEU ARG LEU NH2 HET ACE A 0 6 HET NH2 A 38 3 HET ZN A 64 1 HETNAM ACE ACETYL GROUP HETNAM NH2 AMINO GROUP HETNAM ZN ZINC ION FORMUL 1 ACE C2 H4 O FORMUL 1 NH2 H2 N FORMUL 2 ZN ZN 2+ HELIX 1 1 SER A 17 VAL A 27 1 11 SHEET 1 A 2 TYR A 6 THR A 7 0 SHEET 2 A 2 GLU A 14 PHE A 15 -1 O PHE A 15 N TYR A 6 LINK C ACE A 0 N TRP A 1 1555 1555 1.32 LINK C LEU A 37 N NH2 A 38 1555 1555 1.32 SITE 1 AC1 3 TRP A 1 LEU A 21 MET A 25 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 - b 23 2 Bytes