Header list of 1jwe.pdb file
Complete list - b 23 2 Bytes
HEADER HYDROLASE 22-JAN-99 1JWE TITLE NMR STRUCTURE OF THE N-TERMINAL DOMAIN OF E. COLI DNAB HELICASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (DNAB HELICASE); COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-TERMINAL DOMAIN; COMPND 5 EC: 3.6.1.-; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: N-TERMINAL MET (23) NOT CLEAVED OFF DURING EXPRESSION SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) KEYWDS HELICASE, HYDROLASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.WEIGELT,S.E.BROWN,C.S.MILES,N.E.DIXON,G.OTTING REVDAT 5 23-FEB-22 1JWE 1 REMARK REVDAT 4 24-FEB-09 1JWE 1 VERSN REVDAT 3 01-APR-03 1JWE 1 JRNL REVDAT 2 29-DEC-99 1JWE 4 HEADER COMPND REMARK JRNL REVDAT 2 2 4 ATOM SOURCE SEQRES REVDAT 1 27-JAN-99 1JWE 0 JRNL AUTH J.WEIGELT,S.E.BROWN,C.S.MILES,N.E.DIXON,G.OTTING JRNL TITL NMR STRUCTURE OF THE N-TERMINAL DOMAIN OF E. COLI DNAB JRNL TITL 2 HELICASE: IMPLICATIONS FOR STRUCTURE REARRANGEMENTS IN THE JRNL TITL 3 HELICASE HEXAMER. JRNL REF STRUCTURE FOLD.DES. V. 7 681 1999 JRNL REFN ISSN 0969-2126 JRNL PMID 10404597 JRNL DOI 10.1016/S0969-2126(99)80089-6 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : OPAL REMARK 3 AUTHORS : LUGINBUHL,GUNTERT,BILLETER,WUTHRICH REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL CITATION ABOVE REMARK 4 REMARK 4 1JWE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JAN-99. REMARK 100 THE DEPOSITION ID IS D_1000000348. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 305 REMARK 210 PH : 7.5 REMARK 210 IONIC STRENGTH : 20 MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DMX, DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA REMARK 210 METHOD USED : SIMULATED ANNEALING IN TORSION REMARK 210 ANGLE SPACE REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION 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 OE1 GLU A 33 HG1 THR A 61 1.54 REMARK 500 OD2 ASP A 49 HG SER A 119 1.57 REMARK 500 HG SER A 29 OE2 GLU A 33 1.58 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 73 CD - NE - CZ ANGL. DEV. = 8.9 DEGREES REMARK 500 1 ARG A 128 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 6 ARG A 46 CD - NE - CZ ANGL. DEV. = 9.5 DEGREES REMARK 500 6 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES REMARK 500 14 ARG A 62 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 15 ARG A 65 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 17 ARG A 46 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES REMARK 500 17 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 18 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.1 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 ILE A 30 -65.38 -27.83 REMARK 500 1 ALA A 115 4.34 55.10 REMARK 500 2 HIS A 28 -26.84 -162.62 REMARK 500 2 SER A 29 72.78 52.61 REMARK 500 2 ILE A 81 30.06 -94.45 REMARK 500 2 SER A 114 177.23 60.53 REMARK 500 2 ASN A 117 34.50 -145.66 REMARK 500 3 ILE A 30 -65.61 -28.07 REMARK 500 3 ASP A 43 78.34 -152.30 REMARK 500 3 SER A 114 -30.36 -176.47 REMARK 500 3 ASN A 117 21.24 -76.82 REMARK 500 4 LYS A 24 166.14 59.67 REMARK 500 4 VAL A 25 134.04 69.15 REMARK 500 4 LYS A 110 34.90 -92.76 REMARK 500 4 ASN A 111 36.59 -145.28 REMARK 500 4 SER A 114 170.88 61.19 REMARK 500 5 SER A 114 55.45 39.02 REMARK 500 5 ALA A 115 -38.71 64.81 REMARK 500 5 ALA A 116 -101.70 45.23 REMARK 500 6 PRO A 27 36.52 -68.24 REMARK 500 6 TYR A 60 -33.31 -131.78 REMARK 500 6 ALA A 115 5.44 54.24 REMARK 500 6 MET A 134 65.04 -111.50 REMARK 500 7 VAL A 25 142.89 71.55 REMARK 500 7 HIS A 28 -172.23 46.15 REMARK 500 7 SER A 29 82.56 -160.33 REMARK 500 7 SER A 114 10.69 55.71 REMARK 500 7 ALA A 115 10.23 56.10 REMARK 500 8 SER A 29 66.09 64.70 REMARK 500 8 ALA A 115 -65.35 66.09 REMARK 500 8 ALA A 116 -112.12 44.23 REMARK 500 8 ASN A 117 27.21 -73.56 REMARK 500 9 HIS A 28 168.60 61.00 REMARK 500 9 SER A 29 40.69 -151.32 REMARK 500 9 SER A 114 -95.90 46.78 REMARK 500 9 ASN A 117 49.64 -144.57 REMARK 500 9 ILE A 135 109.64 -47.55 REMARK 500 10 HIS A 28 177.88 55.25 REMARK 500 10 SER A 29 16.36 -155.20 REMARK 500 10 ASP A 43 93.23 -161.47 REMARK 500 10 PRO A 113 49.78 -82.04 REMARK 500 10 SER A 114 27.64 48.42 REMARK 500 10 ASN A 117 54.65 -150.51 REMARK 500 10 MET A 134 39.62 -76.75 REMARK 500 11 HIS A 28 -171.82 59.66 REMARK 500 11 SER A 29 25.40 -142.95 REMARK 500 11 TYR A 60 -33.49 -140.12 REMARK 500 11 SER A 114 -172.74 60.12 REMARK 500 11 ALA A 115 12.31 -65.69 REMARK 500 12 ASP A 43 100.06 -161.51 REMARK 500 REMARK 500 THIS ENTRY HAS 98 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 MET A 23 LYS A 24 1 148.20 REMARK 500 MET A 23 LYS A 24 4 -141.87 REMARK 500 MET A 23 LYS A 24 20 -149.05 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 2 ARG A 46 0.11 SIDE CHAIN REMARK 500 2 ARG A 73 0.10 SIDE CHAIN REMARK 500 2 ARG A 126 0.12 SIDE CHAIN REMARK 500 4 ARG A 73 0.12 SIDE CHAIN REMARK 500 4 TYR A 104 0.07 SIDE CHAIN REMARK 500 4 ARG A 132 0.10 SIDE CHAIN REMARK 500 5 ARG A 53 0.12 SIDE CHAIN REMARK 500 7 TYR A 60 0.10 SIDE CHAIN REMARK 500 8 ARG A 126 0.09 SIDE CHAIN REMARK 500 9 ARG A 46 0.16 SIDE CHAIN REMARK 500 9 ARG A 73 0.10 SIDE CHAIN REMARK 500 10 TYR A 104 0.07 SIDE CHAIN REMARK 500 12 ARG A 92 0.09 SIDE CHAIN REMARK 500 13 ARG A 62 0.08 SIDE CHAIN REMARK 500 14 TYR A 60 0.12 SIDE CHAIN REMARK 500 16 ARG A 62 0.08 SIDE CHAIN REMARK 500 17 ARG A 92 0.08 SIDE CHAIN REMARK 500 17 ARG A 126 0.08 SIDE CHAIN REMARK 500 18 TYR A 60 0.06 SIDE CHAIN REMARK 500 18 ARG A 128 0.09 SIDE CHAIN REMARK 500 19 ARG A 53 0.10 SIDE CHAIN REMARK 500 19 TYR A 60 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1JWE A 23 136 UNP P0ACB0 DNAB_ECOLI 24 137 SEQADV 1JWE MET A 23 UNP P0ACB0 LEU 24 SEE REMARK 999 SEQRES 1 A 114 MET LYS VAL PRO PRO HIS SER ILE GLU ALA GLU GLN SER SEQRES 2 A 114 VAL LEU GLY GLY LEU MET LEU ASP ASN GLU ARG TRP ASP SEQRES 3 A 114 ASP VAL ALA GLU ARG VAL VAL ALA ASP ASP PHE TYR THR SEQRES 4 A 114 ARG PRO HIS ARG HIS ILE PHE THR GLU MET ALA ARG LEU SEQRES 5 A 114 GLN GLU SER GLY SER PRO ILE ASP LEU ILE THR LEU ALA SEQRES 6 A 114 GLU SER LEU GLU ARG GLN GLY GLN LEU ASP SER VAL GLY SEQRES 7 A 114 GLY PHE ALA TYR LEU ALA GLU LEU SER LYS ASN THR PRO SEQRES 8 A 114 SER ALA ALA ASN ILE SER ALA TYR ALA ASP ILE VAL ARG SEQRES 9 A 114 GLU ARG ALA VAL VAL ARG GLU MET ILE SER HELIX 1 1 ILE A 30 LEU A 42 1 13 HELIX 2 2 ASN A 44 ALA A 51 5 8 HELIX 3 3 ALA A 56 ASP A 58 5 3 HELIX 4 4 ARG A 62 GLU A 76 1 15 HELIX 5 5 LEU A 83 GLN A 93 1 11 HELIX 6 6 ASP A 97 VAL A 99 5 3 HELIX 7 7 GLY A 101 LYS A 110 1 10 HELIX 8 8 ILE A 118 GLU A 133 1 16 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