Header list of 1hmj.pdb file
Complete list - 23 202 Bytes
HEADER RNA POLYMERASE 05-FEB-99 1HMJ TITLE SOLUTION STRUCTURE OF RNA POLYMERASE SUBUNIT H COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (SUBUNIT H); COMPND 3 CHAIN: A; COMPND 4 SYNONYM: RPB5; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: METHANOCALDOCOCCUS JANNASCHII; SOURCE 3 ORGANISM_TAXID: 2190; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS RNA POLYMERASE, SUBUNIT H, RPB5, ARCHAEA EXPDTA SOLUTION NMR AUTHOR A.THIRU,M.HODACH,J.ELORANTA,V.KOSTOUROU,R.WEINZIERL REVDAT 4 23-FEB-22 1HMJ 1 REMARK REVDAT 3 24-FEB-09 1HMJ 1 VERSN REVDAT 2 01-APR-03 1HMJ 1 JRNL REVDAT 1 05-APR-99 1HMJ 0 JRNL AUTH A.THIRU,M.HODACH,J.J.ELORANTA,V.KOSTOUROU,R.O.WEINZIERL, JRNL AUTH 2 S.MATTHEWS JRNL TITL RNA POLYMERASE SUBUNIT H FEATURES A BETA-RIBBON MOTIF WITHIN JRNL TITL 2 A NOVEL FOLD THAT IS PRESENT IN ARCHAEA AND EUKARYOTES. JRNL REF J.MOL.BIOL. V. 287 753 1999 JRNL REFN ISSN 0022-2836 JRNL PMID 10191143 JRNL DOI 10.1006/JMBI.1999.2638 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1HMJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-99. REMARK 100 THE DEPOSITION ID IS D_1000000454. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 302 REMARK 210 PH : 5 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 : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: MEAN STRUCTURE. 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 RES C SSSEQI REMARK 465 MET A 1 REMARK 465 LYS A 2 REMARK 465 VAL A 3 REMARK 465 THR A 4 REMARK 465 ASP A 5 REMARK 465 HIS A 6 REMARK 465 ILE A 7 REMARK 465 LEU A 8 REMARK 465 VAL A 9 REMARK 465 ILE A 78 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME; REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 470 RES CSSEQI ATOMS REMARK 470 PRO A 10 O CB CG CD REMARK 470 LYS A 11 O CB CG CD CE NZ REMARK 470 HIS A 12 O CB CG ND1 CD2 CE1 NE2 REMARK 470 GLU A 13 O CB CG CD OE1 OE2 REMARK 470 ILE A 14 O CB CG1 CG2 CD1 REMARK 470 VAL A 15 O CB CG1 CG2 REMARK 470 PRO A 16 O CB CG CD REMARK 470 LYS A 17 O CB CG CD CE NZ REMARK 470 GLU A 18 O CB CG CD OE1 OE2 REMARK 470 GLU A 19 O CB CG CD OE1 OE2 REMARK 470 VAL A 20 O CB CG1 CG2 REMARK 470 GLU A 21 O CB CG CD OE1 OE2 REMARK 470 GLU A 22 O CB CG CD OE1 OE2 REMARK 470 ILE A 23 O CB CG1 CG2 CD1 REMARK 470 LEU A 24 O CB CG CD1 CD2 REMARK 470 LYS A 25 O CB CG CD CE NZ REMARK 470 ARG A 26 O CB CG CD NE CZ NH1 REMARK 470 ARG A 26 NH2 REMARK 470 TYR A 27 O CB CG CD1 CD2 CE1 CE2 REMARK 470 TYR A 27 CZ OH REMARK 470 ASN A 28 O CB CG OD1 ND2 REMARK 470 ILE A 29 O CB CG1 CG2 CD1 REMARK 470 LYS A 30 O CB CG CD CE NZ REMARK 470 ILE A 31 O CB CG1 CG2 CD1 REMARK 470 GLN A 32 O CB CG CD OE1 NE2 REMARK 470 GLN A 33 O CB CG CD OE1 NE2 REMARK 470 LEU A 34 O CB CG CD1 CD2 REMARK 470 PRO A 35 O CB CG CD REMARK 470 LYS A 36 O CB CG CD CE NZ REMARK 470 ILE A 37 O CB CG1 CG2 CD1 REMARK 470 TYR A 38 O CB CG CD1 CD2 CE1 CE2 REMARK 470 TYR A 38 CZ OH REMARK 470 GLU A 39 O CB CG CD OE1 OE2 REMARK 470 ASP A 40 O CB CG OD1 OD2 REMARK 470 ASP A 41 O CB CG OD1 OD2 REMARK 470 PRO A 42 O CB CG CD REMARK 470 VAL A 43 O CB CG1 CG2 REMARK 470 ILE A 44 O CB CG1 CG2 CD1 REMARK 470 GLN A 45 O CB CG CD OE1 NE2 REMARK 470 GLU A 46 O CB CG CD OE1 OE2 REMARK 470 ILE A 47 O CB CG1 CG2 CD1 REMARK 470 GLY A 48 O REMARK 470 ALA A 49 O CB REMARK 470 LYS A 50 O CB CG CD CE NZ REMARK 470 GLU A 51 O CB CG CD OE1 OE2 REMARK 470 GLY A 52 O REMARK 470 ASP A 53 O CB CG OD1 OD2 REMARK 470 VAL A 54 O CB CG1 CG2 REMARK 470 VAL A 55 O CB CG1 CG2 REMARK 470 ARG A 56 O CB CG CD NE CZ NH1 REMARK 470 ARG A 56 NH2 REMARK 470 VAL A 57 O CB CG1 CG2 REMARK 470 ILE A 58 O CB CG1 CG2 CD1 REMARK 470 ARG A 59 O CB CG CD NE CZ NH1 REMARK 470 ARG A 59 NH2 REMARK 470 LYS A 60 O CB CG CD CE NZ REMARK 470 SER A 61 O CB OG REMARK 470 PRO A 62 O CB CG CD REMARK 470 THR A 63 O CB OG1 CG2 REMARK 470 ALA A 64 O CB REMARK 470 GLY A 65 O REMARK 470 VAL A 66 O CB CG1 CG2 REMARK 470 SER A 67 O CB OG REMARK 470 ILE A 68 O CB CG1 CG2 CD1 REMARK 470 ALA A 69 O CB REMARK 470 TYR A 70 O CB CG CD1 CD2 CE1 CE2 REMARK 470 TYR A 70 CZ OH REMARK 470 ARG A 71 O CB CG CD NE CZ NH1 REMARK 470 ARG A 71 NH2 REMARK 470 LEU A 72 O CB CG CD1 CD2 REMARK 470 VAL A 73 O CB CG1 CG2 REMARK 470 ILE A 74 O CB CG1 CG2 CD1 REMARK 470 LYS A 75 O CB CG CD CE NZ REMARK 470 ARG A 76 O CB CG CD NE CZ NH1 REMARK 470 ARG A 76 NH2 REMARK 470 ILE A 77 O CB CG1 CG2 CD1 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 CA ARG A 76 N ILE A 77 1.36 REMARK 500 C ARG A 76 CA ILE A 77 1.37 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 PRO A 10 N PRO A 10 CA -0.168 REMARK 500 PRO A 10 CA PRO A 10 C -0.302 REMARK 500 PRO A 10 C LYS A 11 N -0.173 REMARK 500 LYS A 11 N LYS A 11 CA -0.263 REMARK 500 LYS A 11 C HIS A 12 N -0.316 REMARK 500 GLU A 13 C ILE A 14 N -0.145 REMARK 500 LYS A 30 C ILE A 31 N -0.403 REMARK 500 ILE A 31 CA ILE A 31 C -0.200 REMARK 500 ILE A 31 C GLN A 32 N -0.189 REMARK 500 GLN A 32 N GLN A 32 CA -0.173 REMARK 500 GLN A 32 C GLN A 33 N -0.274 REMARK 500 GLN A 33 C LEU A 34 N -0.251 REMARK 500 ALA A 49 C LYS A 50 N -0.530 REMARK 500 LYS A 50 CA LYS A 50 C -0.376 REMARK 500 LYS A 50 C GLU A 51 N -0.433 REMARK 500 GLU A 51 N GLU A 51 CA -0.332 REMARK 500 GLU A 51 C GLY A 52 N -0.307 REMARK 500 ARG A 59 C LYS A 60 N -0.182 REMARK 500 LYS A 60 CA LYS A 60 C -0.339 REMARK 500 LYS A 60 C SER A 61 N -0.221 REMARK 500 SER A 61 N SER A 61 CA -0.298 REMARK 500 SER A 61 C PRO A 62 N -0.244 REMARK 500 PRO A 62 CA PRO A 62 C -0.229 REMARK 500 PRO A 62 C THR A 63 N -0.350 REMARK 500 THR A 63 N THR A 63 CA -0.202 REMARK 500 THR A 63 CA THR A 63 C -0.354 REMARK 500 THR A 63 C ALA A 64 N -0.308 REMARK 500 ALA A 64 N ALA A 64 CA -0.318 REMARK 500 ALA A 64 CA ALA A 64 C -0.249 REMARK 500 ALA A 64 C GLY A 65 N -0.504 REMARK 500 GLY A 65 N GLY A 65 CA -0.218 REMARK 500 GLY A 65 CA GLY A 65 C -0.189 REMARK 500 GLY A 65 C VAL A 66 N -0.158 REMARK 500 VAL A 66 N VAL A 66 CA -0.162 REMARK 500 LYS A 75 C ARG A 76 N -0.267 REMARK 500 ARG A 76 CA ARG A 76 C -0.947 REMARK 500 ARG A 76 C ILE A 77 N -0.505 REMARK 500 ILE A 77 N ILE A 77 CA -0.871 REMARK 500 ILE A 77 CA ILE A 77 C -0.603 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 LYS A 30 CA - C - N ANGL. DEV. = 24.7 DEGREES REMARK 500 ILE A 31 C - N - CA ANGL. DEV. = 22.1 DEGREES REMARK 500 ALA A 49 CA - C - N ANGL. DEV. = 41.1 DEGREES REMARK 500 LYS A 50 C - N - CA ANGL. DEV. = 37.4 DEGREES REMARK 500 LYS A 50 N - CA - C ANGL. DEV. = 21.7 DEGREES REMARK 500 LYS A 50 CA - C - N ANGL. DEV. = 21.3 DEGREES REMARK 500 GLU A 51 C - N - CA ANGL. DEV. = 18.1 DEGREES REMARK 500 GLU A 51 N - CA - C ANGL. DEV. = 30.4 DEGREES REMARK 500 LYS A 75 CA - C - N ANGL. DEV. = 13.8 DEGREES REMARK 500 ARG A 76 N - CA - C ANGL. DEV. = 50.1 DEGREES REMARK 500 ARG A 76 CA - C - N ANGL. DEV. = 30.7 DEGREES REMARK 500 ILE A 77 C - N - CA ANGL. DEV. = 28.6 DEGREES REMARK 500 ILE A 77 N - CA - C ANGL. DEV. = 28.1 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 GLU A 19 -36.93 -151.47 REMARK 500 ASN A 28 39.48 164.61 REMARK 500 ILE A 29 38.66 31.41 REMARK 500 ILE A 31 14.95 175.02 REMARK 500 LEU A 34 102.05 172.98 REMARK 500 PRO A 35 34.76 -82.02 REMARK 500 ALA A 49 76.71 -113.15 REMARK 500 GLU A 51 74.10 107.19 REMARK 500 REMARK 500 REMARK: NULL DBREF 1HMJ A 1 78 UNP Q58443 RPOH_METJA 1 78 SEQRES 1 A 78 MET LYS VAL THR ASP HIS ILE LEU VAL PRO LYS HIS GLU SEQRES 2 A 78 ILE VAL PRO LYS GLU GLU VAL GLU GLU ILE LEU LYS ARG SEQRES 3 A 78 TYR ASN ILE LYS ILE GLN GLN LEU PRO LYS ILE TYR GLU SEQRES 4 A 78 ASP ASP PRO VAL ILE GLN GLU ILE GLY ALA LYS GLU GLY SEQRES 5 A 78 ASP VAL VAL ARG VAL ILE ARG LYS SER PRO THR ALA GLY SEQRES 6 A 78 VAL SER ILE ALA TYR ARG LEU VAL ILE LYS ARG ILE ILE HELIX 1 1 LYS A 17 ASN A 28 1 12 HELIX 2 2 VAL A 43 ILE A 47 1 5 HELIX 3 3 ILE A 31 LEU A 34 1 4 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
Complete list - 23 202 Bytes