Header list of 1jhb.pdb file
Complete list - b 23 2 Bytes
HEADER ELECTRON TRANSPORT 17-FEB-98 1JHB TITLE HUMAN GLUTAREDOXIN IN FULLY REDUCED FORM, NMR, 20 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: GLUTAREDOXIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PET KEYWDS GLUTAREDOXIN, OXIDOREDUCTASE, ELECTRON TRANSPORT EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR C.SUN,J.H.BUSHWELLER REVDAT 3 23-FEB-22 1JHB 1 REMARK REVDAT 2 24-FEB-09 1JHB 1 VERSN REVDAT 1 26-AUG-98 1JHB 0 JRNL AUTH C.SUN,M.J.BERARDI,J.H.BUSHWELLER JRNL TITL THE NMR SOLUTION STRUCTURE OF HUMAN GLUTAREDOXIN IN THE JRNL TITL 2 FULLY REDUCED FORM. JRNL REF J.MOL.BIOL. V. 280 687 1998 JRNL REFN ISSN 0022-2836 JRNL PMID 9677297 JRNL DOI 10.1006/JMBI.1998.1913 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.SUN,A.HOLMGREN,J.H.BUSHWELLER REMARK 1 TITL COMPLETE 1H, 13C, AND 15N NMR RESONANCE ASSIGNMENTS AND REMARK 1 TITL 2 SECONDARY STRUCTURE OF HUMAN GLUTAREDOXIN IN THE FULLY REMARK 1 TITL 3 REDUCED FORM REMARK 1 REF PROTEIN SCI. V. 6 383 1997 REMARK 1 REFN ISSN 0961-8368 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 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 1JHB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000174328. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; HCCH-TOCSY; HACAHB; HNHB; REMARK 210 HSQC; CT-HSQC; HNCA; HN(CO)CA; REMARK 210 HNCACB; HN (CO)CACB; HN(CA)HA; REMARK 210 HNCO; (HB)CB(CGCD)HD; HB(CBCGCD) REMARK 210 HD REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS 500 REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION 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 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 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 MET A 1 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 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 9 ARG A 98 CD - NE - CZ ANGL. DEV. = 8.6 DEGREES REMARK 500 9 ARG A 98 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 9 ARG A 98 NE - CZ - NH2 ANGL. DEV. = -3.8 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 VAL A 15 79.17 -103.68 REMARK 500 1 THR A 51 20.74 -149.29 REMARK 500 1 ASN A 52 -148.64 -156.60 REMARK 500 1 LYS A 77 16.69 46.43 REMARK 500 1 ALA A 104 -74.52 -84.31 REMARK 500 2 GLN A 3 34.54 -66.67 REMARK 500 2 GLU A 4 -57.41 -163.42 REMARK 500 2 THR A 22 -106.17 -133.35 REMARK 500 2 CYS A 23 115.06 33.83 REMARK 500 2 THR A 51 -43.67 -150.97 REMARK 500 2 ASN A 52 -160.30 -170.53 REMARK 500 2 THR A 65 -71.67 -116.09 REMARK 500 2 LYS A 77 22.10 46.67 REMARK 500 2 CYS A 83 -55.70 -132.43 REMARK 500 2 ALA A 104 -70.47 -75.74 REMARK 500 3 GLN A 3 -91.42 34.22 REMARK 500 3 THR A 22 31.45 -75.58 REMARK 500 3 ASN A 52 -106.66 -78.63 REMARK 500 3 HIS A 53 93.12 -163.60 REMARK 500 3 LYS A 77 21.14 47.26 REMARK 500 4 GLN A 3 58.70 34.74 REMARK 500 4 GLU A 4 -34.12 61.79 REMARK 500 4 THR A 65 -72.22 -127.22 REMARK 500 4 LYS A 77 27.73 46.21 REMARK 500 4 ALA A 104 -72.49 -91.34 REMARK 500 5 GLN A 3 46.78 -66.95 REMARK 500 5 GLU A 4 -56.41 -163.53 REMARK 500 5 PRO A 12 79.18 -67.50 REMARK 500 5 VAL A 15 79.39 -113.07 REMARK 500 5 ALA A 50 53.14 -69.04 REMARK 500 5 HIS A 53 79.82 67.62 REMARK 500 5 LYS A 77 15.28 46.48 REMARK 500 6 GLN A 3 158.06 -48.64 REMARK 500 6 CYS A 8 38.60 -81.40 REMARK 500 6 LYS A 9 -47.79 -130.91 REMARK 500 6 VAL A 15 79.58 -119.88 REMARK 500 6 THR A 51 -27.19 -172.03 REMARK 500 6 HIS A 53 82.32 124.63 REMARK 500 6 LYS A 77 21.37 47.31 REMARK 500 6 ALA A 104 -74.86 -84.93 REMARK 500 7 VAL A 6 -60.26 -90.51 REMARK 500 7 THR A 51 -106.41 -132.78 REMARK 500 7 LYS A 77 19.53 46.13 REMARK 500 7 ALA A 104 -75.65 -114.46 REMARK 500 8 GLN A 3 48.30 -85.45 REMARK 500 8 GLU A 4 -43.13 -163.45 REMARK 500 8 THR A 65 -76.03 -125.06 REMARK 500 9 GLU A 4 -55.88 -163.10 REMARK 500 9 ASN A 52 -163.37 57.76 REMARK 500 9 LYS A 77 -9.18 46.55 REMARK 500 REMARK 500 THIS ENTRY HAS 126 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 ARG A 72 0.09 SIDE CHAIN REMARK 500 2 ARG A 27 0.12 SIDE CHAIN REMARK 500 2 ARG A 28 0.09 SIDE CHAIN REMARK 500 2 ARG A 72 0.07 SIDE CHAIN REMARK 500 3 TYR A 60 0.08 SIDE CHAIN REMARK 500 3 ARG A 98 0.08 SIDE CHAIN REMARK 500 4 ARG A 72 0.12 SIDE CHAIN REMARK 500 6 TYR A 60 0.11 SIDE CHAIN REMARK 500 6 ARG A 98 0.09 SIDE CHAIN REMARK 500 8 TYR A 25 0.07 SIDE CHAIN REMARK 500 8 ARG A 28 0.11 SIDE CHAIN REMARK 500 8 ARG A 68 0.08 SIDE CHAIN REMARK 500 9 ARG A 27 0.12 SIDE CHAIN REMARK 500 9 ARG A 68 0.10 SIDE CHAIN REMARK 500 10 ARG A 27 0.11 SIDE CHAIN REMARK 500 11 ARG A 68 0.10 SIDE CHAIN REMARK 500 11 ARG A 98 0.10 SIDE CHAIN REMARK 500 12 ARG A 98 0.09 SIDE CHAIN REMARK 500 13 TYR A 25 0.12 SIDE CHAIN REMARK 500 13 TYR A 60 0.08 SIDE CHAIN REMARK 500 15 ARG A 72 0.08 SIDE CHAIN REMARK 500 16 TYR A 25 0.08 SIDE CHAIN REMARK 500 17 ARG A 28 0.09 SIDE CHAIN REMARK 500 17 ARG A 68 0.09 SIDE CHAIN REMARK 500 19 ARG A 68 0.10 SIDE CHAIN REMARK 500 20 ARG A 28 0.09 SIDE CHAIN REMARK 500 20 ARG A 98 0.10 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AVE REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: ACTIVE SITE. DBREF 1JHB A 2 106 UNP P35754 GLRX1_HUMAN 1 105 SEQRES 1 A 106 MET ALA GLN GLU PHE VAL ASN CYS LYS ILE GLN PRO GLY SEQRES 2 A 106 LYS VAL VAL VAL PHE ILE LYS PRO THR CYS PRO TYR CYS SEQRES 3 A 106 ARG ARG ALA GLN GLU ILE LEU SER GLN LEU PRO ILE LYS SEQRES 4 A 106 GLN GLY LEU LEU GLU PHE VAL ASP ILE THR ALA THR ASN SEQRES 5 A 106 HIS THR ASN GLU ILE GLN ASP TYR LEU GLN GLN LEU THR SEQRES 6 A 106 GLY ALA ARG THR VAL PRO ARG VAL PHE ILE GLY LYS ASP SEQRES 7 A 106 CYS ILE GLY GLY CYS SER ASP LEU VAL SER LEU GLN GLN SEQRES 8 A 106 SER GLY GLU LEU LEU THR ARG LEU LYS GLN ILE GLY ALA SEQRES 9 A 106 LEU GLN HELIX 1 H1 GLU A 4 LYS A 9 1 6 HELIX 2 H2 PRO A 24 SER A 34 1 11 HELIX 3 H3 THR A 54 THR A 65 1 12 HELIX 4 H4 SER A 84 GLN A 91 1 8 HELIX 5 H5 GLU A 94 LYS A 100 1 7 SHEET 1 S1 4 LEU A 43 ASP A 47 0 SHEET 2 S1 4 VAL A 15 ILE A 19 1 N VAL A 17 O GLU A 44 SHEET 3 S1 4 ARG A 72 ILE A 75 -1 N PHE A 74 O VAL A 16 SHEET 4 S1 4 ASP A 78 GLY A 81 -1 N ILE A 80 O VAL A 73 CISPEP 1 VAL A 70 PRO A 71 1 -3.52 CISPEP 2 VAL A 70 PRO A 71 2 -5.29 CISPEP 3 VAL A 70 PRO A 71 3 -10.00 CISPEP 4 VAL A 70 PRO A 71 4 -6.96 CISPEP 5 VAL A 70 PRO A 71 5 -1.21 CISPEP 6 VAL A 70 PRO A 71 6 -10.95 CISPEP 7 VAL A 70 PRO A 71 7 3.46 CISPEP 8 VAL A 70 PRO A 71 8 -11.91 CISPEP 9 VAL A 70 PRO A 71 9 -4.64 CISPEP 10 VAL A 70 PRO A 71 10 -9.01 CISPEP 11 VAL A 70 PRO A 71 11 -4.19 CISPEP 12 VAL A 70 PRO A 71 12 -7.29 CISPEP 13 VAL A 70 PRO A 71 13 -13.90 CISPEP 14 VAL A 70 PRO A 71 14 -8.35 CISPEP 15 VAL A 70 PRO A 71 15 -4.55 CISPEP 16 VAL A 70 PRO A 71 16 -7.89 CISPEP 17 VAL A 70 PRO A 71 17 -15.44 CISPEP 18 VAL A 70 PRO A 71 18 -5.15 CISPEP 19 VAL A 70 PRO A 71 19 -15.57 CISPEP 20 VAL A 70 PRO A 71 20 -4.99 SITE 1 AVE 2 CYS A 23 CYS A 26 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