Header list of 1fa4.pdb file
Complete list - b 23 2 Bytes
HEADER ELECTRON TRANSPORT 12-JUL-00 1FA4 TITLE ELUCIDATION OF THE PARAMAGNETIC RELAXATION OF HETERONUCLEI AND PROTONS TITLE 2 IN CU(II) PLASTOCYANIN FROM ANABAENA VARIABILIS COMPND MOL_ID: 1; COMPND 2 MOLECULE: PLASTOCYANIN; COMPND 3 CHAIN: A SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ANABAENA VARIABILIS; SOURCE 3 ORGANISM_TAXID: 1172 KEYWDS PLASTOCYANIN, ANABAENA VARIABILIS, ELECTRON TRANSPORT EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR L.MA,A.M.JORGENSEN,G.O.SORENSEN,J.ULSTRUP,J.J.LED REVDAT 4 23-FEB-22 1FA4 1 REMARK LINK REVDAT 3 24-FEB-09 1FA4 1 VERSN REVDAT 2 03-OCT-01 1FA4 1 JRNL REMARK CRYST1 REVDAT 1 16-AUG-00 1FA4 0 JRNL AUTH L.MA,A.M.JORGENSEN,G.O.SOERENSEN,J.ULSTRUP,J.J.LED JRNL TITL ELUCIDATION OF THE PARAMAGNETIC R1 RELAXATION OF JRNL TITL 2 HETERONUCLEI AND PROTONS IN CU(II) PLASTOCYANIN FROM JRNL TITL 3 ANABAENA VARIABILIS JRNL REF J.AM.CHEM.SOC. V. 122 9473 2000 JRNL REFN ISSN 0002-7863 JRNL DOI 10.1021/JA001368Z REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH U.BADSBERG,A.M.JORGENSEN,H.GESMAR,J.J.LED,J.M.HAMMERSTAD, REMARK 1 AUTH 2 L.L.JESPERSEN,J.ULSTRUP REMARK 1 TITL SOLUTION STRUCTURE OF REDUCED PLASTOCYANIN FROM THE REMARK 1 TITL 2 BLUE-GREEN ALGA ANABAENA VARIABILIS REMARK 1 REF BIOCHEMISTRY V. 35 7021 1996 REMARK 1 REFN ISSN 0006-2960 REMARK 1 DOI 10.1021/BI960621Y REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851, X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1FA4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-00. REMARK 100 THE DEPOSITION ID IS D_1000011431. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298; 298 REMARK 210 PH : 6.9; 6.9 REMARK 210 IONIC STRENGTH : 100 MM; 100 MM REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 2.9 TO 3.2 MM UNLABELED A. V. REMARK 210 PCU; 100 MM NACL; 2.9 TO 3.2 MM REMARK 210 UNLABELED A. V. PCU; 100 MM NACL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING AND RESTRAINED ENERGY REMARK 210 MINIMIZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 60 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: INPUT DATA FOR STRUCTURE CALCULATION: 595 INTRARESIDUAL REMARK 210 RESTRAINTS, 279 SEQUENTIAL RESTRAINTS, 585 INTERRESIDUAL REMARK 210 RESTRAINTS, 49 DIHEDRAL (PHI) RESTRAINTS, 29 DIHEDRAL (CHI) REMARK 210 RESTRAINTS, 9 DIHEDRAL (OMIGA_PROLIN) RESTRAINTS, 0 HYDROGEN REMARK 210 BOND RESTRAINTS, 4 COPPER RESTRAINTS. THE RMS DEVIATION FROM REMARK 210 IDEALIZED GEOMETRY: BONDS:0.0031 ANGSTROMS, ANGLES:1.06 REMARK 210 ANGSTROMS, IMPROPERS:0.42 ANGSTROMS. 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 O LEU A 21 H THR A 102 1.56 REMARK 500 O ALA A 56 H LEU A 59 1.59 REMARK 500 OD1 ASP A 10 H LYS A 11 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 LYS A 6 79.21 -69.46 REMARK 500 1 SER A 9 -82.45 -69.86 REMARK 500 1 ASP A 10 -50.17 163.45 REMARK 500 1 LEU A 13 -156.51 -138.65 REMARK 500 1 PHE A 16 165.83 -44.47 REMARK 500 1 ASP A 27 -176.14 -53.30 REMARK 500 1 ASN A 34 -109.01 -101.50 REMARK 500 1 VAL A 36 61.98 -153.02 REMARK 500 1 LYS A 51 92.94 -40.37 REMARK 500 1 SER A 52 -159.21 -140.71 REMARK 500 1 ALA A 53 56.95 -155.81 REMARK 500 1 ASP A 54 -60.99 -138.78 REMARK 500 1 LEU A 59 -54.88 -127.00 REMARK 500 1 LYS A 62 -160.20 -125.06 REMARK 500 1 GLN A 63 135.51 65.87 REMARK 500 1 SER A 71 -78.46 -120.01 REMARK 500 1 THR A 72 119.00 -160.14 REMARK 500 1 ALA A 80 110.88 -39.95 REMARK 500 1 THR A 86 101.23 -165.18 REMARK 500 1 ALA A 104 161.64 -46.03 REMARK 500 2 SER A 9 -82.17 -50.47 REMARK 500 2 ASP A 10 -93.67 -176.88 REMARK 500 2 LYS A 11 54.28 -100.06 REMARK 500 2 LEU A 13 -159.32 -144.89 REMARK 500 2 ASN A 34 -129.63 -97.10 REMARK 500 2 VAL A 36 67.89 -154.96 REMARK 500 2 LYS A 51 35.58 34.28 REMARK 500 2 LYS A 62 -163.07 -121.25 REMARK 500 2 GLN A 63 -165.82 59.19 REMARK 500 2 SER A 71 -168.87 -124.62 REMARK 500 2 PHE A 76 160.03 -39.79 REMARK 500 2 ASP A 79 -61.41 -98.85 REMARK 500 2 ALA A 80 94.70 42.88 REMARK 500 2 TYR A 85 70.76 -100.71 REMARK 500 2 THR A 86 97.53 -62.83 REMARK 500 2 HIS A 92 67.25 -106.84 REMARK 500 2 ALA A 95 39.08 -93.43 REMARK 500 2 MET A 97 47.17 -86.59 REMARK 500 2 ALA A 104 -151.49 -119.39 REMARK 500 3 LEU A 7 100.12 -50.86 REMARK 500 3 SER A 9 -95.80 -48.00 REMARK 500 3 ASP A 10 33.27 176.86 REMARK 500 3 LYS A 11 -43.05 -136.08 REMARK 500 3 ASP A 27 -178.69 -55.81 REMARK 500 3 ASN A 34 -95.49 -110.02 REMARK 500 3 LYS A 35 33.14 -143.05 REMARK 500 3 VAL A 36 59.58 -151.49 REMARK 500 3 PRO A 38 -158.57 -82.42 REMARK 500 3 LYS A 51 36.79 34.53 REMARK 500 3 ALA A 53 80.31 -166.12 REMARK 500 REMARK 500 THIS ENTRY HAS 386 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 93 0.18 SIDE CHAIN REMARK 500 2 ARG A 93 0.20 SIDE CHAIN REMARK 500 3 ARG A 93 0.23 SIDE CHAIN REMARK 500 5 ARG A 93 0.08 SIDE CHAIN REMARK 500 6 ARG A 93 0.31 SIDE CHAIN REMARK 500 7 ARG A 93 0.23 SIDE CHAIN REMARK 500 8 ARG A 93 0.27 SIDE CHAIN REMARK 500 9 ARG A 93 0.29 SIDE CHAIN REMARK 500 10 ARG A 93 0.32 SIDE CHAIN REMARK 500 11 ARG A 93 0.18 SIDE CHAIN REMARK 500 12 ARG A 93 0.23 SIDE CHAIN REMARK 500 13 ARG A 93 0.20 SIDE CHAIN REMARK 500 14 ARG A 93 0.22 SIDE CHAIN REMARK 500 15 ARG A 93 0.24 SIDE CHAIN REMARK 500 16 ARG A 93 0.22 SIDE CHAIN REMARK 500 17 ARG A 93 0.20 SIDE CHAIN REMARK 500 18 ARG A 93 0.31 SIDE CHAIN REMARK 500 19 ARG A 93 0.28 SIDE CHAIN REMARK 500 20 ARG A 93 0.32 SIDE CHAIN 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 CU A 106 CU REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 39 ND1 REMARK 620 2 CYS A 89 SG 130.6 REMARK 620 3 HIS A 92 ND1 86.8 104.7 REMARK 620 N 1 2 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 106 DBREF 1FA4 A 1 105 UNP P00301 PLAS_ANAVA 1 105 SEQRES 1 A 105 GLU THR TYR THR VAL LYS LEU GLY SER ASP LYS GLY LEU SEQRES 2 A 105 LEU VAL PHE GLU PRO ALA LYS LEU THR ILE LYS PRO GLY SEQRES 3 A 105 ASP THR VAL GLU PHE LEU ASN ASN LYS VAL PRO PRO HIS SEQRES 4 A 105 ASN VAL VAL PHE ASP ALA ALA LEU ASN PRO ALA LYS SER SEQRES 5 A 105 ALA ASP LEU ALA LYS SER LEU SER HIS LYS GLN LEU LEU SEQRES 6 A 105 MET SER PRO GLY GLN SER THR SER THR THR PHE PRO ALA SEQRES 7 A 105 ASP ALA PRO ALA GLY GLU TYR THR PHE TYR CYS GLU PRO SEQRES 8 A 105 HIS ARG GLY ALA GLY MET VAL GLY LYS ILE THR VAL ALA SEQRES 9 A 105 GLY HET CU A 106 1 HETNAM CU COPPER (II) ION FORMUL 2 CU CU 2+ SHEET 1 A 3 TYR A 3 VAL A 5 0 SHEET 2 A 3 VAL A 29 PHE A 31 1 N GLU A 30 O TYR A 3 SHEET 3 A 3 THR A 72 THR A 74 -1 N THR A 72 O PHE A 31 SHEET 1 B 2 LYS A 20 ILE A 23 0 SHEET 2 B 2 LYS A 100 VAL A 103 1 O LYS A 100 N LEU A 21 SHEET 1 C 2 VAL A 42 PHE A 43 0 SHEET 2 C 2 PHE A 87 TYR A 88 -1 N TYR A 88 O VAL A 42 LINK ND1 HIS A 39 CU CU A 106 1555 1555 2.06 LINK SG CYS A 89 CU CU A 106 1555 1555 2.11 LINK ND1 HIS A 92 CU CU A 106 1555 1555 2.05 CISPEP 1 GLU A 17 PRO A 18 1 0.19 CISPEP 2 PRO A 37 PRO A 38 1 -1.76 CISPEP 3 GLU A 17 PRO A 18 2 0.18 CISPEP 4 PRO A 37 PRO A 38 2 -1.75 CISPEP 5 GLU A 17 PRO A 18 3 -0.27 CISPEP 6 PRO A 37 PRO A 38 3 -0.89 CISPEP 7 GLU A 17 PRO A 18 4 -0.05 CISPEP 8 PRO A 37 PRO A 38 4 -1.64 CISPEP 9 GLU A 17 PRO A 18 5 0.52 CISPEP 10 PRO A 37 PRO A 38 5 -1.39 CISPEP 11 GLU A 17 PRO A 18 6 0.27 CISPEP 12 PRO A 37 PRO A 38 6 -1.62 CISPEP 13 GLU A 17 PRO A 18 7 0.34 CISPEP 14 PRO A 37 PRO A 38 7 -1.50 CISPEP 15 GLU A 17 PRO A 18 8 0.19 CISPEP 16 PRO A 37 PRO A 38 8 -1.28 CISPEP 17 GLU A 17 PRO A 18 9 0.30 CISPEP 18 PRO A 37 PRO A 38 9 -1.66 CISPEP 19 GLU A 17 PRO A 18 10 0.40 CISPEP 20 PRO A 37 PRO A 38 10 -1.82 CISPEP 21 GLU A 17 PRO A 18 11 0.09 CISPEP 22 PRO A 37 PRO A 38 11 -0.97 CISPEP 23 GLU A 17 PRO A 18 12 0.12 CISPEP 24 PRO A 37 PRO A 38 12 -1.81 CISPEP 25 GLU A 17 PRO A 18 13 0.52 CISPEP 26 PRO A 37 PRO A 38 13 -1.47 CISPEP 27 GLU A 17 PRO A 18 14 -0.18 CISPEP 28 PRO A 37 PRO A 38 14 -1.89 CISPEP 29 GLU A 17 PRO A 18 15 0.65 CISPEP 30 PRO A 37 PRO A 38 15 -1.81 CISPEP 31 GLU A 17 PRO A 18 16 0.47 CISPEP 32 PRO A 37 PRO A 38 16 -1.43 CISPEP 33 GLU A 17 PRO A 18 17 0.33 CISPEP 34 PRO A 37 PRO A 38 17 -1.64 CISPEP 35 GLU A 17 PRO A 18 18 0.10 CISPEP 36 PRO A 37 PRO A 38 18 -2.15 CISPEP 37 GLU A 17 PRO A 18 19 0.12 CISPEP 38 PRO A 37 PRO A 38 19 -1.76 CISPEP 39 GLU A 17 PRO A 18 20 0.02 CISPEP 40 PRO A 37 PRO A 38 20 -1.76 SITE 1 AC1 4 HIS A 39 CYS A 89 HIS A 92 MET A 97 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