Header list of 1nin.pdb file
Complete list - b 23 2 Bytes
HEADER ELECTRON TRANSPORT 13-MAR-96 1NIN TITLE PLASTOCYANIN FROM ANABAENA VARIABILIS, NMR, 20 STRUCTURES 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 ELECTRON TRANSPORT EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR U.BADSBERG,A.M.M.JORGENSEN,H.GESMAR,J.J.LED,J.M.HAMMERSTAD-PETERSEN, AUTHOR 2 J.ULSTRUP REVDAT 3 23-FEB-22 1NIN 1 REMARK LINK REVDAT 2 24-FEB-09 1NIN 1 VERSN REVDAT 1 14-OCT-96 1NIN 0 JRNL AUTH U.BADSBERG,A.M.JORGENSEN,H.GESMAR,J.J.LED,J.M.HAMMERSTAD, JRNL AUTH 2 L.L.JESPERSEN,J.ULSTRUP JRNL TITL SOLUTION STRUCTURE OF REDUCED PLASTOCYANIN FROM THE JRNL TITL 2 BLUE-GREEN ALGA ANABAENA VARIABILIS. JRNL REF BIOCHEMISTRY V. 35 7021 1996 JRNL REFN ISSN 0006-2960 JRNL PMID 8679527 JRNL DOI 10.1021/BI960621Y REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1NIN 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_1000175305. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL 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 : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL 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 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 1 HIS A 39 NE2 HIS A 39 CD2 -0.085 REMARK 500 1 HIS A 92 NE2 HIS A 92 CD2 -0.073 REMARK 500 2 HIS A 39 NE2 HIS A 39 CD2 -0.088 REMARK 500 2 HIS A 92 NE2 HIS A 92 CD2 -0.075 REMARK 500 2 ARG A 93 CZ ARG A 93 NH2 -0.082 REMARK 500 3 HIS A 39 NE2 HIS A 39 CD2 -0.090 REMARK 500 3 HIS A 92 NE2 HIS A 92 CD2 -0.073 REMARK 500 4 HIS A 39 NE2 HIS A 39 CD2 -0.086 REMARK 500 4 HIS A 92 NE2 HIS A 92 CD2 -0.084 REMARK 500 4 ARG A 93 CZ ARG A 93 NH1 -0.080 REMARK 500 4 ARG A 93 CZ ARG A 93 NH2 -0.082 REMARK 500 5 HIS A 39 NE2 HIS A 39 CD2 -0.087 REMARK 500 5 HIS A 92 NE2 HIS A 92 CD2 -0.079 REMARK 500 5 ARG A 93 CZ ARG A 93 NH1 -0.081 REMARK 500 5 ARG A 93 CZ ARG A 93 NH2 -0.083 REMARK 500 6 HIS A 39 NE2 HIS A 39 CD2 -0.091 REMARK 500 6 HIS A 92 NE2 HIS A 92 CD2 -0.080 REMARK 500 6 ARG A 93 CZ ARG A 93 NH1 -0.079 REMARK 500 7 HIS A 39 NE2 HIS A 39 CD2 -0.083 REMARK 500 7 HIS A 92 NE2 HIS A 92 CD2 -0.077 REMARK 500 8 HIS A 39 NE2 HIS A 39 CD2 -0.083 REMARK 500 8 HIS A 92 NE2 HIS A 92 CD2 -0.080 REMARK 500 9 HIS A 39 NE2 HIS A 39 CD2 -0.088 REMARK 500 9 HIS A 92 NE2 HIS A 92 CD2 -0.077 REMARK 500 9 ARG A 93 CZ ARG A 93 NH1 -0.087 REMARK 500 10 HIS A 39 NE2 HIS A 39 CD2 -0.083 REMARK 500 10 HIS A 92 NE2 HIS A 92 CD2 -0.081 REMARK 500 11 HIS A 39 NE2 HIS A 39 CD2 -0.086 REMARK 500 11 HIS A 92 NE2 HIS A 92 CD2 -0.075 REMARK 500 11 ARG A 93 CZ ARG A 93 NH1 -0.079 REMARK 500 11 ARG A 93 CZ ARG A 93 NH2 -0.082 REMARK 500 12 HIS A 39 NE2 HIS A 39 CD2 -0.084 REMARK 500 12 HIS A 61 CG HIS A 61 ND1 -0.090 REMARK 500 12 HIS A 92 NE2 HIS A 92 CD2 -0.077 REMARK 500 12 ARG A 93 CZ ARG A 93 NH1 -0.082 REMARK 500 12 ARG A 93 CZ ARG A 93 NH2 -0.081 REMARK 500 13 HIS A 39 NE2 HIS A 39 CD2 -0.088 REMARK 500 13 HIS A 92 NE2 HIS A 92 CD2 -0.089 REMARK 500 14 HIS A 39 NE2 HIS A 39 CD2 -0.092 REMARK 500 14 HIS A 92 NE2 HIS A 92 CD2 -0.077 REMARK 500 14 ARG A 93 CZ ARG A 93 NH1 -0.084 REMARK 500 14 ARG A 93 CZ ARG A 93 NH2 -0.083 REMARK 500 15 HIS A 39 NE2 HIS A 39 CD2 -0.088 REMARK 500 15 HIS A 92 NE2 HIS A 92 CD2 -0.078 REMARK 500 15 ARG A 93 CZ ARG A 93 NH1 -0.081 REMARK 500 15 ARG A 93 CZ ARG A 93 NH2 -0.083 REMARK 500 16 HIS A 39 NE2 HIS A 39 CD2 -0.091 REMARK 500 16 HIS A 92 NE2 HIS A 92 CD2 -0.085 REMARK 500 17 HIS A 39 NE2 HIS A 39 CD2 -0.089 REMARK 500 17 HIS A 92 NE2 HIS A 92 CD2 -0.077 REMARK 500 REMARK 500 THIS ENTRY HAS 58 BOND DEVIATIONS. 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 2 LYS A 20 CA - CB - CG ANGL. DEV. = 15.3 DEGREES REMARK 500 2 GLY A 83 N - CA - C ANGL. DEV. = 15.9 DEGREES REMARK 500 3 THR A 2 OG1 - CB - CG2 ANGL. DEV. = -16.8 DEGREES REMARK 500 3 PHE A 16 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES REMARK 500 3 ASP A 27 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES REMARK 500 3 ASP A 54 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 3 TYR A 85 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 3 TYR A 85 CB - CG - CD1 ANGL. DEV. = 3.9 DEGREES REMARK 500 4 TYR A 3 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES REMARK 500 4 TYR A 3 CB - CG - CD1 ANGL. DEV. = 3.7 DEGREES REMARK 500 4 THR A 86 OG1 - CB - CG2 ANGL. DEV. = -15.4 DEGREES REMARK 500 4 CYS A 89 CA - CB - SG ANGL. DEV. = 7.1 DEGREES REMARK 500 5 ASP A 27 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES REMARK 500 5 HIS A 61 CA - CB - CG ANGL. DEV. = -10.5 DEGREES REMARK 500 5 TYR A 88 N - CA - CB ANGL. DEV. = -12.5 DEGREES REMARK 500 6 ASP A 27 N - CA - CB ANGL. DEV. = -12.0 DEGREES REMARK 500 6 THR A 28 OG1 - CB - CG2 ANGL. DEV. = -13.9 DEGREES REMARK 500 7 PHE A 16 CB - CG - CD2 ANGL. DEV. = -5.8 DEGREES REMARK 500 7 PHE A 16 CB - CG - CD1 ANGL. DEV. = 5.4 DEGREES REMARK 500 7 ASP A 44 CB - CG - OD1 ANGL. DEV. = -5.9 DEGREES REMARK 500 7 TYR A 88 N - CA - C ANGL. DEV. = 21.6 DEGREES REMARK 500 7 GLU A 90 N - CA - CB ANGL. DEV. = -11.7 DEGREES REMARK 500 7 ARG A 93 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES REMARK 500 8 ASP A 44 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES REMARK 500 8 CYS A 89 CA - CB - SG ANGL. DEV. = 15.8 DEGREES REMARK 500 9 PHE A 16 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES REMARK 500 9 PHE A 16 CB - CG - CD1 ANGL. DEV. = 5.1 DEGREES REMARK 500 9 ASP A 44 N - CA - CB ANGL. DEV. = -11.0 DEGREES REMARK 500 9 TYR A 85 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 9 ARG A 93 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 10 ASP A 54 N - CA - CB ANGL. DEV. = -12.3 DEGREES REMARK 500 10 CYS A 89 CA - CB - SG ANGL. DEV. = 12.4 DEGREES REMARK 500 10 ARG A 93 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES REMARK 500 11 GLU A 1 OE1 - CD - OE2 ANGL. DEV. = 9.4 DEGREES REMARK 500 11 ASP A 44 CB - CG - OD1 ANGL. DEV. = -6.3 DEGREES REMARK 500 12 TYR A 88 N - CA - CB ANGL. DEV. = -14.3 DEGREES REMARK 500 12 ARG A 93 NH1 - CZ - NH2 ANGL. DEV. = 6.6 DEGREES REMARK 500 12 ARG A 93 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES REMARK 500 12 ARG A 93 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 13 ASP A 27 CA - CB - CG ANGL. DEV. = 13.7 DEGREES REMARK 500 13 ASP A 27 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES REMARK 500 13 ASP A 27 CB - CG - OD2 ANGL. DEV. = -10.2 DEGREES REMARK 500 13 CYS A 89 CA - CB - SG ANGL. DEV. = 10.5 DEGREES REMARK 500 14 THR A 86 OG1 - CB - CG2 ANGL. DEV. = -15.2 DEGREES REMARK 500 14 ARG A 93 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES REMARK 500 15 GLU A 30 OE1 - CD - OE2 ANGL. DEV. = 7.7 DEGREES REMARK 500 15 PHE A 87 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES REMARK 500 15 ARG A 93 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 16 ASN A 40 N - CA - CB ANGL. DEV. = -11.4 DEGREES REMARK 500 16 THR A 86 OG1 - CB - CG2 ANGL. DEV. = -15.6 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 69 ANGLE DEVIATIONS. 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 THR A 2 84.49 -48.55 REMARK 500 1 SER A 9 -74.61 -114.88 REMARK 500 1 ASP A 10 -88.59 -99.31 REMARK 500 1 LEU A 13 112.11 -20.60 REMARK 500 1 LEU A 14 56.54 -100.82 REMARK 500 1 ILE A 23 -146.91 -100.39 REMARK 500 1 PRO A 25 63.61 -62.02 REMARK 500 1 VAL A 36 108.99 -4.25 REMARK 500 1 ASP A 44 50.27 -26.83 REMARK 500 1 LEU A 47 57.58 -90.57 REMARK 500 1 ALA A 50 48.31 -103.05 REMARK 500 1 LYS A 51 58.20 5.89 REMARK 500 1 ALA A 53 -55.89 -124.44 REMARK 500 1 ASP A 54 -58.41 -26.61 REMARK 500 1 LYS A 57 32.00 -85.53 REMARK 500 1 LEU A 64 62.33 19.88 REMARK 500 1 LEU A 65 88.62 -52.28 REMARK 500 1 PRO A 68 81.41 -56.16 REMARK 500 1 THR A 72 73.40 -114.75 REMARK 500 1 SER A 73 107.92 -49.31 REMARK 500 1 ALA A 80 61.44 10.29 REMARK 500 1 PRO A 81 66.79 -11.80 REMARK 500 1 ALA A 82 47.50 6.71 REMARK 500 1 GLU A 90 -70.19 -2.76 REMARK 500 1 HIS A 92 73.73 -111.75 REMARK 500 2 THR A 2 76.76 -46.84 REMARK 500 2 ASP A 10 -58.48 14.96 REMARK 500 2 LEU A 14 51.03 -94.78 REMARK 500 2 PRO A 18 44.91 -38.75 REMARK 500 2 ALA A 19 -61.35 66.28 REMARK 500 2 LYS A 20 67.51 -114.98 REMARK 500 2 PRO A 25 69.21 -36.78 REMARK 500 2 THR A 28 50.78 -108.12 REMARK 500 2 LYS A 35 -169.59 96.07 REMARK 500 2 VAL A 36 75.57 22.15 REMARK 500 2 HIS A 39 74.97 -110.49 REMARK 500 2 LEU A 47 42.26 -99.80 REMARK 500 2 PRO A 49 -79.03 -47.37 REMARK 500 2 ALA A 50 53.06 -94.92 REMARK 500 2 LYS A 51 54.63 11.57 REMARK 500 2 SER A 52 -168.53 -114.78 REMARK 500 2 ASP A 54 -81.42 -28.08 REMARK 500 2 LYS A 62 -111.11 -6.77 REMARK 500 2 GLN A 63 -74.83 -144.59 REMARK 500 2 MET A 66 52.14 -92.58 REMARK 500 2 SER A 67 67.59 -109.47 REMARK 500 2 PRO A 68 83.21 -52.48 REMARK 500 2 THR A 75 109.26 -54.78 REMARK 500 2 PRO A 77 -43.90 -24.20 REMARK 500 2 ALA A 78 39.02 145.10 REMARK 500 REMARK 500 THIS ENTRY HAS 556 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 GLU A 17 PRO A 18 2 -97.44 REMARK 500 ASN A 48 PRO A 49 3 -146.94 REMARK 500 GLU A 17 PRO A 18 6 119.49 REMARK 500 SER A 67 PRO A 68 6 147.78 REMARK 500 PHE A 76 PRO A 77 6 -143.66 REMARK 500 PRO A 37 PRO A 38 8 -31.22 REMARK 500 ASN A 48 PRO A 49 13 -126.77 REMARK 500 GLU A 90 PRO A 91 13 144.95 REMARK 500 ASN A 48 PRO A 49 15 -114.13 REMARK 500 LYS A 24 PRO A 25 16 149.40 REMARK 500 LYS A 24 PRO A 25 19 149.91 REMARK 500 LYS A 24 PRO A 25 20 121.76 REMARK 500 ALA A 80 PRO A 81 20 -146.47 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 0.30 SIDE CHAIN REMARK 500 2 ARG A 93 0.25 SIDE CHAIN REMARK 500 3 ARG A 93 0.26 SIDE CHAIN REMARK 500 4 ARG A 93 0.30 SIDE CHAIN REMARK 500 5 ARG A 93 0.25 SIDE CHAIN REMARK 500 6 ARG A 93 0.22 SIDE CHAIN REMARK 500 8 ARG A 93 0.30 SIDE CHAIN REMARK 500 9 ARG A 93 0.27 SIDE CHAIN REMARK 500 10 ARG A 93 0.27 SIDE CHAIN REMARK 500 11 ARG A 93 0.29 SIDE CHAIN REMARK 500 12 ARG A 93 0.28 SIDE CHAIN REMARK 500 13 ARG A 93 0.27 SIDE CHAIN REMARK 500 14 ARG A 93 0.31 SIDE CHAIN REMARK 500 15 ARG A 93 0.28 SIDE CHAIN REMARK 500 16 ARG A 93 0.25 SIDE CHAIN REMARK 500 17 ARG A 93 0.22 SIDE CHAIN REMARK 500 18 ARG A 93 0.29 SIDE CHAIN REMARK 500 19 ARG A 93 0.29 SIDE CHAIN REMARK 500 20 ARG A 93 0.31 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 107.9 REMARK 620 3 HIS A 92 ND1 109.5 113.5 REMARK 620 4 MET A 97 SD 96.6 120.8 106.9 REMARK 620 N 1 2 3 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 1NIN 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+ HELIX 1 1 ALA A 56 SER A 58 5 3 HELIX 2 2 ALA A 80 ALA A 82 5 3 SHEET 1 A 2 TYR A 3 LEU A 7 0 SHEET 2 A 2 VAL A 29 ASN A 33 1 N GLU A 30 O TYR A 3 SHEET 1 B 2 LYS A 20 THR A 22 0 SHEET 2 B 2 LYS A 100 THR A 102 1 N LYS A 100 O LEU A 21 SHEET 1 C 2 VAL A 41 PHE A 43 0 SHEET 2 C 2 PHE A 87 CYS A 89 -1 N TYR A 88 O VAL A 42 LINK ND1 HIS A 39 CU CU A 106 1555 1555 1.75 LINK SG CYS A 89 CU CU A 106 1555 1555 2.06 LINK ND1 HIS A 92 CU CU A 106 1555 1555 1.75 LINK SD MET A 97 CU CU A 106 1555 1555 2.35 CISPEP 1 GLU A 17 PRO A 18 1 -13.80 CISPEP 2 PRO A 37 PRO A 38 1 -18.73 CISPEP 3 PRO A 37 PRO A 38 2 -17.93 CISPEP 4 GLU A 17 PRO A 18 3 -0.02 CISPEP 5 PRO A 37 PRO A 38 3 -14.72 CISPEP 6 GLU A 17 PRO A 18 4 -3.45 CISPEP 7 PRO A 37 PRO A 38 4 14.53 CISPEP 8 GLU A 17 PRO A 18 5 -5.41 CISPEP 9 PRO A 37 PRO A 38 5 4.38 CISPEP 10 PRO A 37 PRO A 38 6 -8.45 CISPEP 11 GLU A 17 PRO A 18 7 -9.78 CISPEP 12 PRO A 37 PRO A 38 7 -7.29 CISPEP 13 GLU A 17 PRO A 18 8 -14.06 CISPEP 14 GLU A 17 PRO A 18 9 -22.90 CISPEP 15 PRO A 37 PRO A 38 9 -17.22 CISPEP 16 GLU A 17 PRO A 18 10 -1.10 CISPEP 17 PRO A 37 PRO A 38 10 -7.55 CISPEP 18 GLU A 17 PRO A 18 11 -1.71 CISPEP 19 PRO A 37 PRO A 38 11 -7.18 CISPEP 20 GLU A 17 PRO A 18 12 -24.24 CISPEP 21 PRO A 37 PRO A 38 12 -18.28 CISPEP 22 GLU A 17 PRO A 18 13 -17.65 CISPEP 23 PRO A 37 PRO A 38 13 20.85 CISPEP 24 GLU A 17 PRO A 18 14 -10.74 CISPEP 25 PRO A 37 PRO A 38 14 -9.31 CISPEP 26 GLU A 17 PRO A 18 15 4.19 CISPEP 27 PRO A 37 PRO A 38 15 -22.19 CISPEP 28 GLU A 17 PRO A 18 16 17.70 CISPEP 29 PRO A 37 PRO A 38 16 -11.19 CISPEP 30 GLU A 17 PRO A 18 17 5.24 CISPEP 31 PRO A 37 PRO A 38 17 -7.55 CISPEP 32 GLU A 17 PRO A 18 18 -10.19 CISPEP 33 PRO A 37 PRO A 38 18 -13.24 CISPEP 34 GLU A 17 PRO A 18 19 4.18 CISPEP 35 PRO A 37 PRO A 38 19 -11.16 CISPEP 36 GLU A 17 PRO A 18 20 -25.75 CISPEP 37 PRO A 37 PRO A 38 20 -10.90 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