Header list of 1xyd.pdb file
Complete list - r 2 2 Bytes
HEADER METAL BINDING PROTEIN 09-NOV-04 1XYD TITLE NMR SOLUTION STRUCTURE OF RAT ZINC-CALCIUM-S100B, 20 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: S-100 PROTEIN, BETA CHAIN; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: S100B; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 GENE: S100B; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HMS174(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11B KEYWDS METAL BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR P.T.WILDER,K.M.VARNEY,D.J.WEBER REVDAT 3 02-MAR-22 1XYD 1 REMARK LINK REVDAT 2 24-FEB-09 1XYD 1 VERSN REVDAT 1 07-JUN-05 1XYD 0 JRNL AUTH P.T.WILDER,K.M.VARNEY,M.B.WEISS,R.K.GITTI,D.J.WEBER JRNL TITL SOLUTION STRUCTURE OF ZINC- AND CALCIUM-BOUND RAT S100B AS JRNL TITL 2 DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY JRNL REF BIOCHEMISTRY V. 44 5690 2005 JRNL REFN ISSN 0006-2960 JRNL PMID 15823027 JRNL DOI 10.1021/BI0475830 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE, X-PLOR XPLOR-NIH-2.9.2 REMARK 3 AUTHORS : BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1XYD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-NOV-04. REMARK 100 THE DEPOSITION ID IS D_1000030905. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310.15 REMARK 210 PH : 7.2 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 3 MM 15N S100B (MONOMER REMARK 210 CONCENTRATION), 3 MM ZINC REMARK 210 ACETATE, 10 MM CACL2, 0.34 MM REMARK 210 NAN3, 15 MM NACL, <0.07 MM DTT, REMARK 210 10 MM TES, 10% D2O; 3 MM 15N,13C REMARK 210 S100B (MONOMER CONCENTRATION), 3 REMARK 210 MM ZINC ACETATE, 10 MM CACL2, REMARK 210 0.34 MM NAN3, 15 MM NACL, <0.07 REMARK 210 MM DTT, 10 MM TES, 10% D2O; 1 MM REMARK 210 15N S100B (MONOMER CONCENTRATION) REMARK 210 , 1 MM ZINC ACETATE, 3.3 MM REMARK 210 CACL2, 0.34 MM NAN3, 15 MM NACL, REMARK 210 <0.07 MM DTT, 10 MM TES, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : FAST HSQC; 3D_15N REMARK 210 -SEPARATED_NOESY; 3D_15N-EDITED REMARK 210 HOHAHA-HSQC; 3D_15N,15N-EDITED REMARK 210 HMQC-NOESY-HSQC; HNHA; 3D REMARK 210 CBCA(CO)NH; LONG RANGE HSQC; 3D REMARK 210 HNCA, 3D HNCO, AND 3D HNCACB; 4D_ REMARK 210 13C-SEPARATED_NOESY; 4D_13C/15N- REMARK 210 SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DMX; AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 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 : 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 10 H PHE A 14 1.40 REMARK 500 O LEU B 10 H PHE B 14 1.40 REMARK 500 OD2 ASP B 61 H GLY B 66 1.40 REMARK 500 OD2 ASP A 61 H GLY A 66 1.40 REMARK 500 O VAL B 77 HG1 THR B 81 1.42 REMARK 500 O VAL A 52 H VAL A 56 1.50 REMARK 500 O VAL B 52 H VAL B 56 1.50 REMARK 500 O GLU A 31 H LEU A 35 1.52 REMARK 500 O GLU B 31 H LEU B 35 1.52 REMARK 500 O SER A 1 H GLU A 4 1.55 REMARK 500 O VAL B 77 H THR B 81 1.55 REMARK 500 O SER B 1 H GLU B 4 1.55 REMARK 500 O VAL A 77 H THR A 81 1.55 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 24 -7.58 -179.59 REMARK 500 1 HIS A 25 47.79 -153.93 REMARK 500 1 SER A 30 -10.79 -49.01 REMARK 500 1 GLU A 39 -69.95 -100.16 REMARK 500 1 LEU A 40 37.81 -76.19 REMARK 500 1 ASP A 69 -169.91 -53.00 REMARK 500 1 LYS B 24 -7.55 -179.63 REMARK 500 1 HIS B 25 47.73 -153.90 REMARK 500 1 SER B 30 -10.80 -48.92 REMARK 500 1 GLU B 39 -69.98 -100.16 REMARK 500 1 LEU B 40 37.88 -76.19 REMARK 500 1 ASP B 69 -170.04 -53.07 REMARK 500 2 LYS A 24 -42.80 -179.66 REMARK 500 2 SER A 30 -11.60 -48.85 REMARK 500 2 GLU A 39 -61.10 -102.39 REMARK 500 2 LEU A 40 34.96 -78.11 REMARK 500 2 ASP A 61 108.86 -55.04 REMARK 500 2 ASP A 69 -176.36 -51.76 REMARK 500 2 HIS A 90 102.26 -57.70 REMARK 500 2 LYS B 24 -42.85 -179.74 REMARK 500 2 SER B 30 -11.29 -49.07 REMARK 500 2 GLU B 39 -60.88 -102.30 REMARK 500 2 LEU B 40 34.97 -78.25 REMARK 500 2 ASP B 61 108.74 -54.98 REMARK 500 2 ASP B 69 -176.22 -52.01 REMARK 500 2 HIS B 90 102.09 -57.63 REMARK 500 3 LYS A 24 144.31 169.13 REMARK 500 3 LEU A 40 31.60 -75.11 REMARK 500 3 ASP A 61 98.87 -55.41 REMARK 500 3 ASP A 69 -175.13 -53.05 REMARK 500 3 GLU A 89 47.22 -82.74 REMARK 500 3 LYS B 24 144.22 168.65 REMARK 500 3 LEU B 40 31.00 -74.60 REMARK 500 3 ASP B 61 99.13 -55.60 REMARK 500 3 ASP B 69 -175.25 -53.00 REMARK 500 3 GLU B 89 47.14 -82.67 REMARK 500 4 ASP A 23 -93.81 -49.52 REMARK 500 4 LYS A 24 -8.95 -171.95 REMARK 500 4 HIS A 25 35.02 -142.92 REMARK 500 4 SER A 30 -15.76 -49.80 REMARK 500 4 GLU A 39 -69.53 -99.35 REMARK 500 4 LEU A 40 38.92 -73.91 REMARK 500 4 GLU A 46 84.83 -55.51 REMARK 500 4 ASP A 61 96.08 -55.97 REMARK 500 4 ASP A 69 -173.56 -52.49 REMARK 500 4 GLU A 89 20.75 -71.96 REMARK 500 4 ASP B 23 -93.97 -49.75 REMARK 500 4 LYS B 24 -8.93 -171.77 REMARK 500 4 HIS B 25 34.97 -142.76 REMARK 500 4 SER B 30 -15.78 -49.60 REMARK 500 REMARK 500 THIS ENTRY HAS 284 RAMACHANDRAN OUTLIERS. 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 ZN A 94 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 15 NE2 REMARK 620 2 HIS A 25 ND1 107.9 REMARK 620 3 HIS B 85 NE2 124.7 115.3 REMARK 620 4 GLU B 89 OE1 114.6 118.2 72.9 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 92 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER A 18 O REMARK 620 2 GLU A 21 O 69.8 REMARK 620 3 LYS A 26 O 70.2 110.0 REMARK 620 4 GLU A 31 OE2 129.5 111.1 138.6 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 93 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 61 OD1 REMARK 620 2 ASP A 63 OD1 50.7 REMARK 620 3 ASP A 63 OD2 88.3 39.2 REMARK 620 4 ASP A 65 OD2 99.2 66.3 61.9 REMARK 620 5 ASP A 65 OD1 58.4 64.6 92.4 51.4 REMARK 620 6 GLU A 67 O 94.8 122.4 140.9 79.2 57.7 REMARK 620 7 GLU A 72 OE1 93.0 106.7 96.9 154.8 149.7 121.7 REMARK 620 8 GLU A 72 OE2 148.7 128.2 90.8 107.9 152.8 105.2 56.0 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN B 94 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 85 NE2 REMARK 620 2 GLU A 89 OE1 73.1 REMARK 620 3 HIS B 15 NE2 124.0 113.9 REMARK 620 4 HIS B 25 ND1 115.8 118.8 108.1 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B 92 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER B 18 O REMARK 620 2 GLU B 21 O 83.0 REMARK 620 3 LYS B 26 O 69.9 107.3 REMARK 620 4 GLU B 31 OE2 147.6 122.2 114.7 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B 93 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 61 OD1 REMARK 620 2 ASP B 63 OD1 66.0 REMARK 620 3 ASP B 65 OD1 71.6 80.4 REMARK 620 4 ASP B 65 OD2 119.8 78.1 55.5 REMARK 620 5 GLU B 67 O 100.9 137.0 56.8 74.1 REMARK 620 6 GLU B 72 OE1 100.9 119.7 154.4 139.2 102.7 REMARK 620 7 GLU B 72 OE2 147.1 130.4 133.0 92.8 83.5 47.0 REMARK 620 N 1 2 3 4 5 6 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 92 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 93 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 94 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 92 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 93 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 94 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1QLK RELATED DB: PDB REMARK 900 NMR SOLUTION STRUCTURE OF RAT CA2+-S100B REMARK 900 RELATED ID: 1B4C RELATED DB: PDB REMARK 900 NMR SOLUTION STRUCTURE OF RAT APO-S100B USING DIPOLAR COUPLING REMARK 900 RELATED ID: 1DT7 RELATED DB: PDB REMARK 900 NMR SOLUTION STRUCTURE OF RAT CA2+-S100B WITH C-TERMINAL NEGATIVE REMARK 900 REGULATORY DOMAIN OF P53 REMARK 900 RELATED ID: 1MWN RELATED DB: PDB REMARK 900 NMR SOLUTION STRUCTURE OF RAT CA2+-S100B WITH THE TRTK-12 PEPTIDE REMARK 900 RELATED ID: 3PSR RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF ZN2+-CA2+-S100A7 REMARK 900 RELATED ID: 1ODB RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF CU2+-CA2+-S100A12 DBREF 1XYD A 0 91 UNP P04631 S100B_RAT 0 91 DBREF 1XYD B 0 91 UNP P04631 S100B_RAT 0 91 SEQRES 1 A 92 MET SER GLU LEU GLU LYS ALA MET VAL ALA LEU ILE ASP SEQRES 2 A 92 VAL PHE HIS GLN TYR SER GLY ARG GLU GLY ASP LYS HIS SEQRES 3 A 92 LYS LEU LYS LYS SER GLU LEU LYS GLU LEU ILE ASN ASN SEQRES 4 A 92 GLU LEU SER HIS PHE LEU GLU GLU ILE LYS GLU GLN GLU SEQRES 5 A 92 VAL VAL ASP LYS VAL MET GLU THR LEU ASP GLU ASP GLY SEQRES 6 A 92 ASP GLY GLU CYS ASP PHE GLN GLU PHE MET ALA PHE VAL SEQRES 7 A 92 SER MET VAL THR THR ALA CYS HIS GLU PHE PHE GLU HIS SEQRES 8 A 92 GLU SEQRES 1 B 92 MET SER GLU LEU GLU LYS ALA MET VAL ALA LEU ILE ASP SEQRES 2 B 92 VAL PHE HIS GLN TYR SER GLY ARG GLU GLY ASP LYS HIS SEQRES 3 B 92 LYS LEU LYS LYS SER GLU LEU LYS GLU LEU ILE ASN ASN SEQRES 4 B 92 GLU LEU SER HIS PHE LEU GLU GLU ILE LYS GLU GLN GLU SEQRES 5 B 92 VAL VAL ASP LYS VAL MET GLU THR LEU ASP GLU ASP GLY SEQRES 6 B 92 ASP GLY GLU CYS ASP PHE GLN GLU PHE MET ALA PHE VAL SEQRES 7 B 92 SER MET VAL THR THR ALA CYS HIS GLU PHE PHE GLU HIS SEQRES 8 B 92 GLU HET CA A 92 1 HET CA A 93 1 HET ZN A 94 1 HET CA B 92 1 HET CA B 93 1 HET ZN B 94 1 HETNAM CA CALCIUM ION HETNAM ZN ZINC ION FORMUL 3 CA 4(CA 2+) FORMUL 5 ZN 2(ZN 2+) HELIX 1 1 GLU A 2 ARG A 20 1 19 HELIX 2 2 LYS A 29 ASN A 38 1 10 HELIX 3 3 GLN A 50 ASP A 61 1 12 HELIX 4 4 PHE A 70 PHE A 88 1 19 HELIX 5 5 GLU B 2 ARG B 20 1 19 HELIX 6 6 LYS B 29 ASN B 38 1 10 HELIX 7 7 GLN B 50 ASP B 61 1 12 HELIX 8 8 PHE B 70 PHE B 88 1 19 SHEET 1 A 2 LYS A 26 LYS A 28 0 SHEET 2 A 2 GLU A 67 ASP A 69 -1 O CYS A 68 N LEU A 27 SHEET 1 B 2 LYS B 26 LYS B 28 0 SHEET 2 B 2 GLU B 67 ASP B 69 -1 O CYS B 68 N LEU B 27 LINK NE2 HIS A 15 ZN ZN A 94 1555 1555 2.03 LINK O SER A 18 CA CA A 92 1555 1555 2.81 LINK O GLU A 21 CA CA A 92 1555 1555 2.77 LINK ND1 HIS A 25 ZN ZN A 94 1555 1555 2.03 LINK O LYS A 26 CA CA A 92 1555 1555 2.13 LINK OE2 GLU A 31 CA CA A 92 1555 1555 2.76 LINK OD1 ASP A 61 CA CA A 93 1555 1555 2.62 LINK OD1 ASP A 63 CA CA A 93 1555 1555 2.90 LINK OD2 ASP A 63 CA CA A 93 1555 1555 3.38 LINK OD2 ASP A 65 CA CA A 93 1555 1555 2.43 LINK OD1 ASP A 65 CA CA A 93 1555 1555 2.53 LINK O GLU A 67 CA CA A 93 1555 1555 2.37 LINK OE1 GLU A 72 CA CA A 93 1555 1555 2.38 LINK OE2 GLU A 72 CA CA A 93 1555 1555 2.19 LINK NE2 HIS A 85 ZN ZN B 94 1555 1555 2.01 LINK OE1 GLU A 89 ZN ZN B 94 1555 1555 2.10 LINK ZN ZN A 94 NE2 HIS B 85 1555 1555 2.02 LINK ZN ZN A 94 OE1 GLU B 89 1555 1555 2.11 LINK NE2 HIS B 15 ZN ZN B 94 1555 1555 2.03 LINK O SER B 18 CA CA B 92 1555 1555 2.43 LINK O GLU B 21 CA CA B 92 1555 1555 2.39 LINK ND1 HIS B 25 ZN ZN B 94 1555 1555 2.02 LINK O LYS B 26 CA CA B 92 1555 1555 2.62 LINK OE2 GLU B 31 CA CA B 92 1555 1555 2.82 LINK OD1 ASP B 61 CA CA B 93 1555 1555 2.06 LINK OD1 ASP B 63 CA CA B 93 1555 1555 2.29 LINK OD1 ASP B 65 CA CA B 93 1555 1555 2.24 LINK OD2 ASP B 65 CA CA B 93 1555 1555 2.38 LINK O GLU B 67 CA CA B 93 1555 1555 2.68 LINK OE1 GLU B 72 CA CA B 93 1555 1555 2.63 LINK OE2 GLU B 72 CA CA B 93 1555 1555 2.77 SITE 1 AC1 6 TYR A 17 SER A 18 GLU A 21 LYS A 26 SITE 2 AC1 6 LYS A 28 GLU A 31 SITE 1 AC2 5 ASP A 61 ASP A 63 ASP A 65 GLU A 67 SITE 2 AC2 5 GLU A 72 SITE 1 AC3 5 HIS A 15 LYS A 24 HIS A 25 HIS B 85 SITE 2 AC3 5 GLU B 89 SITE 1 AC4 5 TYR B 17 SER B 18 GLU B 21 LYS B 26 SITE 2 AC4 5 GLU B 31 SITE 1 AC5 5 ASP B 61 ASP B 63 ASP B 65 GLU B 67 SITE 2 AC5 5 GLU B 72 SITE 1 AC6 5 HIS A 85 GLU A 89 HIS B 15 LYS B 24 SITE 2 AC6 5 HIS B 25 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 - r 2 2 Bytes