Header list of 1s6i.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE, PLANT PROTEIN 23-JAN-04 1S6I TITLE CA2+-REGULATORY REGION (CLD) FROM SOYBEAN CALCIUM-DEPENDENT PROTEIN TITLE 2 KINASE-ALPHA (CDPK) IN THE PRESENCE OF CA2+ AND THE JUNCTION DOMAIN TITLE 3 (JD) COMPND MOL_ID: 1; COMPND 2 MOLECULE: CALCIUM-DEPENDENT PROTEIN KINASE SK5; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CALMODULIN-LIKE DOMAIN (CLD) AND C-TERMINAL TAIL; COMPND 5 SYNONYM: CDPK; CALCIUM-DEPENDENT PROTEIN KINASE-ALPHA; COMPND 6 EC: 2.7.1.-; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GLYCINE MAX; SOURCE 3 ORGANISM_COMMON: SOYBEAN; SOURCE 4 ORGANISM_TAXID: 3847; SOURCE 5 GENE: CDPK SK5; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PT7-7; SOURCE 11 OTHER_DETAILS: CA2+-BINDING REGION AND C-TERMINAL TAIL, ALONG WITH SOURCE 12 HIS(6) AT C-TERMINUS KEYWDS EF-HAND; HELIX-LOOP-HELIX; CALCIUM-BINDING; CALMODULIN SUPERFAMILY, KEYWDS 2 TRANSFERASE, PLANT PROTEIN EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR A.M.WELJIE,H.J.VOGEL REVDAT 4 02-MAR-22 1S6I 1 REMARK SEQADV LINK REVDAT 3 24-FEB-09 1S6I 1 VERSN REVDAT 2 21-DEC-04 1S6I 1 JRNL REMARK REVDAT 1 15-JUN-04 1S6I 0 JRNL AUTH A.M.WELJIE,H.J.VOGEL JRNL TITL UNEXPECTED STRUCTURE OF THE CA2+-REGULATORY REGION FROM JRNL TITL 2 SOYBEAN CALCIUM-DEPENDENT PROTEIN KINASE-ALPHA JRNL REF J.BIOL.CHEM. V. 279 35494 2004 JRNL REFN ISSN 0021-9258 JRNL PMID 15155727 JRNL DOI 10.1074/JBC.M311520200 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.M.WELJIE,K.M.ROBERTSON,H.J.VOGEL REMARK 1 TITL CONFORMATIONAL CHANGES IN THE CA2+-REGULATORY REGION FROM REMARK 1 TITL 2 SOYBEAN CALCIUM-DEPENDENT PROTEIN KINASE-ALPHA: FLUORESCENCE REMARK 1 TITL 3 RESONANCE ENERGY TRANSFER STUDIES REMARK 1 REF J.BIOL.CHEM. V. 278 43764 2003 REMARK 1 REFN ISSN 0021-9258 REMARK 1 REFERENCE 2 REMARK 1 AUTH A.M.WELJIE,S.M.GAGNE,H.J.VOGEL REMARK 1 TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF THE N-TERMINAL REMARK 1 TITL 2 REGION OF THE CALCIUM REGULATORY DOMAIN FROM SOYBEAN REMARK 1 TITL 3 CALCIUM-DEPENDENT PROTEIN KINASE ALPHA REMARK 1 REF BIOCHEMISTRY V. 42 15131 2004 REMARK 1 REFN ISSN 0006-2960 REMARK 1 PMID 15568805 REMARK 1 DOI 10.1021/BI048751R REMARK 1 REFERENCE 3 REMARK 1 AUTH J.F.HARPER,M.R.SUSSMAN,G.E.SCHALLER,C.PUTNAM-EVANS, REMARK 1 AUTH 2 H.CHARBONNEAU,A.C.HARMON REMARK 1 TITL A CALCIUM-DEPENDENT PROTEIN KINASE WITH A REGULATORY DOMAIN REMARK 1 TITL 2 SIMILAR TO CALMODULIN REMARK 1 REF SCIENCE V. 252 951 1991 REMARK 1 REFN ISSN 0036-8075 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.1 REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 BASED ON 3051 UNAMBIGUOUS NOE-DERIVED RESTRAINTS, 1183 AMBIGUOUS REMARK 3 NOE-DERIVED RESTRAINTS, REMARK 3 122 DIHEDRAL ANGLE RESTRAINTS (TALOS DERIVED), 45 HN RESIDUAL REMARK 3 DIPOLAR COUPLING RESTRAINTS REMARK 4 REMARK 4 1S6I COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-04. REMARK 100 THE DEPOSITION ID IS D_1000021428. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 313; 313 REMARK 210 PH : 7.3; 7.3 REMARK 210 IONIC STRENGTH : 200 MM NACL, 10 MM CACL2, 50 MM REMARK 210 H2-IMIDAZOLE; 150 MM NACL, 10 MM REMARK 210 CACL2, 50 MM H2-IMIDAZOLE REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 0.8 MM U-15N,13C CLD; 0.9 MM REMARK 210 UNLABELLED JD PEPTIDE; 50 MM H2- REMARK 210 IMIDAZOLE, PH 7.3; 150 MM NACL; REMARK 210 10 MM CACL2; 95% H2O, 5% D2O; REMARK 210 0.5 MM U-15N CLD; 0.6 MM REMARK 210 UNLABELLED JD PEPTIDE; 50 MM H2- REMARK 210 IMIDAZOLE, PH 7.3; 200 MM NACL; REMARK 210 10 MM CACL2; 95% H2O, 5% D2O; REMARK 210 0.5 MM UNLABELLED CLD; 0.6 MM REMARK 210 UNLABELLED JD PEPTIDE; 50 MM H2- REMARK 210 IMIDAZOLE, PH 7.3; 200 MM NACL, REMARK 210 10 MM CACL2; 95% H2O, 5% D2O; REMARK 210 0.4 MM U-15N CLD; 50 MM H2- REMARK 210 IMIDAZOLE, PH 7.3; 200 MM NACL; REMARK 210 10 MM CACL2; 95% H2O, 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA; AVANCE REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.1, NMRVIEW 5.04, CNS REMARK 210 1.1, ARIA 1.2, VNMR UNKNOWN REMARK 210 METHOD USED : SIMULATED ANNEALING; MOLECULAR REMARK 210 DYNAMICS; MATRIX RELAXATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE REMARK 210 COVALENT GEOMETRY,STRUCTURES REMARK 210 WITH FAVORABLE NON-BOND ENERGY, REMARK 210 STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY 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 1-15 REMARK 465 RES C SSSEQI REMARK 465 HIS A 183 REMARK 465 HIS A 184 REMARK 465 HIS A 185 REMARK 465 HIS A 186 REMARK 465 HIS A 187 REMARK 465 HIS A 188 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 H ASP A 134 HB2 GLU A 137 1.22 REMARK 500 HE21 GLN A 127 HG2 GLU A 137 1.23 REMARK 500 HA MET A 121 HB3 GLU A 124 1.29 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 ARG A 3 115.91 -162.18 REMARK 500 1 LEU A 4 -43.43 -159.63 REMARK 500 1 GLU A 6 41.96 -109.33 REMARK 500 1 ASN A 23 -87.07 -74.42 REMARK 500 1 SER A 24 6.59 -176.66 REMARK 500 1 PHE A 29 -36.40 -34.09 REMARK 500 1 ASP A 34 -36.17 -36.34 REMARK 500 1 SER A 46 -34.99 -39.47 REMARK 500 1 ASP A 56 95.98 -61.24 REMARK 500 1 LYS A 59 90.38 -32.57 REMARK 500 1 ASN A 76 75.28 -102.78 REMARK 500 1 LYS A 77 -156.27 -175.40 REMARK 500 1 GLU A 81 38.89 -165.81 REMARK 500 1 ASN A 83 -155.98 -109.05 REMARK 500 1 LEU A 101 -33.91 -34.44 REMARK 500 1 LEU A 113 132.74 -33.09 REMARK 500 1 ILE A 116 -64.12 -92.59 REMARK 500 1 ASP A 126 98.37 -62.80 REMARK 500 1 ASN A 129 -71.76 179.96 REMARK 500 1 ASP A 130 18.83 -64.92 REMARK 500 1 TYR A 135 -30.48 -38.76 REMARK 500 1 MET A 142 -31.13 -134.97 REMARK 500 1 ARG A 143 -137.62 -112.11 REMARK 500 1 ARG A 145 78.32 -101.29 REMARK 500 1 ARG A 153 170.55 -53.78 REMARK 500 1 THR A 155 80.15 -50.23 REMARK 500 1 MET A 156 -18.64 -175.90 REMARK 500 1 LYS A 158 -87.23 -161.49 REMARK 500 1 THR A 159 -36.42 -162.96 REMARK 500 1 ASN A 161 -101.17 -103.96 REMARK 500 2 ASN A 23 -82.45 -69.82 REMARK 500 2 SER A 24 5.42 -175.91 REMARK 500 2 PHE A 29 -27.87 -34.03 REMARK 500 2 SER A 46 -18.76 -41.73 REMARK 500 2 ASP A 56 97.05 -49.39 REMARK 500 2 LYS A 59 88.03 -30.94 REMARK 500 2 LYS A 77 -153.91 -174.42 REMARK 500 2 LEU A 78 62.27 -100.78 REMARK 500 2 GLU A 82 90.47 -174.99 REMARK 500 2 SER A 96 -9.07 -55.37 REMARK 500 2 LEU A 101 -39.03 -35.47 REMARK 500 2 CYS A 108 76.31 -64.40 REMARK 500 2 LEU A 113 144.50 -34.06 REMARK 500 2 ASP A 114 -164.06 -160.16 REMARK 500 2 HIS A 117 -68.51 -92.06 REMARK 500 2 ASN A 129 -80.89 179.63 REMARK 500 2 LYS A 144 -153.53 -128.91 REMARK 500 2 LYS A 158 -45.45 -164.97 REMARK 500 2 THR A 159 2.84 -152.05 REMARK 500 2 SER A 173 -35.34 -151.16 REMARK 500 REMARK 500 THIS ENTRY HAS 397 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 CA A 189 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 THR A 26 O REMARK 620 2 GLU A 31 OE2 130.0 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 190 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 58 O REMARK 620 2 SER A 60 OG 64.7 REMARK 620 3 THR A 62 O 100.6 83.4 REMARK 620 4 GLU A 67 OE1 87.8 122.8 52.1 REMARK 620 5 GLU A 67 OE2 90.6 153.8 93.6 43.1 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 191 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER A 96 OG REMARK 620 2 TYR A 98 O 92.6 REMARK 620 3 GLU A 103 OE1 168.8 83.5 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 192 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 126 OD1 REMARK 620 2 ASP A 128 OD1 83.2 REMARK 620 3 ASP A 130 N 68.6 87.0 REMARK 620 4 GLY A 131 N 58.1 132.5 55.4 REMARK 620 5 GLN A 132 N 93.2 166.3 104.0 53.2 REMARK 620 6 GLN A 132 O 101.5 110.5 159.3 103.9 57.2 REMARK 620 7 GLU A 137 OE2 85.9 54.9 136.9 136.2 111.8 56.4 REMARK 620 8 GLU A 137 OE1 129.7 70.4 146.4 155.6 102.6 53.8 43.9 REMARK 620 N 1 2 3 4 5 6 7 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 189 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 190 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 191 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 192 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1S6J RELATED DB: PDB REMARK 900 N-TERMINAL REGION OF THE CA2+-SATURATED CALCIUM REGULATORY DOMAIN REMARK 900 (CLD) FROM SOYBEAN CALCIUM-DEPENDENT PROTEIN KINASE-ALPHA (CDPK) DBREF 1S6I A 1 182 UNP P28583 CDPK_SOYBN 329 508 SEQADV 1S6I ARG A 143 UNP P28583 INSERTION SEQADV 1S6I LYS A 144 UNP P28583 INSERTION SEQADV 1S6I HIS A 183 UNP P28583 EXPRESSION TAG SEQADV 1S6I HIS A 184 UNP P28583 EXPRESSION TAG SEQADV 1S6I HIS A 185 UNP P28583 EXPRESSION TAG SEQADV 1S6I HIS A 186 UNP P28583 EXPRESSION TAG SEQADV 1S6I HIS A 187 UNP P28583 EXPRESSION TAG SEQADV 1S6I HIS A 188 UNP P28583 EXPRESSION TAG SEQRES 1 A 188 ALA GLU ARG LEU SER GLU GLU GLU ILE GLY GLY LEU LYS SEQRES 2 A 188 GLU LEU PHE LYS MET ILE ASP THR ASP ASN SER GLY THR SEQRES 3 A 188 ILE THR PHE ASP GLU LEU LYS ASP GLY LEU LYS ARG VAL SEQRES 4 A 188 GLY SER GLU LEU MET GLU SER GLU ILE LYS ASP LEU MET SEQRES 5 A 188 ASP ALA ALA ASP ILE ASP LYS SER GLY THR ILE ASP TYR SEQRES 6 A 188 GLY GLU PHE ILE ALA ALA THR VAL HIS LEU ASN LYS LEU SEQRES 7 A 188 GLU ARG GLU GLU ASN LEU VAL SER ALA PHE SER TYR PHE SEQRES 8 A 188 ASP LYS ASP GLY SER GLY TYR ILE THR LEU ASP GLU ILE SEQRES 9 A 188 GLN GLN ALA CYS LYS ASP PHE GLY LEU ASP ASP ILE HIS SEQRES 10 A 188 ILE ASP ASP MET ILE LYS GLU ILE ASP GLN ASP ASN ASP SEQRES 11 A 188 GLY GLN ILE ASP TYR GLY GLU PHE ALA ALA MET MET ARG SEQRES 12 A 188 LYS ARG LYS GLY ASN GLY GLY ILE GLY ARG ARG THR MET SEQRES 13 A 188 ARG LYS THR LEU ASN LEU ARG ASP ALA LEU GLY LEU VAL SEQRES 14 A 188 ASP ASN GLY SER ASN GLN VAL ILE GLU GLY TYR PHE LYS SEQRES 15 A 188 HIS HIS HIS HIS HIS HIS HET CA A 189 1 HET CA A 190 1 HET CA A 191 1 HET CA A 192 1 HETNAM CA CALCIUM ION FORMUL 2 CA 4(CA 2+) HELIX 1 1 GLY A 11 MET A 18 1 8 HELIX 2 2 PHE A 29 LYS A 37 1 9 HELIX 3 3 MET A 44 ALA A 55 1 12 HELIX 4 4 ASP A 64 VAL A 73 1 10 HELIX 5 5 LEU A 84 PHE A 91 1 8 HELIX 6 6 LEU A 101 ALA A 107 1 7 HELIX 7 7 ILE A 116 ASP A 126 1 11 HELIX 8 8 GLY A 136 MET A 141 1 6 SHEET 1 A 2 ILE A 27 THR A 28 0 SHEET 2 A 2 THR A 62 ILE A 63 -1 O ILE A 63 N ILE A 27 SHEET 1 B 2 TYR A 98 THR A 100 0 SHEET 2 B 2 GLN A 132 ASP A 134 -1 O ILE A 133 N ILE A 99 LINK O THR A 26 CA CA A 189 1555 1555 2.42 LINK OE2 GLU A 31 CA CA A 189 1555 1555 2.90 LINK O ASP A 58 CA CA A 190 1555 1555 3.27 LINK OG SER A 60 CA CA A 190 1555 1555 2.50 LINK O THR A 62 CA CA A 190 1555 1555 2.79 LINK OE1 GLU A 67 CA CA A 190 1555 1555 3.21 LINK OE2 GLU A 67 CA CA A 190 1555 1555 2.47 LINK OG SER A 96 CA CA A 191 1555 1555 2.84 LINK O TYR A 98 CA CA A 191 1555 1555 2.38 LINK OE1 GLU A 103 CA CA A 191 1555 1555 2.97 LINK OD1 ASP A 126 CA CA A 192 1555 1555 2.25 LINK OD1 ASP A 128 CA CA A 192 1555 1555 2.75 LINK N ASP A 130 CA CA A 192 1555 1555 3.13 LINK N GLY A 131 CA CA A 192 1555 1555 3.18 LINK N GLN A 132 CA CA A 192 1555 1555 2.72 LINK O GLN A 132 CA CA A 192 1555 1555 2.80 LINK OE2 GLU A 137 CA CA A 192 1555 1555 2.36 LINK OE1 GLU A 137 CA CA A 192 1555 1555 3.17 SITE 1 AC1 4 ASP A 20 ASN A 23 THR A 26 GLU A 31 SITE 1 AC2 4 ASP A 58 SER A 60 THR A 62 GLU A 67 SITE 1 AC3 4 ASP A 94 SER A 96 TYR A 98 GLU A 103 SITE 1 AC4 7 ASP A 126 ASP A 128 ASN A 129 ASP A 130 SITE 2 AC4 7 GLY A 131 GLN A 132 GLU A 137 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