Header list of 1tnx.pdb file
Complete list - 2 20 Bytes
HEADER CALCIUM-BINDING PROTEIN 23-AUG-95 1TNX TITLE NMR SOLUTION STRUCTURE OF CALCIUM SATURATED SKELETAL MUSCLE TROPONIN C COMPND MOL_ID: 1; COMPND 2 MOLECULE: TROPONIN C; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS; SOURCE 3 ORGANISM_COMMON: CHICKEN; SOURCE 4 ORGANISM_TAXID: 9031; SOURCE 5 ORGAN: SKELETAL; SOURCE 6 TISSUE: SKELETAL MUSCLE; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3A-TNC KEYWDS EF-HAND, CALCIUM-BINDING PROTEIN EXPDTA SOLUTION NMR AUTHOR C.M.SLUPSKY,B.D.SYKES REVDAT 3 02-MAR-22 1TNX 1 REMARK REVDAT 2 24-FEB-09 1TNX 1 VERSN REVDAT 1 15-OCT-95 1TNX 0 JRNL AUTH C.M.SLUPSKY,B.D.SYKES JRNL TITL NMR SOLUTION STRUCTURE OF CALCIUM-SATURATED SKELETAL MUSCLE JRNL TITL 2 TROPONIN C. JRNL REF BIOCHEMISTRY V. 34 15953 1995 JRNL REFN ISSN 0006-2960 JRNL PMID 8519752 JRNL DOI 10.1021/BI00049A010 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.M.SLUPSKY,F.C.REINACH,L.B.SMILLIE,B.D.SYKES REMARK 1 TITL SOLUTION SECONDARY STRUCTURE OF CALCIUM SATURATED TROPONIN C REMARK 1 TITL 2 MONOMER DETERMINED BY MULTIDIMENSIONAL HETERONUCLEAR NMR REMARK 1 TITL 3 SPECTROSCOPY REMARK 1 REF PROTEIN SCI. V. 4 1279 1995 REMARK 1 REFN ISSN 0961-8368 REMARK 1 REFERENCE 2 REMARK 1 AUTH C.M.SLUPSKY,C.M.KAY,F.C.REINACH,L.B.SMILLIE,B.D.SYKES REMARK 1 TITL CALCIUM-INDUCED DIMERIZATION OF TROPONIN C: MODE OF REMARK 1 TITL 2 INTERACTION AND USE OF TRIFLUOROETHANOL AS A DENATURANT OF REMARK 1 TITL 3 QUATERNARY STRUCTURE REMARK 1 REF BIOCHEMISTRY V. 34 7365 1995 REMARK 1 REFN ISSN 0006-2960 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 1TNX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000176765. 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 : 1 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 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 RES C SSSEQI REMARK 465 ALA A 1 REMARK 465 SER A 2 REMARK 465 MET A 3 REMARK 465 THR A 4 REMARK 465 MET A 86 REMARK 465 LYS A 87 REMARK 465 GLU A 88 REMARK 465 ASP A 89 REMARK 465 ALA A 90 REMARK 465 LYS A 91 REMARK 465 GLY A 92 REMARK 465 LYS A 93 REMARK 465 SER A 94 REMARK 465 GLU A 159 REMARK 465 GLY A 160 REMARK 465 VAL A 161 REMARK 465 GLN A 162 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 GLY A 34 N GLY A 35 0.77 REMARK 500 C GLY A 34 H GLY A 35 1.41 REMARK 500 O GLU A 127 N HIS A 128 1.46 REMARK 500 O GLY A 33 N GLY A 34 1.72 REMARK 500 REMARK 500 REMARK: NULL 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 GLU A 9 CD GLU A 9 OE2 0.108 REMARK 500 ARG A 11 CZ ARG A 11 NH2 -0.111 REMARK 500 GLU A 16 CD GLU A 16 OE2 0.113 REMARK 500 GLU A 17 CD GLU A 17 OE2 0.102 REMARK 500 GLU A 21 CD GLU A 21 OE2 0.107 REMARK 500 ASP A 32 C ASP A 32 O -0.123 REMARK 500 GLY A 33 CA GLY A 33 C -0.158 REMARK 500 GLY A 33 C GLY A 33 O -0.385 REMARK 500 GLY A 33 C GLY A 34 N -0.155 REMARK 500 GLY A 34 N GLY A 34 CA -0.114 REMARK 500 GLY A 34 C GLY A 34 O -0.675 REMARK 500 GLY A 34 C GLY A 35 N -0.477 REMARK 500 GLU A 41 CD GLU A 41 OE2 0.105 REMARK 500 ARG A 47 CZ ARG A 47 NH2 -0.088 REMARK 500 GLN A 51 C GLN A 51 O -0.120 REMARK 500 GLU A 56 CD GLU A 56 OE2 0.110 REMARK 500 GLU A 57 CD GLU A 57 OE2 0.101 REMARK 500 GLU A 63 CD GLU A 63 OE2 0.112 REMARK 500 GLU A 64 CD GLU A 64 OE2 0.100 REMARK 500 GLU A 67 CD GLU A 67 OE2 0.111 REMARK 500 SER A 70 C SER A 70 O -0.138 REMARK 500 GLU A 76 CD GLU A 76 OE2 0.102 REMARK 500 GLU A 77 CD GLU A 77 OE2 0.096 REMARK 500 GLU A 95 N GLU A 95 CA -0.244 REMARK 500 GLU A 95 CD GLU A 95 OE2 0.111 REMARK 500 GLU A 96 CD GLU A 96 OE2 0.108 REMARK 500 GLU A 97 CD GLU A 97 OE2 0.106 REMARK 500 ARG A 103 CZ ARG A 103 NH1 -0.094 REMARK 500 ARG A 103 CZ ARG A 103 NH2 -0.110 REMARK 500 GLU A 116 CD GLU A 116 OE2 0.103 REMARK 500 GLU A 117 CD GLU A 117 OE2 0.111 REMARK 500 LEU A 118 C LEU A 118 O -0.121 REMARK 500 GLU A 120 CD GLU A 120 OE2 0.104 REMARK 500 GLU A 127 CD GLU A 127 OE2 0.105 REMARK 500 GLU A 127 C GLU A 127 O -0.362 REMARK 500 GLU A 127 C HIS A 128 N -0.319 REMARK 500 GLU A 131 CD GLU A 131 OE2 0.104 REMARK 500 GLU A 132 CD GLU A 132 OE2 0.102 REMARK 500 GLU A 135 CD GLU A 135 OE2 0.109 REMARK 500 ARG A 148 CZ ARG A 148 NH2 -0.109 REMARK 500 GLU A 153 CD GLU A 153 OE2 0.098 REMARK 500 MET A 158 CA MET A 158 C -0.206 REMARK 500 MET A 158 C MET A 158 O -0.473 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 ASP A 5 CB - CG - OD2 ANGL. DEV. = -6.9 DEGREES REMARK 500 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 9.2 DEGREES REMARK 500 ARG A 11 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES REMARK 500 ASP A 27 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES REMARK 500 ASP A 27 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES REMARK 500 MET A 28 N - CA - CB ANGL. DEV. = 14.3 DEGREES REMARK 500 ASP A 32 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES REMARK 500 ASP A 32 CB - CG - OD2 ANGL. DEV. = -7.9 DEGREES REMARK 500 GLY A 33 CA - C - N ANGL. DEV. = 15.9 DEGREES REMARK 500 GLY A 34 C - N - CA ANGL. DEV. = 12.6 DEGREES REMARK 500 GLY A 34 CA - C - O ANGL. DEV. = 23.2 DEGREES REMARK 500 GLY A 34 CA - C - N ANGL. DEV. = 38.2 DEGREES REMARK 500 GLY A 34 O - C - N ANGL. DEV. = -61.4 DEGREES REMARK 500 GLY A 35 C - N - CA ANGL. DEV. = 33.2 DEGREES REMARK 500 ASP A 36 CB - CG - OD2 ANGL. DEV. = -7.4 DEGREES REMARK 500 LYS A 40 N - CA - CB ANGL. DEV. = 16.9 DEGREES REMARK 500 LEU A 42 CB - CG - CD2 ANGL. DEV. = 17.2 DEGREES REMARK 500 ARG A 47 CG - CD - NE ANGL. DEV. = -12.9 DEGREES REMARK 500 ARG A 47 NE - CZ - NH1 ANGL. DEV. = 7.9 DEGREES REMARK 500 ARG A 47 NE - CZ - NH2 ANGL. DEV. = -6.5 DEGREES REMARK 500 MET A 48 CB - CA - C ANGL. DEV. = 12.8 DEGREES REMARK 500 THR A 54 CA - CB - CG2 ANGL. DEV. = 10.8 DEGREES REMARK 500 ASP A 59 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES REMARK 500 ASP A 59 CB - CG - OD2 ANGL. DEV. = -6.6 DEGREES REMARK 500 ASP A 66 CB - CG - OD2 ANGL. DEV. = -7.1 DEGREES REMARK 500 ASP A 68 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES REMARK 500 ASP A 68 CB - CG - OD2 ANGL. DEV. = -8.3 DEGREES REMARK 500 ASP A 74 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES REMARK 500 ASP A 74 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES REMARK 500 ARG A 103 CG - CD - NE ANGL. DEV. = -13.7 DEGREES REMARK 500 ARG A 103 NH1 - CZ - NH2 ANGL. DEV. = -7.0 DEGREES REMARK 500 ARG A 103 NE - CZ - NH1 ANGL. DEV. = 7.9 DEGREES REMARK 500 ASP A 114 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES REMARK 500 ARG A 123 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 ARG A 123 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 GLU A 127 CA - C - N ANGL. DEV. = 14.1 DEGREES REMARK 500 GLU A 127 O - C - N ANGL. DEV. = -21.6 DEGREES REMARK 500 HIS A 128 N - CA - CB ANGL. DEV. = -11.6 DEGREES REMARK 500 HIS A 128 ND1 - CE1 - NE2 ANGL. DEV. = 8.4 DEGREES REMARK 500 ASP A 136 CB - CG - OD2 ANGL. DEV. = -6.9 DEGREES REMARK 500 LYS A 139 N - CA - CB ANGL. DEV. = 14.0 DEGREES REMARK 500 LYS A 139 CD - CE - NZ ANGL. DEV. = -16.5 DEGREES REMARK 500 ASP A 140 CB - CG - OD2 ANGL. DEV. = -6.9 DEGREES REMARK 500 ASP A 142 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 ARG A 148 NH1 - CZ - NH2 ANGL. DEV. = -8.1 DEGREES REMARK 500 ARG A 148 NE - CZ - NH1 ANGL. DEV. = 8.8 DEGREES REMARK 500 ASP A 150 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES REMARK 500 ASP A 152 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES REMARK 500 ASP A 152 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES REMARK 500 MET A 158 CA - C - O ANGL. DEV. = 17.8 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 ASP A 30 44.41 -84.30 REMARK 500 ASN A 145 76.18 61.83 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 ARG A 84 0.34 SIDE CHAIN REMARK 500 ARG A 123 0.28 SIDE CHAIN REMARK 500 ARG A 148 0.13 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: I REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: NULL REMARK 800 REMARK 800 SITE_IDENTIFIER: II REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: NULL REMARK 800 REMARK 800 SITE_IDENTIFIER: III REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: NULL REMARK 800 REMARK 800 SITE_IDENTIFIER: IV REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1TNW RELATED DB: PDB DBREF 1TNX A 1 162 UNP P02588 TNNC2_CHICK 2 163 SEQRES 1 A 162 ALA SER MET THR ASP GLN GLN ALA GLU ALA ARG ALA PHE SEQRES 2 A 162 LEU SER GLU GLU MET ILE ALA GLU PHE LYS ALA ALA PHE SEQRES 3 A 162 ASP MET PHE ASP ALA ASP GLY GLY GLY ASP ILE SER THR SEQRES 4 A 162 LYS GLU LEU GLY THR VAL MET ARG MET LEU GLY GLN ASN SEQRES 5 A 162 PRO THR LYS GLU GLU LEU ASP ALA ILE ILE GLU GLU VAL SEQRES 6 A 162 ASP GLU ASP GLY SER GLY THR ILE ASP PHE GLU GLU PHE SEQRES 7 A 162 LEU VAL MET MET VAL ARG GLN MET LYS GLU ASP ALA LYS SEQRES 8 A 162 GLY LYS SER GLU GLU GLU LEU ALA ASN CYS PHE ARG ILE SEQRES 9 A 162 PHE ASP LYS ASN ALA ASP GLY PHE ILE ASP ILE GLU GLU SEQRES 10 A 162 LEU GLY GLU ILE LEU ARG ALA THR GLY GLU HIS VAL ILE SEQRES 11 A 162 GLU GLU ASP ILE GLU ASP LEU MET LYS ASP SER ASP LYS SEQRES 12 A 162 ASN ASN ASP GLY ARG ILE ASP PHE ASP GLU PHE LEU LYS SEQRES 13 A 162 MET MET GLU GLY VAL GLN HELIX 1 N GLN A 6 PHE A 13 1 8 HELIX 2 A GLU A 16 PHE A 29 1 14 HELIX 3 B THR A 39 MET A 48 1 10 HELIX 4 C LYS A 55 VAL A 65 1 11 HELIX 5 D PHE A 75 ARG A 84 1 10 HELIX 6 E GLU A 96 PHE A 105 1 10 HELIX 7 F ILE A 115 ALA A 124 1 10 HELIX 8 G GLU A 131 SER A 141 1 11 HELIX 9 H PHE A 151 MET A 157 1 7 SHEET 1 S1 2 ASP A 36 SER A 38 0 SHEET 2 S1 2 THR A 72 ASP A 74 -1 SHEET 1 S2 2 PHE A 112 ASP A 114 0 SHEET 2 S2 2 ARG A 148 ASP A 150 -1 SITE 1 I 12 ASP A 30 ALA A 31 ASP A 32 GLY A 33 SITE 2 I 12 GLY A 34 GLY A 35 ASP A 36 ILE A 37 SITE 3 I 12 SER A 38 THR A 39 LYS A 40 GLU A 41 SITE 1 II 12 ASP A 66 GLU A 67 ASP A 68 GLY A 69 SITE 2 II 12 SER A 70 GLY A 71 THR A 72 ILE A 73 SITE 3 II 12 ASP A 74 PHE A 75 GLU A 76 GLU A 77 SITE 1 III 12 ASP A 106 LYS A 107 ASN A 108 ALA A 109 SITE 2 III 12 ASP A 110 GLY A 111 PHE A 112 ILE A 113 SITE 3 III 12 ASP A 114 ILE A 115 GLU A 116 GLU A 117 SITE 1 IV 12 ASP A 142 LYS A 143 ASN A 144 ASN A 145 SITE 2 IV 12 ASP A 146 GLY A 147 ARG A 148 ILE A 149 SITE 3 IV 12 ASP A 150 PHE A 151 ASP A 152 GLU A 153 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
Complete list - 2 20 Bytes