Header list of 1hod.pdb file
Complete list - 23 202 Bytes
HEADER MEMBRANE PROTEIN 10-DEC-00 1HOD TITLE NMR STRUCTURE OF D130I MUTANT T3-I2, A 32 RESIDUE PEPTIDE FROM THE TITLE 2 ALPHA 2A ADRENERGIC RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-2A ADRENERGIC RECEPTOR; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: SECOND INTRACELLULAR LOOP (RESIDUES 118-149); COMPND 5 SYNONYM: ALPHA-2A ADRENOCEPTOR; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE SOURCE 4 OF THE PEPTIDE OCCURS NATURALLY IN HOMO SAPIENS (HUMAN). KEYWDS HELIX-LINKER-HELIX, MEMBRANE PROTEIN EXPDTA SOLUTION NMR AUTHOR D.A.CHUNG,E.R.ZUIDERWEG,R.R.NEUBIG REVDAT 4 23-FEB-22 1HOD 1 REMARK SEQADV REVDAT 3 24-FEB-09 1HOD 1 VERSN REVDAT 2 01-APR-03 1HOD 1 JRNL REVDAT 1 24-JUL-02 1HOD 0 JRNL AUTH D.A.CHUNG,E.R.ZUIDERWEG,C.B.FOWLER,O.S.SOYER,H.I.MOSBERG, JRNL AUTH 2 R.R.NEUBIG JRNL TITL NMR STRUCTURE OF THE SECOND INTRACELLULAR LOOP OF THE ALPHA JRNL TITL 2 2A ADRENERGIC RECEPTOR: EVIDENCE FOR A NOVEL CYTOPLASMIC JRNL TITL 3 HELIX. JRNL REF BIOCHEMISTRY V. 41 3596 2002 JRNL REFN ISSN 0006-2960 JRNL PMID 11888275 JRNL DOI 10.1021/BI015811+ REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA, DYANA REMARK 3 AUTHORS : GUNTERT (DYANA), GUNTERT (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1HOD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-DEC-00. REMARK 100 THE DEPOSITION ID IS D_1000012483. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303.00; 303.00 REMARK 210 PH : 4.50; 4.50 REMARK 210 IONIC STRENGTH : 50 MM NACL; 50 MM REMARK 210 PRESSURE : NULL; NULL REMARK 210 SAMPLE CONTENTS : 0.9 MM PEPTIDE NATURAL REMARK 210 ABUNDANCE; 460 MM D38- REMARK 210 DODECYLPHOSPHOCHOLINE, 50 MM REMARK 210 NACL, 10 MM NAH2PO4, PH 4.5; 0.9 REMARK 210 MM PEPTIDE NATURAL ABUNDANCE; REMARK 210 460 MM D38- REMARK 210 DODECYLPHOSPHOCHOLINE, 50 MM REMARK 210 NACL, 10 MM NAH2PO4, PH 4.5 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 2D COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY, NMRPIPE, NMRVIEW, SPSCAN REMARK 210 METHOD USED : SIMULATED ANNEALING IN TORSION REMARK 210 ANGLE SPACE 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 : 1 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: 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 THR A 29 N PRO A 30 0.52 REMARK 500 HA THR A 29 HD3 PRO A 30 0.55 REMARK 500 C THR A 29 CD PRO A 30 0.57 REMARK 500 C THR A 29 HD2 PRO A 30 0.64 REMARK 500 C LYS A 27 H ARG A 28 0.66 REMARK 500 O LYS A 27 N ARG A 28 0.71 REMARK 500 HG2 ARG A 31 N ARG A 32 0.71 REMARK 500 C PRO A 30 H ARG A 31 0.75 REMARK 500 CA THR A 29 HD3 PRO A 30 0.76 REMARK 500 O PRO A 30 N ARG A 31 0.79 REMARK 500 C ARG A 31 H ARG A 32 0.82 REMARK 500 HG2 ARG A 31 H ARG A 32 0.83 REMARK 500 O ARG A 31 N ARG A 32 0.88 REMARK 500 OG1 THR A 29 HD2 PRO A 30 0.89 REMARK 500 O THR A 29 CD PRO A 30 0.89 REMARK 500 C TRP A 16 H SER A 17 0.94 REMARK 500 HA ARG A 31 N ARG A 32 0.97 REMARK 500 O THR A 29 HD2 PRO A 30 0.97 REMARK 500 O PRO A 30 H ARG A 31 0.97 REMARK 500 C THR A 29 HD3 PRO A 30 0.97 REMARK 500 O LYS A 27 H ARG A 28 0.99 REMARK 500 O TRP A 16 N SER A 17 1.00 REMARK 500 HG1 THR A 29 HD2 PRO A 30 1.00 REMARK 500 HA ARG A 31 H ARG A 32 1.01 REMARK 500 C LEU A 26 H LYS A 27 1.03 REMARK 500 C THR A 29 CG PRO A 30 1.04 REMARK 500 CA THR A 29 HD2 PRO A 30 1.04 REMARK 500 HA THR A 29 HD2 PRO A 30 1.05 REMARK 500 CG ARG A 31 N ARG A 32 1.05 REMARK 500 C ARG A 31 HA ARG A 32 1.07 REMARK 500 O THR A 29 CA PRO A 30 1.08 REMARK 500 HA THR A 29 CD PRO A 30 1.08 REMARK 500 CA ARG A 31 N ARG A 32 1.08 REMARK 500 OG1 THR A 29 HD3 PRO A 30 1.09 REMARK 500 CA THR A 29 CD PRO A 30 1.09 REMARK 500 O THR A 29 CG PRO A 30 1.10 REMARK 500 C ARG A 31 CA ARG A 32 1.10 REMARK 500 HB3 ARG A 31 N ARG A 32 1.10 REMARK 500 O LEU A 26 N LYS A 27 1.11 REMARK 500 HG2 ARG A 31 CA ARG A 32 1.12 REMARK 500 CG ARG A 31 H ARG A 32 1.12 REMARK 500 HG2 ARG A 31 HA ARG A 32 1.13 REMARK 500 O ARG A 31 H ARG A 32 1.13 REMARK 500 HG2 ARG A 31 HB3 ARG A 32 1.14 REMARK 500 CB ARG A 31 N ARG A 32 1.15 REMARK 500 C THR A 29 HG3 PRO A 30 1.15 REMARK 500 O THR A 29 HA PRO A 30 1.15 REMARK 500 HB2 PRO A 30 H ARG A 31 1.16 REMARK 500 OG1 THR A 29 CD PRO A 30 1.16 REMARK 500 HB2 PRO A 30 N ARG A 31 1.16 REMARK 500 REMARK 500 THIS ENTRY HAS 157 CLOSE CONTACTS 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 THR A 1 N THR A 1 CA -0.252 REMARK 500 THR A 1 CA THR A 1 CB -0.224 REMARK 500 THR A 1 CB THR A 1 OG1 -0.264 REMARK 500 THR A 1 CB THR A 1 CG2 -0.343 REMARK 500 THR A 1 CA THR A 1 C -0.165 REMARK 500 THR A 1 C THR A 1 O -0.131 REMARK 500 THR A 1 C SER A 2 N -0.203 REMARK 500 SER A 2 N SER A 2 CA -0.174 REMARK 500 SER A 2 CA SER A 2 CB -0.106 REMARK 500 SER A 2 CB SER A 2 OG -0.668 REMARK 500 SER A 2 C SER A 2 O -0.197 REMARK 500 SER A 2 C SER A 3 N -0.181 REMARK 500 SER A 3 N SER A 3 CA -0.138 REMARK 500 SER A 3 CA SER A 3 CB -0.092 REMARK 500 SER A 3 CB SER A 3 OG -0.304 REMARK 500 SER A 3 C SER A 3 O -0.170 REMARK 500 SER A 3 C ILE A 4 N -0.187 REMARK 500 ILE A 4 CG1 ILE A 4 CD1 -0.891 REMARK 500 VAL A 5 CB VAL A 5 CG1 -0.149 REMARK 500 VAL A 5 CB VAL A 5 CG2 -0.180 REMARK 500 HIS A 6 N HIS A 6 CA -0.124 REMARK 500 HIS A 6 CB HIS A 6 CG -0.180 REMARK 500 HIS A 6 CG HIS A 6 CD2 -0.432 REMARK 500 HIS A 6 CG HIS A 6 ND1 -0.316 REMARK 500 HIS A 6 ND1 HIS A 6 CE1 -0.223 REMARK 500 HIS A 6 CE1 HIS A 6 NE2 -0.478 REMARK 500 HIS A 6 NE2 HIS A 6 CD2 -0.212 REMARK 500 LEU A 7 CB LEU A 7 CG -0.634 REMARK 500 LEU A 7 CG LEU A 7 CD1 -0.365 REMARK 500 LEU A 7 CG LEU A 7 CD2 -0.668 REMARK 500 LEU A 7 C LEU A 7 O -0.329 REMARK 500 LEU A 7 C CYS A 8 N -0.320 REMARK 500 CYS A 8 CB CYS A 8 SG -0.383 REMARK 500 SER A 11 CB SER A 11 OG -0.281 REMARK 500 SER A 11 C SER A 11 O -0.305 REMARK 500 SER A 11 C LEU A 12 N -0.263 REMARK 500 LEU A 12 CG LEU A 12 CD1 -0.616 REMARK 500 LEU A 12 CG LEU A 12 CD2 -0.663 REMARK 500 ARG A 14 CB ARG A 14 CG -0.274 REMARK 500 ARG A 14 CG ARG A 14 CD -0.639 REMARK 500 ARG A 14 CD ARG A 14 NE -0.551 REMARK 500 ARG A 14 NE ARG A 14 CZ -0.488 REMARK 500 ARG A 14 CZ ARG A 14 NH1 -1.220 REMARK 500 ARG A 14 CZ ARG A 14 NH2 -0.537 REMARK 500 TYR A 15 CB TYR A 15 CG -0.094 REMARK 500 TYR A 15 CG TYR A 15 CD2 -0.737 REMARK 500 TYR A 15 CG TYR A 15 CD1 -0.723 REMARK 500 TYR A 15 CE1 TYR A 15 CZ -0.768 REMARK 500 TYR A 15 CZ TYR A 15 OH -0.114 REMARK 500 TYR A 15 CZ TYR A 15 CE2 -0.755 REMARK 500 REMARK 500 THIS ENTRY HAS 162 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 ILE A 4 CB - CG1 - CD1 ANGL. DEV. = 36.0 DEGREES REMARK 500 HIS A 6 ND1 - CG - CD2 ANGL. DEV. = -19.7 DEGREES REMARK 500 HIS A 6 CG - ND1 - CE1 ANGL. DEV. = 17.6 DEGREES REMARK 500 HIS A 6 ND1 - CE1 - NE2 ANGL. DEV. = -12.5 DEGREES REMARK 500 HIS A 6 CG - CD2 - NE2 ANGL. DEV. = 11.8 DEGREES REMARK 500 LEU A 7 CA - CB - CG ANGL. DEV. = 31.2 DEGREES REMARK 500 LEU A 7 CB - CG - CD2 ANGL. DEV. = 12.8 DEGREES REMARK 500 LEU A 7 O - C - N ANGL. DEV. = -16.8 DEGREES REMARK 500 SER A 11 O - C - N ANGL. DEV. = -13.8 DEGREES REMARK 500 LEU A 12 CD1 - CG - CD2 ANGL. DEV. = -21.6 DEGREES REMARK 500 LEU A 12 CB - CG - CD1 ANGL. DEV. = 18.6 DEGREES REMARK 500 LEU A 12 CB - CG - CD2 ANGL. DEV. = 12.9 DEGREES REMARK 500 ARG A 14 CB - CG - CD ANGL. DEV. = 25.9 DEGREES REMARK 500 ARG A 14 CG - CD - NE ANGL. DEV. = 28.6 DEGREES REMARK 500 ARG A 14 CD - NE - CZ ANGL. DEV. = 50.5 DEGREES REMARK 500 ARG A 14 NH1 - CZ - NH2 ANGL. DEV. = -54.5 DEGREES REMARK 500 ARG A 14 NE - CZ - NH2 ANGL. DEV. = 53.3 DEGREES REMARK 500 TYR A 15 CB - CG - CD2 ANGL. DEV. = 45.8 DEGREES REMARK 500 TYR A 15 CD1 - CG - CD2 ANGL. DEV. = -91.7 DEGREES REMARK 500 TYR A 15 CB - CG - CD1 ANGL. DEV. = 46.1 DEGREES REMARK 500 TYR A 15 CG - CD1 - CE1 ANGL. DEV. = 45.7 DEGREES REMARK 500 TYR A 15 CG - CD2 - CE2 ANGL. DEV. = 45.4 DEGREES REMARK 500 TYR A 15 CD1 - CE1 - CZ ANGL. DEV. = 46.3 DEGREES REMARK 500 TYR A 15 OH - CZ - CE2 ANGL. DEV. = 46.2 DEGREES REMARK 500 TYR A 15 CE1 - CZ - OH ANGL. DEV. = 46.0 DEGREES REMARK 500 TYR A 15 CE1 - CZ - CE2 ANGL. DEV. = -92.2 DEGREES REMARK 500 TYR A 15 CZ - CE2 - CD2 ANGL. DEV. = 46.5 DEGREES REMARK 500 TRP A 16 CA - C - O ANGL. DEV. = 16.5 DEGREES REMARK 500 TRP A 16 CA - C - N ANGL. DEV. = 25.0 DEGREES REMARK 500 TRP A 16 O - C - N ANGL. DEV. = -41.5 DEGREES REMARK 500 SER A 17 C - N - CA ANGL. DEV. = 23.2 DEGREES REMARK 500 ILE A 18 CB - CG1 - CD1 ANGL. DEV. = 38.4 DEGREES REMARK 500 GLN A 20 CB - CG - CD ANGL. DEV. = 25.3 DEGREES REMARK 500 GLN A 20 OE1 - CD - NE2 ANGL. DEV. = -52.0 DEGREES REMARK 500 GLN A 20 CG - CD - OE1 ANGL. DEV. = 12.1 DEGREES REMARK 500 GLN A 20 CG - CD - NE2 ANGL. DEV. = 39.7 DEGREES REMARK 500 ALA A 21 CA - C - N ANGL. DEV. = 13.9 DEGREES REMARK 500 ALA A 21 O - C - N ANGL. DEV. = -18.6 DEGREES REMARK 500 GLU A 23 CB - CG - CD ANGL. DEV. = 20.2 DEGREES REMARK 500 GLU A 23 OE1 - CD - OE2 ANGL. DEV. = -53.0 DEGREES REMARK 500 GLU A 23 CG - CD - OE2 ANGL. DEV. = 48.1 DEGREES REMARK 500 TYR A 24 CB - CG - CD2 ANGL. DEV. = 26.3 DEGREES REMARK 500 TYR A 24 CD1 - CG - CD2 ANGL. DEV. = -53.6 DEGREES REMARK 500 TYR A 24 CB - CG - CD1 ANGL. DEV. = 27.4 DEGREES REMARK 500 TYR A 24 CG - CD1 - CE1 ANGL. DEV. = 27.1 DEGREES REMARK 500 TYR A 24 CG - CD2 - CE2 ANGL. DEV. = 26.0 DEGREES REMARK 500 TYR A 24 CD1 - CE1 - CZ ANGL. DEV. = 25.8 DEGREES REMARK 500 TYR A 24 OH - CZ - CE2 ANGL. DEV. = 26.8 DEGREES REMARK 500 TYR A 24 CE1 - CZ - OH ANGL. DEV. = 25.5 DEGREES REMARK 500 TYR A 24 CE1 - CZ - CE2 ANGL. DEV. = -52.3 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 103 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 TRP A 16 -89.23 -90.62 REMARK 500 SER A 17 53.75 -28.65 REMARK 500 ILE A 18 -45.09 -152.26 REMARK 500 ALA A 21 46.61 -108.49 REMARK 500 THR A 29 116.44 -166.79 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1HLL RELATED DB: PDB REMARK 900 MEAN STRUCTURE OF WILD-TYPE T3-I2 PEPTIDE REMARK 900 RELATED ID: 1HOF RELATED DB: PDB REMARK 900 BEST 20 DYANA CONFORMERS OF WILD-TYPE T3-I2 PEPTIDE REMARK 900 RELATED ID: 1H09 RELATED DB: PDB REMARK 900 BEST 20 DYANA CONFORMERS OF D130I MUTANT T3-I2 PEPTIDE DBREF 1HOD A 1 32 UNP P08913 ADA2A_HUMAN 118 149 SEQADV 1HOD ILE A 13 UNP P08913 ASP 130 CONFLICT SEQRES 1 A 32 THR SER SER ILE VAL HIS LEU CYS ALA ILE SER LEU ILE SEQRES 2 A 32 ARG TYR TRP SER ILE THR GLN ALA ILE GLU TYR ASN LEU SEQRES 3 A 32 LYS ARG THR PRO ARG ARG HELIX 1 1 THR A 1 ARG A 14 1 14 HELIX 2 2 THR A 19 LYS A 27 1 9 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 - 23 202 Bytes