Header list of 1hll.pdb file
Complete list - 23 202 Bytes
HEADER MEMBRANE PROTEIN 01-DEC-00 1HLL
TITLE NMR STRUCTURE OF T3-I2, A 32 RESIDUE PEPTIDE FROM THE ALPHA-2A
TITLE 2 ADRENERGIC RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-2A ADRENERGIC RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SECOND INTRACELLULAR LOOP T3-I2 (RESIDUES 118-149);
COMPND 5 SYNONYM: ALPHA-2A ADRENOCEPTOR;
COMPND 6 ENGINEERED: 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.P.ZUIDERWEG,R.R.NEUBIG
REVDAT 4 23-FEB-22 1HLL 1 REMARK
REVDAT 3 24-FEB-09 1HLL 1 VERSN
REVDAT 2 01-APR-03 1HLL 1 JRNL
REVDAT 1 10-APR-02 1HLL 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 : GUENTERT (DYANA), GUENTERT (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HLL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-00.
REMARK 100 THE DEPOSITION ID IS D_1000012435.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : 50 MM NACL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 0.9 MM T3-I2 NATURAL ABUNDANCE;
REMARK 210 460 MM D38-DODECYLPHOSPHOCHOLINE,
REMARK 210 50 MM NACL, 10 MM NAH2PO4, PH
REMARK 210 4.5; 0.9 MM T3-I2 NATURAL
REMARK 210 ABUNDANCE; 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 : UNITY
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 : 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: 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 HA THR A 29 N PRO A 30 0.16
REMARK 500 C THR A 29 HA PRO A 30 0.32
REMARK 500 HA THR A 29 HD2 PRO A 30 0.33
REMARK 500 C THR A 29 CA PRO A 30 0.36
REMARK 500 O THR A 29 CA PRO A 30 0.36
REMARK 500 HA THR A 29 HA PRO A 30 0.37
REMARK 500 CA THR A 29 CD PRO A 30 0.37
REMARK 500 CA THR A 29 N PRO A 30 0.38
REMARK 500 C THR A 29 HD2 PRO A 30 0.39
REMARK 500 HA THR A 29 CD PRO A 30 0.39
REMARK 500 HA THR A 29 CA PRO A 30 0.40
REMARK 500 O THR A 29 N PRO A 30 0.43
REMARK 500 O THR A 29 HD2 PRO A 30 0.43
REMARK 500 CB THR A 29 HD2 PRO A 30 0.44
REMARK 500 HA THR A 29 HG2 PRO A 30 0.47
REMARK 500 C THR A 29 CD PRO A 30 0.48
REMARK 500 CA THR A 29 HA PRO A 30 0.49
REMARK 500 HA THR A 29 CB PRO A 30 0.50
REMARK 500 HG1 THR A 29 CA PRO A 30 0.51
REMARK 500 O THR A 29 HA PRO A 30 0.51
REMARK 500 HB THR A 29 HD2 PRO A 30 0.51
REMARK 500 CB THR A 29 N PRO A 30 0.53
REMARK 500 C THR A 29 HG2 PRO A 30 0.54
REMARK 500 C THR A 29 CB PRO A 30 0.55
REMARK 500 CA THR A 29 CG PRO A 30 0.58
REMARK 500 HA THR A 29 CG PRO A 30 0.58
REMARK 500 CA THR A 29 CB PRO A 30 0.59
REMARK 500 HA THR A 29 HB2 PRO A 30 0.61
REMARK 500 C THR A 29 HB2 PRO A 30 0.61
REMARK 500 CB THR A 29 CA PRO A 30 0.62
REMARK 500 N THR A 29 HD3 PRO A 30 0.62
REMARK 500 O THR A 29 HB2 PRO A 30 0.63
REMARK 500 CA THR A 29 HD2 PRO A 30 0.63
REMARK 500 OG1 THR A 29 CA PRO A 30 0.64
REMARK 500 O THR A 29 HG2 PRO A 30 0.65
REMARK 500 HA ARG A 31 N ARG A 32 0.65
REMARK 500 HB THR A 29 N PRO A 30 0.66
REMARK 500 C ARG A 31 HA ARG A 32 0.66
REMARK 500 HG1 THR A 29 HD2 PRO A 30 0.67
REMARK 500 C THR A 29 CG PRO A 30 0.67
REMARK 500 CA THR A 29 CA PRO A 30 0.67
REMARK 500 HG1 THR A 29 H ARG A 31 0.67
REMARK 500 OG1 THR A 29 HD2 PRO A 30 0.68
REMARK 500 HB THR A 29 HG2 PRO A 30 0.69
REMARK 500 HG1 THR A 29 HB2 PRO A 30 0.70
REMARK 500 HG1 THR A 29 N PRO A 30 0.70
REMARK 500 HG1 THR A 29 HA PRO A 30 0.70
REMARK 500 HB THR A 29 CD PRO A 30 0.71
REMARK 500 CB THR A 29 HA PRO A 30 0.71
REMARK 500 CB THR A 29 HG2 PRO A 30 0.74
REMARK 500
REMARK 500 THIS ENTRY HAS 398 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 -0.313
REMARK 500 THR A 1 CA THR A 1 CB -0.288
REMARK 500 THR A 1 CB THR A 1 OG1 -0.466
REMARK 500 THR A 1 CB THR A 1 CG2 -0.437
REMARK 500 SER A 2 CB SER A 2 OG -0.526
REMARK 500 SER A 3 CB SER A 3 OG -0.242
REMARK 500 SER A 3 C SER A 3 O -0.182
REMARK 500 SER A 3 C ILE A 4 N -0.191
REMARK 500 ILE A 4 CG1 ILE A 4 CD1 -0.810
REMARK 500 HIS A 6 CG HIS A 6 CD2 -0.150
REMARK 500 HIS A 6 CG HIS A 6 ND1 -0.372
REMARK 500 HIS A 6 CE1 HIS A 6 NE2 -0.321
REMARK 500 HIS A 6 NE2 HIS A 6 CD2 -0.234
REMARK 500 LEU A 7 CB LEU A 7 CG -0.216
REMARK 500 LEU A 7 CG LEU A 7 CD1 -0.520
REMARK 500 LEU A 7 CG LEU A 7 CD2 -0.649
REMARK 500 CYS A 8 CB CYS A 8 SG -0.219
REMARK 500 ALA A 9 C ALA A 9 O -0.225
REMARK 500 ALA A 9 C ILE A 10 N -0.142
REMARK 500 ILE A 10 CG1 ILE A 10 CD1 -0.692
REMARK 500 SER A 11 CB SER A 11 OG -0.557
REMARK 500 SER A 11 C SER A 11 O -0.464
REMARK 500 SER A 11 C LEU A 12 N -0.380
REMARK 500 LEU A 12 CB LEU A 12 CG -0.489
REMARK 500 LEU A 12 CG LEU A 12 CD1 -0.605
REMARK 500 LEU A 12 CG LEU A 12 CD2 -0.670
REMARK 500 ASP A 13 CB ASP A 13 CG -0.137
REMARK 500 ASP A 13 CG ASP A 13 OD1 -0.793
REMARK 500 ASP A 13 CG ASP A 13 OD2 -0.636
REMARK 500 ARG A 14 CG ARG A 14 CD -0.276
REMARK 500 ARG A 14 CD ARG A 14 NE -0.441
REMARK 500 ARG A 14 NE ARG A 14 CZ -0.536
REMARK 500 ARG A 14 CZ ARG A 14 NH1 -0.772
REMARK 500 ARG A 14 CZ ARG A 14 NH2 -0.415
REMARK 500 TYR A 15 CG TYR A 15 CD2 -0.682
REMARK 500 TYR A 15 CG TYR A 15 CD1 -0.657
REMARK 500 TYR A 15 CE1 TYR A 15 CZ -0.713
REMARK 500 TYR A 15 CZ TYR A 15 CE2 -0.688
REMARK 500 TYR A 15 C TYR A 15 O -0.259
REMARK 500 TYR A 15 C TRP A 16 N -0.275
REMARK 500 SER A 17 CB SER A 17 OG -0.175
REMARK 500 SER A 17 C SER A 17 O -0.198
REMARK 500 SER A 17 C ILE A 18 N -0.191
REMARK 500 ILE A 18 CG1 ILE A 18 CD1 -0.573
REMARK 500 THR A 19 CB THR A 19 OG1 -0.321
REMARK 500 THR A 19 CB THR A 19 CG2 -0.333
REMARK 500 GLN A 20 CB GLN A 20 CG -0.317
REMARK 500 GLN A 20 CG GLN A 20 CD -0.659
REMARK 500 GLN A 20 CD GLN A 20 OE1 -0.918
REMARK 500 GLN A 20 CD GLN A 20 NE2 -0.556
REMARK 500
REMARK 500 THIS ENTRY HAS 153 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 THR A 1 OG1 - CB - CG2 ANGL. DEV. = -21.0 DEGREES
REMARK 500 THR A 1 CA - CB - CG2 ANGL. DEV. = 13.0 DEGREES
REMARK 500 SER A 2 CA - CB - OG ANGL. DEV. = 22.2 DEGREES
REMARK 500 ILE A 4 CB - CG1 - CD1 ANGL. DEV. = 43.6 DEGREES
REMARK 500 HIS A 6 CB - CG - CD2 ANGL. DEV. = 11.1 DEGREES
REMARK 500 HIS A 6 ND1 - CG - CD2 ANGL. DEV. = -12.5 DEGREES
REMARK 500 HIS A 6 CG - CD2 - NE2 ANGL. DEV. = 15.0 DEGREES
REMARK 500 LEU A 7 CD1 - CG - CD2 ANGL. DEV. = -22.9 DEGREES
REMARK 500 LEU A 7 CB - CG - CD1 ANGL. DEV. = 20.5 DEGREES
REMARK 500 LEU A 7 CB - CG - CD2 ANGL. DEV. = 12.3 DEGREES
REMARK 500 ILE A 10 CB - CG1 - CD1 ANGL. DEV. = 30.6 DEGREES
REMARK 500 SER A 11 CA - C - N ANGL. DEV. = 17.8 DEGREES
REMARK 500 SER A 11 O - C - N ANGL. DEV. = -26.5 DEGREES
REMARK 500 LEU A 12 C - N - CA ANGL. DEV. = 16.8 DEGREES
REMARK 500 LEU A 12 CA - CB - CG ANGL. DEV. = 19.7 DEGREES
REMARK 500 LEU A 12 CD1 - CG - CD2 ANGL. DEV. = -49.4 DEGREES
REMARK 500 LEU A 12 CB - CG - CD1 ANGL. DEV. = 32.6 DEGREES
REMARK 500 LEU A 12 CB - CG - CD2 ANGL. DEV. = 29.2 DEGREES
REMARK 500 ASP A 13 OD1 - CG - OD2 ANGL. DEV. = -88.4 DEGREES
REMARK 500 ASP A 13 CB - CG - OD1 ANGL. DEV. = 41.6 DEGREES
REMARK 500 ASP A 13 CB - CG - OD2 ANGL. DEV. = 46.9 DEGREES
REMARK 500 ARG A 14 CD - NE - CZ ANGL. DEV. = 21.7 DEGREES
REMARK 500 ARG A 14 NE - CZ - NH1 ANGL. DEV. = -23.7 DEGREES
REMARK 500 ARG A 14 NE - CZ - NH2 ANGL. DEV. = 22.6 DEGREES
REMARK 500 TYR A 15 CB - CG - CD2 ANGL. DEV. = 37.0 DEGREES
REMARK 500 TYR A 15 CD1 - CG - CD2 ANGL. DEV. = -74.8 DEGREES
REMARK 500 TYR A 15 CB - CG - CD1 ANGL. DEV. = 37.8 DEGREES
REMARK 500 TYR A 15 CG - CD1 - CE1 ANGL. DEV. = 37.5 DEGREES
REMARK 500 TYR A 15 CG - CD2 - CE2 ANGL. DEV. = 36.7 DEGREES
REMARK 500 TYR A 15 CD1 - CE1 - CZ ANGL. DEV. = 37.0 DEGREES
REMARK 500 TYR A 15 OH - CZ - CE2 ANGL. DEV. = 37.5 DEGREES
REMARK 500 TYR A 15 CE1 - CZ - OH ANGL. DEV. = 36.7 DEGREES
REMARK 500 TYR A 15 CE1 - CZ - CE2 ANGL. DEV. = -74.2 DEGREES
REMARK 500 TYR A 15 CZ - CE2 - CD2 ANGL. DEV. = 37.8 DEGREES
REMARK 500 TYR A 15 O - C - N ANGL. DEV. = -11.7 DEGREES
REMARK 500 ILE A 18 CB - CG1 - CD1 ANGL. DEV. = 17.9 DEGREES
REMARK 500 GLN A 20 CB - CG - CD ANGL. DEV. = 33.9 DEGREES
REMARK 500 GLN A 20 CG - CD - OE1 ANGL. DEV. = -24.9 DEGREES
REMARK 500 GLN A 20 CG - CD - NE2 ANGL. DEV. = 34.5 DEGREES
REMARK 500 GLN A 20 CA - C - N ANGL. DEV. = 13.7 DEGREES
REMARK 500 GLN A 20 O - C - N ANGL. DEV. = -15.5 DEGREES
REMARK 500 ALA A 21 O - C - N ANGL. DEV. = -12.5 DEGREES
REMARK 500 GLU A 23 CB - CG - CD ANGL. DEV. = 23.0 DEGREES
REMARK 500 GLU A 23 OE1 - CD - OE2 ANGL. DEV. = 105.0 DEGREES
REMARK 500 GLU A 23 CG - CD - OE1 ANGL. DEV. = 54.1 DEGREES
REMARK 500 GLU A 23 CG - CD - OE2 ANGL. DEV. = 51.0 DEGREES
REMARK 500 TYR A 24 CB - CG - CD2 ANGL. DEV. = 15.9 DEGREES
REMARK 500 TYR A 24 CD1 - CG - CD2 ANGL. DEV. = -53.6 DEGREES
REMARK 500 TYR A 24 CB - CG - CD1 ANGL. DEV. = 37.8 DEGREES
REMARK 500 TYR A 24 CG - CD1 - CE1 ANGL. DEV. = 37.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 99 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 LEU A 26 -64.24 -130.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HOF RELATED DB: PDB
REMARK 900 TOP 20 DYANA CONFORMERS OF WILD-TYPE T3-I2 PEPTIDE
REMARK 900 RELATED ID: 1HOD RELATED DB: PDB
REMARK 900 MEAN STRUCTURE OF D130I MUTANT T3-I2 PEPTIDE
REMARK 900 RELATED ID: 1HO9 RELATED DB: PDB
REMARK 900 TOP 20 DYANA CONFORMERS OF D130I MUTANT T3-I2 PEPTIDE
DBREF 1HLL A 1 32 UNP P08913 ADA2A_HUMAN 118 149
SEQRES 1 A 32 THR SER SER ILE VAL HIS LEU CYS ALA ILE SER LEU ASP
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 LEU A 12 1 12
HELIX 2 2 LEU A 12 GLU A 23 1 12
HELIX 3 3 TYR A 24 LEU A 26 5 3
CRYST1 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