Header list of 1y9o.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE 16-DEC-04 1Y9O
TITLE 1H NMR STRUCTURE OF ACYLPHOSPHATASE FROM THE HYPERTHERMOPHILE
TITLE 2 SULFOLOBUS SOLFATARICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYLPHOSPHATASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.6.1.7;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE 3 ORGANISM_TAXID: 2287;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS SSO, ACYLPHOSPHATASE, HYPERTHERMOPHILE, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.CORAZZA,C.ROSANO,K.PAGANO,V.ALVERDI,G.ESPOSITO,C.CAPANNI,
AUTHOR 2 F.BEMPORAD,G.PLAKOUTSI,M.STEFANI,F.CHITI,S.ZUCCOTTI,M.BOLOGNESI,
AUTHOR 3 P.VIGLINO
REVDAT 5 02-MAR-22 1Y9O 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1Y9O 1 VERSN
REVDAT 3 20-MAR-07 1Y9O 1 JRNL
REVDAT 2 13-MAR-07 1Y9O 1 DBREF SEQADV
REVDAT 1 29-NOV-05 1Y9O 0
JRNL AUTH A.CORAZZA,C.ROSANO,K.PAGANO,V.ALVERDI,G.ESPOSITO,C.CAPANNI,
JRNL AUTH 2 F.BEMPORAD,G.PLAKOUTSI,M.STEFANI,F.CHITI,S.ZUCCOTTI,
JRNL AUTH 3 M.BOLOGNESI,P.VIGLINO
JRNL TITL STRUCTURE, CONFORMATIONAL STABILITY, AND ENZYMATIC
JRNL TITL 2 PROPERTIES OF ACYLPHOSPHATASE FROM THE HYPERTHERMOPHILE
JRNL TITL 3 SULFOLOBUS SOLFATARICUS
JRNL REF PROTEINS V. 62 64 2006
JRNL REFN ISSN 0887-3585
JRNL PMID 16287076
JRNL DOI 10.1002/PROT.20703
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.PLAKOUTSI,N.TADDEI,M.STEFANI,F.CHITI
REMARK 1 TITL AGGREGATION OF THE ACYLPHOSPHATASE FROM SULFOLOBUS
REMARK 1 TITL 2 SOLFATARICUS: THE FOLDED AND PARTIALLY UNFOLDED STATES CAN
REMARK 1 TITL 3 BOTH BE PRECURSORS FOR AMYLOID FORMATION
REMARK 1 REF J.BIOL.CHEM. V. 279 14111 2004
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 14724277
REMARK 1 DOI 10.1074/JBC.M312961200
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.M.THUNNISSEN,N.TADDEI,G.LIGURI,G.RAMPONI,P.NORDLUND
REMARK 1 TITL CRYSTAL STRUCTURE OF COMMON TYPE ACYLPHOSPHATASE FROM BOVINE
REMARK 1 TITL 2 TESTIS
REMARK 1 REF STRUCTURE V. 5 69 1997
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 9016712
REMARK 1 DOI 10.1016/S0969-2126(97)00167-6
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, DISCOVER 2.9.7
REMARK 3 AUTHORS : BRUKER BIOSPIN GMBH (XWINNMR), MOLECULAR
REMARK 3 SIMULATIONS INC. (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESTRAINED DIHEDRAL ANGLE MOLECULAR
REMARK 3 DYNAMICS SIMULATION WAS PERFORMED BY USING THE PROGRAM CYANA.
REMARK 3 THE 20 BEST STRUCTURES OF THE CYANA ENSEMBLE WERE SUBMITTED TO
REMARK 3 RESTRAINED MINIMIZATION USING DISCOVER WITH THE AMBER FORCE
REMARK 3 FIELD.
REMARK 4
REMARK 4 1Y9O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000031291.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 5.7
REMARK 210 IONIC STRENGTH : 50MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.4MM SSO ACP; 50MM PHOSPHATE
REMARK 210 BUFFER NA; 95% H2O, 5% D2O;
REMARK 210 0.4MM SSO ACP; 50MM PHOSPHATE
REMARK 210 BUFFER NA; 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, FELIX 2000, CYANA
REMARK 210 1.0.6
REMARK 210 METHOD USED : RESTRAINED MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES. SPECTRA WERE ACQUIRED WITHIN 36 HOURS
REMARK 210 FROM SAMPLE PREPARATION.
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: 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 1 GLU A 8 CD GLU A 8 OE2 0.111
REMARK 500 1 GLU A 11 CD GLU A 11 OE2 0.111
REMARK 500 1 GLU A 55 CD GLU A 55 OE2 0.110
REMARK 500 1 GLU A 59 CD GLU A 59 OE2 0.113
REMARK 500 1 GLU A 62 CD GLU A 62 OE2 0.110
REMARK 500 1 GLU A 63 CD GLU A 63 OE2 0.112
REMARK 500 1 GLU A 70 CD GLU A 70 OE2 0.111
REMARK 500 1 GLU A 80 CD GLU A 80 OE2 0.110
REMARK 500 1 GLU A 82 CD GLU A 82 OE2 0.111
REMARK 500 1 GLU A 90 CD GLU A 90 OE2 0.110
REMARK 500 1 GLU A 94 CD GLU A 94 OE2 0.113
REMARK 500 1 GLU A 96 CD GLU A 96 OE2 0.111
REMARK 500 1 GLU A 99 CD GLU A 99 OE2 0.111
REMARK 500 2 GLU A 8 CD GLU A 8 OE2 0.112
REMARK 500 2 GLU A 11 CD GLU A 11 OE2 0.112
REMARK 500 2 GLU A 55 CD GLU A 55 OE2 0.111
REMARK 500 2 GLU A 59 CD GLU A 59 OE2 0.111
REMARK 500 2 GLU A 62 CD GLU A 62 OE2 0.112
REMARK 500 2 GLU A 63 CD GLU A 63 OE2 0.111
REMARK 500 2 GLU A 70 CD GLU A 70 OE2 0.112
REMARK 500 2 GLU A 80 CD GLU A 80 OE2 0.110
REMARK 500 2 GLU A 82 CD GLU A 82 OE2 0.111
REMARK 500 2 GLU A 90 CD GLU A 90 OE2 0.110
REMARK 500 2 GLU A 94 CD GLU A 94 OE2 0.111
REMARK 500 2 GLU A 96 CD GLU A 96 OE2 0.112
REMARK 500 2 GLU A 99 CD GLU A 99 OE2 0.111
REMARK 500 3 GLU A 8 CD GLU A 8 OE2 0.112
REMARK 500 3 GLU A 11 CD GLU A 11 OE2 0.111
REMARK 500 3 GLU A 55 CD GLU A 55 OE2 0.110
REMARK 500 3 GLU A 59 CD GLU A 59 OE2 0.109
REMARK 500 3 GLU A 62 CD GLU A 62 OE2 0.112
REMARK 500 3 GLU A 63 CD GLU A 63 OE2 0.111
REMARK 500 3 GLU A 70 CD GLU A 70 OE2 0.112
REMARK 500 3 GLU A 80 CD GLU A 80 OE2 0.111
REMARK 500 3 GLU A 82 CD GLU A 82 OE2 0.111
REMARK 500 3 GLU A 90 CD GLU A 90 OE2 0.112
REMARK 500 3 GLU A 94 CD GLU A 94 OE2 0.111
REMARK 500 3 GLU A 96 CD GLU A 96 OE2 0.112
REMARK 500 3 GLU A 99 CD GLU A 99 OE2 0.111
REMARK 500 4 GLU A 8 CD GLU A 8 OE2 0.112
REMARK 500 4 GLU A 11 CD GLU A 11 OE2 0.112
REMARK 500 4 GLU A 55 CD GLU A 55 OE2 0.112
REMARK 500 4 GLU A 59 CD GLU A 59 OE2 0.114
REMARK 500 4 GLU A 62 CD GLU A 62 OE2 0.112
REMARK 500 4 GLU A 63 CD GLU A 63 OE2 0.110
REMARK 500 4 GLU A 70 CD GLU A 70 OE2 0.112
REMARK 500 4 GLU A 80 CD GLU A 80 OE2 0.111
REMARK 500 4 GLU A 82 CD GLU A 82 OE2 0.111
REMARK 500 4 GLU A 90 CD GLU A 90 OE2 0.112
REMARK 500 4 GLU A 94 CD GLU A 94 OE2 0.111
REMARK 500
REMARK 500 THIS ENTRY HAS 260 BOND 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 1 MET A 1 -57.47 -129.63
REMARK 500 1 THR A 7 97.46 69.74
REMARK 500 1 PHE A 10 -99.21 -137.46
REMARK 500 1 MET A 12 168.35 66.30
REMARK 500 1 TYR A 45 139.99 -170.76
REMARK 500 1 ASP A 51 26.54 -151.14
REMARK 500 1 VAL A 57 61.03 -118.52
REMARK 500 1 TYR A 61 -92.49 -71.99
REMARK 500 1 GLU A 62 -80.41 -154.57
REMARK 500 1 ALA A 78 43.20 -81.37
REMARK 500 1 LYS A 83 71.59 -166.09
REMARK 500 1 VAL A 84 94.35 -65.67
REMARK 500 1 SER A 89 -152.30 -127.69
REMARK 500 1 ASP A 97 -160.46 66.44
REMARK 500 2 MET A 1 44.77 -158.51
REMARK 500 2 ASP A 6 -63.14 -160.80
REMARK 500 2 PHE A 10 -98.23 -139.38
REMARK 500 2 LEU A 13 144.23 61.39
REMARK 500 2 ARG A 30 -73.57 73.51
REMARK 500 2 ASP A 51 -43.68 173.94
REMARK 500 2 TYR A 61 -98.94 -89.74
REMARK 500 2 GLU A 62 -73.75 -152.14
REMARK 500 2 GLN A 74 47.61 -93.09
REMARK 500 2 ALA A 78 48.12 -83.24
REMARK 500 2 ASP A 97 -161.32 67.92
REMARK 500 3 TRP A 4 73.20 21.11
REMARK 500 3 SER A 5 60.28 -106.63
REMARK 500 3 PHE A 10 -19.76 -144.62
REMARK 500 3 LEU A 13 127.84 66.68
REMARK 500 3 PHE A 29 -59.69 66.65
REMARK 500 3 ARG A 30 -37.78 -38.78
REMARK 500 3 TYR A 45 144.20 -175.26
REMARK 500 3 VAL A 57 62.77 -116.39
REMARK 500 3 ALA A 78 48.83 -82.31
REMARK 500 3 SER A 89 -161.89 -127.21
REMARK 500 3 GLU A 96 91.31 63.51
REMARK 500 3 ASP A 97 179.72 68.53
REMARK 500 4 THR A 7 85.95 65.00
REMARK 500 4 GLU A 8 57.62 -141.07
REMARK 500 4 PHE A 10 -95.95 -135.19
REMARK 500 4 LEU A 23 47.80 -88.67
REMARK 500 4 VAL A 24 41.62 -94.02
REMARK 500 4 VAL A 27 150.46 -48.38
REMARK 500 4 TYR A 45 141.64 -171.36
REMARK 500 4 PRO A 50 43.24 -83.07
REMARK 500 4 ASP A 51 47.77 -158.50
REMARK 500 4 GLN A 74 38.36 -94.94
REMARK 500 4 LYS A 83 76.12 -164.85
REMARK 500 4 VAL A 84 89.86 -67.21
REMARK 500 4 ASP A 97 -162.76 68.68
REMARK 500
REMARK 500 THIS ENTRY HAS 251 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR A 100 TYR A 101 19 148.88
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 1 PHE A 29 0.08 SIDE CHAIN
REMARK 500 1 TYR A 45 0.07 SIDE CHAIN
REMARK 500 1 TYR A 61 0.10 SIDE CHAIN
REMARK 500 2 TYR A 17 0.09 SIDE CHAIN
REMARK 500 4 PHE A 29 0.14 SIDE CHAIN
REMARK 500 4 TYR A 61 0.08 SIDE CHAIN
REMARK 500 5 TYR A 17 0.10 SIDE CHAIN
REMARK 500 5 ARG A 71 0.09 SIDE CHAIN
REMARK 500 6 TYR A 17 0.06 SIDE CHAIN
REMARK 500 6 TYR A 21 0.07 SIDE CHAIN
REMARK 500 7 ARG A 30 0.09 SIDE CHAIN
REMARK 500 8 PHE A 29 0.09 SIDE CHAIN
REMARK 500 8 TYR A 101 0.07 SIDE CHAIN
REMARK 500 9 PHE A 29 0.09 SIDE CHAIN
REMARK 500 9 TYR A 45 0.07 SIDE CHAIN
REMARK 500 9 TYR A 61 0.11 SIDE CHAIN
REMARK 500 9 ARG A 71 0.09 SIDE CHAIN
REMARK 500 10 TYR A 45 0.07 SIDE CHAIN
REMARK 500 11 TYR A 91 0.06 SIDE CHAIN
REMARK 500 12 TYR A 91 0.10 SIDE CHAIN
REMARK 500 13 TYR A 17 0.08 SIDE CHAIN
REMARK 500 14 TYR A 45 0.13 SIDE CHAIN
REMARK 500 14 TYR A 61 0.11 SIDE CHAIN
REMARK 500 15 ARG A 71 0.08 SIDE CHAIN
REMARK 500 16 TYR A 45 0.08 SIDE CHAIN
REMARK 500 16 TYR A 91 0.07 SIDE CHAIN
REMARK 500 17 TYR A 45 0.07 SIDE CHAIN
REMARK 500 19 PHE A 29 0.11 SIDE CHAIN
REMARK 500 19 TYR A 101 0.08 SIDE CHAIN
REMARK 500 20 TYR A 91 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8393 RELATED DB: BMRB
DBREF 1Y9O A 1 101 UNP Q97ZL0 Q97ZL0_SULSO 1 101
SEQADV 1Y9O GLY A -1 UNP Q97ZL0 CLONING ARTIFACT
SEQADV 1Y9O SER A 0 UNP Q97ZL0 CLONING ARTIFACT
SEQRES 1 A 103 GLY SER MET LYS LYS TRP SER ASP THR GLU VAL PHE GLU
SEQRES 2 A 103 MET LEU LYS ARG MET TYR ALA ARG VAL TYR GLY LEU VAL
SEQRES 3 A 103 GLN GLY VAL GLY PHE ARG LYS PHE VAL GLN ILE HIS ALA
SEQRES 4 A 103 ILE ARG LEU GLY ILE LYS GLY TYR ALA LYS ASN LEU PRO
SEQRES 5 A 103 ASP GLY SER VAL GLU VAL VAL ALA GLU GLY TYR GLU GLU
SEQRES 6 A 103 ALA LEU SER LYS LEU LEU GLU ARG ILE LYS GLN GLY PRO
SEQRES 7 A 103 PRO ALA ALA GLU VAL GLU LYS VAL ASP TYR SER PHE SER
SEQRES 8 A 103 GLU TYR LYS GLY GLU PHE GLU ASP PHE GLU THR TYR
HELIX 1 1 GLY A 28 LEU A 40 1 13
HELIX 2 2 GLU A 62 GLY A 75 1 14
SHEET 1 A 5 ASP A 85 PHE A 88 0
SHEET 2 A 5 LYS A 14 VAL A 20 -1 N TYR A 17 O SER A 87
SHEET 3 A 5 VAL A 54 GLY A 60 -1 O VAL A 56 N ALA A 18
SHEET 4 A 5 GLY A 44 LYS A 47 -1 N TYR A 45 O VAL A 57
SHEET 5 A 5 PHE A 98 THR A 100 1 O GLU A 99 N ALA A 46
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