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PDBsum entry 2yt0

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Protein binding PDB id
2yt0
Jmol
Contents
Protein chain
176 a.a.
HEADER    PROTEIN BINDING                         05-APR-07   2YT0
TITLE     SOLUTION STRUCTURE OF THE CHIMERA OF THE C-TERMINAL TAIL
TITLE    2 PEPTIDE OF APP AND THE C-TERMINAL PID DOMAIN OF FE65L
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: AMYLOID BETA A4 PROTEIN AND AMYLOID BETA A4
COMPND   3 PRECURSOR PROTEIN-BINDING FAMILY B MEMBER 2;
COMPND   4 CHAIN: A;
COMPND   5 FRAGMENT: APP PEPTIDE AND PID DOMAIN;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   3 ORGANISM_COMMON: MOUSE;
SOURCE   4 ORGANISM_TAXID: 10090;
SOURCE   5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   6 EXPRESSION_SYSTEM_PLASMID: P060710-06;
SOURCE   7 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS    CHIMERA, FE65L, PID DOMAIN, AMYLOID PRECURSOR PROTEIN,
KEYWDS   2 STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS   3 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS   4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, PROTEIN BINDING
EXPDTA    SOLUTION NMR
NUMMDL    20
AUTHOR    H.LI,S.KOSHIBA,N.TOCHIO,S.WATANABE,T.HARADA,T.KIGAWA,
AUTHOR   2 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE
AUTHOR   3 (RSGI)
REVDAT   4   24-FEB-09 2YT0    1       VERSN
REVDAT   3   04-NOV-08 2YT0    1       JRNL
REVDAT   2   02-SEP-08 2YT0    1       SEQADV
REVDAT   1   08-APR-08 2YT0    0
JRNL        AUTH   H.LI,S.KOSHIBA,F.HAYASHI,N.TOCHIO,T.TOMIZAWA,
JRNL        AUTH 2 T.KASAI,T.YABUKI,Y.MOTODA,T.HARADA,S.WATANABE,
JRNL        AUTH 3 M.INOUE,Y.HAYASHIZAKI,A.TANAKA,T.KIGAWA,S.YOKOYAMA
JRNL        TITL   STRUCTURE OF THE C-TERMINAL PHOSPHOTYROSINE
JRNL        TITL 2 INTERACTION DOMAIN OF FE65L1 COMPLEXED WITH THE
JRNL        TITL 3 CYTOPLASMIC TAIL OF AMYLOID PRECURSOR PROTEIN
JRNL        TITL 4 REVEALS A NOVEL PEPTIDE BINDING MODE
JRNL        REF    J.BIOL.CHEM.                  V. 283 27165 2008
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   18650440
JRNL        DOI    10.1074/JBC.M803892200
REMARK   1
REMARK   2
REMARK   2 RESOLUTION. NOT APPLICABLE.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CYANA 2.0.17
REMARK   3   AUTHORS     : GUNTERT, P.
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2YT0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-JUN-07.
REMARK 100 THE RCSB ID CODE IS RCSB027096.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210  EXPERIMENT TYPE                : NMR
REMARK 210  TEMPERATURE           (KELVIN) : 296
REMARK 210  PH                             : 7.0
REMARK 210  IONIC STRENGTH                 : 120MM
REMARK 210  PRESSURE                       : AMBIENT
REMARK 210  SAMPLE CONTENTS                : 1.04MM CHIMERA SAMPLE U-15N,
REMARK 210                                   13C; 20MM D-TRIS-HCL; 100MM
REMARK 210                                   NACL; 1MM D-DTT; 0.02% NAN3;
REMARK 210                                   90% H2O, 10% D2O
REMARK 210
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D_13C-SEPARATED_NOESY, 3D_
REMARK 210                                   15N-SEPARATED_NOESY
REMARK 210  SPECTROMETER FIELD STRENGTH    : 900 MHZ
REMARK 210  SPECTROMETER MODEL             : AVANCE
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER
REMARK 210
REMARK 210  STRUCTURE DETERMINATION.
REMARK 210   SOFTWARE USED                 : XWINNMR 3.5, NMRPIPE
REMARK 210                                   20031121, NMRVIEW 5.0.4,
REMARK 210                                   KUJIRA 0.9820, CYANA 2.0.17
REMARK 210   METHOD USED                   : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LEAST
REMARK 210                                   RESTRAINT VIOLATIONS, TARGET
REMARK 210                                   FUNCTION
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 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 SER A   2      105.66    -52.24
REMARK 500  1 ASN A  24      -60.14   -103.42
REMARK 500  1 PHE A  34       38.64    -81.20
REMARK 500  1 SER A  45      106.27    -51.38
REMARK 500  1 VAL A  61      141.38   -172.85
REMARK 500  1 VAL A 113       95.52    -69.52
REMARK 500  1 GLU A 120       41.68    -81.81
REMARK 500  1 PRO A 163        0.17    -69.74
REMARK 500  2 SER A   3      103.31    -51.12
REMARK 500  2 ALA A   9      179.63    -56.41
REMARK 500  2 LYS A  32      -70.04    -63.14
REMARK 500  2 SER A  42       33.03     37.85
REMARK 500  2 PRO A  56       93.35    -69.78
REMARK 500  2 TRP A  99      109.68    -56.65
REMARK 500  2 GLU A 121       76.85   -103.87
REMARK 500  3 ASP A   8      108.29    -35.23
REMARK 500  3 ALA A  10      126.40   -172.63
REMARK 500  3 PRO A  13        1.92    -69.72
REMARK 500  3 SER A  19      -71.99    -51.43
REMARK 500  3 MET A  37       47.46     34.58
REMARK 500  3 THR A  55      151.11    -39.02
REMARK 500  3 PRO A  56       95.41    -69.73
REMARK 500  3 VAL A 122       54.99     34.63
REMARK 500  3 ALA A 166      -36.71    -39.05
REMARK 500  4 SER A   3      -62.05   -108.12
REMARK 500  4 ALA A  10       52.06    -93.15
REMARK 500  4 PRO A  13        2.62    -69.72
REMARK 500  4 PHE A  34      -37.18   -131.13
REMARK 500  4 MET A  37       34.26     34.54
REMARK 500  4 SER A  42      112.15    -34.53
REMARK 500  4 SER A  46      162.19    -49.53
REMARK 500  4 SER A  51      134.99    -35.91
REMARK 500  4 PRO A  54       99.83    -69.73
REMARK 500  4 LYS A  57      111.81    -38.46
REMARK 500  4 VAL A 168      -72.33    -48.61
REMARK 500  5 SER A   3      135.61   -174.38
REMARK 500  5 SER A  19      -72.19    -56.52
REMARK 500  5 TYR A  31      -71.36    -64.59
REMARK 500  5 PRO A  56     -179.55    -69.77
REMARK 500  5 VAL A 106       50.77   -118.87
REMARK 500  5 VAL A 113       94.05    -69.85
REMARK 500  5 GLU A 120       41.69    -81.65
REMARK 500  6 ALA A   9       43.09   -108.23
REMARK 500  6 ALA A  10      118.63   -174.16
REMARK 500  6 ASN A  24      -68.02    -97.50
REMARK 500  6 TYR A  31      -35.47    -37.59
REMARK 500  6 GLU A  35      -76.91    -55.62
REMARK 500  6 GLN A  36       91.60    -58.07
REMARK 500  6 SER A  46      115.18   -164.99
REMARK 500  6 SER A  52      109.93    -55.49
REMARK 500  6 PRO A  54     -176.99    -69.77
REMARK 500  6 THR A  55      141.33    -37.07
REMARK 500  6 GLU A  59      -51.70   -124.18
REMARK 500  6 GLU A 121       78.67   -110.96
REMARK 500  6 SER A 132      -64.74    -94.92
REMARK 500  6 PRO A 163        0.60    -69.82
REMARK 500  6 ALA A 165       40.45   -100.80
REMARK 500  7 ALA A   9       38.99    -96.88
REMARK 500  7 PRO A  54       95.96    -69.71
REMARK 500  7 ASP A  81      -37.18    -38.76
REMARK 500  7 GLU A 120       32.59    -93.49
REMARK 500  7 VAL A 122       51.74     33.95
REMARK 500  8 GLN A  23      -61.40    -92.11
REMARK 500  8 ASN A  24      -68.83    -95.79
REMARK 500  8 GLN A  36       53.36    -98.44
REMARK 500  8 SER A  40      108.03    -49.83
REMARK 500  8 SER A  42      108.47    -46.10
REMARK 500  8 SER A  43      152.15    -39.11
REMARK 500  8 VAL A 113       90.18    -68.87
REMARK 500  8 GLU A 120       37.55    -89.76
REMARK 500  8 SER A 132      -65.30    -91.49
REMARK 500  8 PRO A 163        0.04    -69.75
REMARK 500  8 VAL A 168      -72.50    -63.82
REMARK 500  9 ALA A   9       51.87     38.52
REMARK 500  9 ASN A  24      -60.14   -106.63
REMARK 500  9 PHE A  33      171.30    -59.72
REMARK 500  9 PHE A  34      -57.44   -122.54
REMARK 500  9 MET A  37       45.58    -85.58
REMARK 500  9 THR A  55      138.50    -35.09
REMARK 500  9 GLU A 120       39.93    -82.33
REMARK 500  9 SER A 132      -65.72    -97.77
REMARK 500  9 PRO A 163        0.23    -69.72
REMARK 500 10 SER A   2       92.20    -56.59
REMARK 500 10 ALA A   9       91.96    -67.94
REMARK 500 10 ALA A  10      106.50   -170.95
REMARK 500 10 ASN A  24      -65.99   -103.85
REMARK 500 10 TYR A  31      -70.54    -67.60
REMARK 500 10 MET A  37       35.86     34.50
REMARK 500 10 GLN A  38       76.41   -108.87
REMARK 500 10 ASN A  39       38.10    -93.49
REMARK 500 10 PRO A  54       96.64    -69.75
REMARK 500 10 THR A  55      147.43    -37.49
REMARK 500 10 LEU A  60      134.12    -36.63
REMARK 500 10 GLU A 120       38.88    -83.17
REMARK 500 10 LEU A 131      136.99    -39.85
REMARK 500 10 ASN A 151      -63.76    -91.72
REMARK 500 10 ALA A 165       30.34    -92.35
REMARK 500 10 VAL A 168      -73.56    -67.40
REMARK 500 10 SER A 169      -34.49    -34.63
REMARK 500 11 SER A   6      137.33   -175.03
REMARK 500 11 ASP A   8      151.55    -42.45
REMARK 500 11 TYR A  31      -39.22    -35.67
REMARK 500 11 GLN A  38      -44.80   -130.94
REMARK 500 11 SER A  43       98.62    -63.00
REMARK 500 11 SER A  52       91.00    -65.64
REMARK 500 11 GLU A 121       79.94   -116.26
REMARK 500 11 ASN A 151      -62.94   -108.60
REMARK 500 11 ALA A 165       42.16    -79.81
REMARK 500 12 SER A  46       92.95    -65.85
REMARK 500 12 GLU A 120       41.05    -83.84
REMARK 500 12 SER A 132      -69.71   -103.74
REMARK 500 12 PRO A 163        0.99    -69.74
REMARK 500 12 ALA A 165       31.45    -96.83
REMARK 500 13 SER A   6       39.71    -89.37
REMARK 500 13 PHE A  34      -50.07   -126.35
REMARK 500 13 PRO A  56     -166.37    -69.75
REMARK 500 13 LYS A  57       40.61     38.88
REMARK 500 13 GLU A 120       31.02    -98.10
REMARK 500 13 GLU A 121       77.80   -114.83
REMARK 500 13 SER A 132      -62.03   -104.48
REMARK 500 14 PRO A  13        6.82    -69.78
REMARK 500 14 ARG A  16      -33.81    -38.25
REMARK 500 14 HIS A  17      -66.14    -91.12
REMARK 500 14 TYR A  31      -34.73    -37.07
REMARK 500 14 LYS A  32      -60.91    -95.29
REMARK 500 14 ASP A  81      -36.91    -36.42
REMARK 500 14 TRP A  99      109.42    -57.58
REMARK 500 14 GLU A 120       31.60    -85.69
REMARK 500 14 VAL A 122       72.25   -103.02
REMARK 500 14 MET A 134      118.61   -161.88
REMARK 500 14 THR A 149       33.62    -98.03
REMARK 500 14 PRO A 163        0.05    -69.80
REMARK 500 15 GLN A  23      -63.71    -91.34
REMARK 500 15 TYR A  31      -70.44    -77.73
REMARK 500 15 MET A  37       43.57   -102.91
REMARK 500 15 GLN A  38       43.65    -96.44
REMARK 500 15 SER A  46      174.95    -50.65
REMARK 500 15 SER A  49      131.74   -170.35
REMARK 500 15 PRO A  54     -177.81    -69.75
REMARK 500 15 GLU A 121       76.45   -107.20
REMARK 500 15 PRO A 163        0.19    -69.73
REMARK 500 15 ALA A 165       33.06    -96.59
REMARK 500 16 SER A   2      119.63   -169.37
REMARK 500 16 ALA A   9      179.47    -50.29
REMARK 500 16 PRO A  13        3.72    -69.76
REMARK 500 16 ASN A  24      -61.06   -107.47
REMARK 500 16 PHE A  34       72.39   -107.35
REMARK 500 16 THR A  55      143.03    -37.61
REMARK 500 16 PRO A  56       99.91    -69.76
REMARK 500 16 SER A 132      -63.60    -98.67
REMARK 500 16 ASN A 151       44.22     71.53
REMARK 500 16 SER A 169      -35.22    -35.12
REMARK 500 17 ALA A  10      113.88   -162.30
REMARK 500 17 PRO A  54     -174.93    -69.74
REMARK 500 17 LYS A  57      145.14    -38.42
REMARK 500 17 GLU A  59      -63.67   -121.24
REMARK 500 17 VAL A 113       92.17    -68.85
REMARK 500 17 GLN A 152       33.36     37.71
REMARK 500 17 PRO A 163        1.25    -69.76
REMARK 500 18 SER A   3      145.23    -38.49
REMARK 500 18 ALA A  10      126.68   -174.41
REMARK 500 18 PRO A  13        0.20    -69.76
REMARK 500 18 LEU A  18      -27.98    -37.63
REMARK 500 18 ASN A  24      -63.21   -107.85
REMARK 500 18 GLN A  36       73.65    -67.10
REMARK 500 18 GLU A 121       78.32   -106.74
REMARK 500 18 SER A 132      -63.55    -97.60
REMARK 500 18 PRO A 163        0.50    -69.71
REMARK 500 19 ASN A  24      -64.64   -102.86
REMARK 500 19 ASN A  39      103.62    -35.49
REMARK 500 19 PRO A  56       96.77    -69.78
REMARK 500 19 GLU A 120       37.11    -87.89
REMARK 500 19 PRO A 163        1.05    -69.79
REMARK 500 19 SER A 169      -34.93    -35.32
REMARK 500 20 SER A   6      -61.81   -100.68
REMARK 500 20 ASP A   8      164.52    -44.80
REMARK 500 20 GLN A  38       42.24     36.65
REMARK 500 20 PRO A  54     -178.05    -69.74
REMARK 500 20 ASN A  89      -70.61    -60.59
REMARK 500 20 SER A 132      -61.00    -92.39
REMARK 500 20 PRO A 163        1.50    -69.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TKR001324504.1   RELATED DB: TARGETDB
DBREF  2YT0 A    8    39  UNP    P12023   A4_MOUSE       739    770
DBREF  2YT0 A   54   176  UNP    Q9DBR4   APBB2_MOUSE    582    704
SEQADV 2YT0 GLY A    1  UNP  P12023              EXPRESSION TAG
SEQADV 2YT0 SER A    2  UNP  P12023              EXPRESSION TAG
SEQADV 2YT0 SER A    3  UNP  P12023              EXPRESSION TAG
SEQADV 2YT0 GLY A    4  UNP  P12023              EXPRESSION TAG
SEQADV 2YT0 SER A    5  UNP  P12023              EXPRESSION TAG
SEQADV 2YT0 SER A    6  UNP  P12023              EXPRESSION TAG
SEQADV 2YT0 GLY A    7  UNP  P12023              EXPRESSION TAG
SEQADV 2YT0 SER A   40  UNP  P12023              LINKER
SEQADV 2YT0 GLY A   41  UNP  P12023              LINKER
SEQADV 2YT0 SER A   42  UNP  P12023              LINKER
SEQADV 2YT0 SER A   43  UNP  P12023              LINKER
SEQADV 2YT0 GLY A   44  UNP  P12023              LINKER
SEQADV 2YT0 SER A   45  UNP  P12023              LINKER
SEQADV 2YT0 SER A   46  UNP  P12023              LINKER
SEQADV 2YT0 GLY A   47  UNP  P12023              LINKER
SEQADV 2YT0 SER A   48  UNP  P12023              LINKER
SEQADV 2YT0 SER A   49  UNP  P12023              LINKER
SEQADV 2YT0 GLY A   50  UNP  P12023              LINKER
SEQADV 2YT0 SER A   51  UNP  P12023              LINKER
SEQADV 2YT0 SER A   52  UNP  P12023              LINKER
SEQADV 2YT0 GLY A   53  UNP  P12023              LINKER
SEQRES   1 A  176  GLY SER SER GLY SER SER GLY ASP ALA ALA VAL THR PRO
SEQRES   2 A  176  GLU GLU ARG HIS LEU SER LYS MET GLN GLN ASN GLY TYR
SEQRES   3 A  176  GLU ASN PRO THR TYR LYS PHE PHE GLU GLN MET GLN ASN
SEQRES   4 A  176  SER GLY SER SER GLY SER SER GLY SER SER GLY SER SER
SEQRES   5 A  176  GLY PRO THR PRO LYS THR GLU LEU VAL GLN LYS PHE ARG
SEQRES   6 A  176  VAL GLN TYR LEU GLY MET LEU PRO VAL ASP ARG PRO VAL
SEQRES   7 A  176  GLY MET ASP THR LEU ASN SER ALA ILE GLU ASN LEU MET
SEQRES   8 A  176  THR SER SER SER LYS GLU ASP TRP PRO SER VAL ASN MET
SEQRES   9 A  176  ASN VAL ALA ASP ALA THR VAL THR VAL ILE SER GLU LYS
SEQRES  10 A  176  ASN GLU GLU GLU VAL LEU VAL GLU CYS ARG VAL ARG PHE
SEQRES  11 A  176  LEU SER PHE MET GLY VAL GLY LYS ASP VAL HIS THR PHE
SEQRES  12 A  176  ALA PHE ILE MET ASP THR GLY ASN GLN ARG PHE GLU CYS
SEQRES  13 A  176  HIS VAL PHE TRP CYS GLU PRO ASN ALA ALA ASN VAL SER
SEQRES  14 A  176  GLU ALA VAL GLN ALA ALA CYS
HELIX    1   1 PRO A   13  GLN A   22  1                                  10
HELIX    2   2 PRO A   29  PHE A   34  1                                   6
HELIX    3   3 MET A   80  SER A   93  1                                  14
HELIX    4   4 ALA A  166  CYS A  176  1                                  11
SHEET    1   A 8 TYR A  26  GLU A  27  0
SHEET    2   A 8 LEU A 131  VAL A 136 -1
SHEET    3   A 8 THR A 142  ASP A 148 -1
SHEET    4   A 8 PHE A 154  TRP A 160 -1
SHEET    5   A 8 GLN A  62  PRO A  73 -1
SHEET    6   A 8 SER A 101  ALA A 107 -1
SHEET    7   A 8 THR A 110  SER A 115 -1
SHEET    8   A 8 VAL A 122  ARG A 127 -1
CISPEP   1 GLU A  162    PRO A  163          1        -0.02
CISPEP   2 GLU A  162    PRO A  163          2         0.06
CISPEP   3 GLU A  162    PRO A  163          3         0.06
CISPEP   4 GLU A  162    PRO A  163          4        -0.03
CISPEP   5 GLU A  162    PRO A  163          5         0.09
CISPEP   6 GLU A  162    PRO A  163          6         0.04
CISPEP   7 GLU A  162    PRO A  163          7        -0.02
CISPEP   8 GLU A  162    PRO A  163          8        -0.02
CISPEP   9 GLU A  162    PRO A  163          9        -0.05
CISPEP  10 GLU A  162    PRO A  163         10         0.03
CISPEP  11 GLU A  162    PRO A  163         11        -0.05
CISPEP  12 GLU A  162    PRO A  163         12        -0.01
CISPEP  13 GLU A  162    PRO A  163         13        -0.02
CISPEP  14 GLU A  162    PRO A  163         14         0.04
CISPEP  15 GLU A  162    PRO A  163         15        -0.04
CISPEP  16 GLU A  162    PRO A  163         16         0.01
CISPEP  17 GLU A  162    PRO A  163         17         0.03
CISPEP  18 GLU A  162    PRO A  163         18        -0.05
CISPEP  19 GLU A  162    PRO A  163         19         0.03
CISPEP  20 GLU A  162    PRO A  163         20        -0.03
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
      
PROCHECK
Go to PROCHECK summary
 References