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PDBsum entry 2m55

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Top Page protein metals Protein-protein interface(s) links
Calcium binding protein/protein fibril PDB id
2m55
Jmol
Contents
Protein chains
148 a.a.
21 a.a.
Metals
_CA ×4
HEADER    CALCIUM BINDING PROTEIN/PROTEIN FIBRIL  13-FEB-13   2M55
TITLE     NMR STRUCTURE OF THE COMPLEX OF AN N-TERMINALLY ACETYLATED ALPHA-
TITLE    2 SYNUCLEIN PEPTIDE WITH CALMODULIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CALMODULIN;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CAM;
COMPND   5 ENGINEERED: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: ALPHA-SYNUCLEIN;
COMPND   8 CHAIN: B;
COMPND   9 FRAGMENT: UNP RESIDUES 1-19;
COMPND  10 SYNONYM: NON-A BETA COMPONENT OF AD AMYLOID, NON-A4 COMPONENT OF
COMPND  11 AMYLOID PRECURSOR, NACP;
COMPND  12 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CALML2,
SOURCE   6 CAM3, CAMC, CAMIII;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET30B;
SOURCE  11 MOL_ID: 2;
SOURCE  12 SYNTHETIC: YES;
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  14 ORGANISM_COMMON: HUMAN;
SOURCE  15 ORGANISM_TAXID: 9606
KEYWDS    PROTEIN/PEPTIDE, CA-BINDING, CALCIUM BINDING PROTEIN-PROTEIN FIBRIL
KEYWDS   2 COMPLEX
EXPDTA    SOLUTION NMR
NUMMDL    20
AUTHOR    J.M.GRUSCHUS,T.YAP,S.PISTOLESI,A.S.MALTSEV,J.C.LEE
REVDAT   3   25-DEC-13 2M55    1       SOURCE
REVDAT   2   18-DEC-13 2M55    1       JRNL
REVDAT   1   08-MAY-13 2M55    0
JRNL        AUTH   J.M.GRUSCHUS,T.L.YAP,S.PISTOLESI,A.S.MALTSEV,J.C.LEE
JRNL        TITL   NMR STRUCTURE OF CALMODULIN COMPLEXED TO AN N-TERMINALLY
JRNL        TITL 2 ACETYLATED ALPHA-SYNUCLEIN PEPTIDE.
JRNL        REF    BIOCHEMISTRY                  V.  52  3436 2013
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   23607618
JRNL        DOI    10.1021/BI400199P
REMARK   2
REMARK   2 RESOLUTION. NOT APPLICABLE.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR_NIH
REMARK   3   AUTHORS     : SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2M55 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-FEB-13.
REMARK 100 THE RCSB ID CODE IS RCSB103221.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210  EXPERIMENT TYPE                : NMR
REMARK 210  TEMPERATURE           (KELVIN) : 310
REMARK 210  PH                             : 6.36
REMARK 210  IONIC STRENGTH                 : NULL
REMARK 210  PRESSURE                       : AMBIENT
REMARK 210  SAMPLE CONTENTS                : 600 UM [U-99% 13C; U-99% 15N]
REMARK 210                                   CALMODULIN, 600 UM ALPHA-
REMARK 210                                   SYNUCLEIN, 50 MM MES, 100 MM
REMARK 210                                   POTASSIUM CHLORIDE, 3 MM CALCIUM
REMARK 210                                   ION, 95% H2O/5% D2O; 700 UM [U-
REMARK 210                                   13C; U-15N]-MET,VAL,PHE,GLY,LEU,
REMARK 210                                   ALA ALPHA-SYNUCLEIN, 700 UM
REMARK 210                                   CALMODULIN, 50 MM MES, 100 MM
REMARK 210                                   POTASSIUM CHLORIDE, 3 MM CALCIUM
REMARK 210                                   ION, 0.1% SODIUM AZIDE, 95% H2O/
REMARK 210                                   5% D2O; 150 UM [U-99% 13C; U-99%
REMARK 210                                   15N] CALMODULIN, 150 UM ALPHA-
REMARK 210                                   SYNUCLEIN, 50 MM MES, 100 MM
REMARK 210                                   POTASSIUM CHLORIDE, 3 MM CALCIUM
REMARK 210                                   ION, 10 MG/ML PF1 PHAGE, 95% H2O/
REMARK 210                                   5% D2O
REMARK 210
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D 1H-15N NOESY; 3D 1H-13C NOESY
REMARK 210                                   ALIPHATIC; 2D 1H-13C HSQC
REMARK 210                                   AROMATIC; 3D 1H-13C NOESY
REMARK 210                                   AROMATIC; 2D 1H-15N HSQC; 2D 1H-
REMARK 210                                   13C HSQC ALIPHATIC; 3D CBCA(CO)NH
REMARK 210  SPECTROMETER FIELD STRENGTH    : 900 MHZ; 800 MHZ; 600 MHZ
REMARK 210  SPECTROMETER MODEL             : AVANCE
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER
REMARK 210
REMARK 210  STRUCTURE DETERMINATION.
REMARK 210   SOFTWARE USED                 : X-PLOR_NIH
REMARK 210   METHOD USED                   : DGSA-DISTANCE GEOMETRY SIMULATED
REMARK 210                                   ANNEALING
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
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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   H    ASP A    95     OE2  GLU A   104              1.56
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 LEU A  39       16.84    -66.56
REMARK 500  1 LYS B 212      -80.33    -92.13
REMARK 500  2 LEU A  39       20.68    -69.54
REMARK 500  2 LYS B 212       -6.71   -166.58
REMARK 500  2 VAL B 216       -9.15    -50.50
REMARK 500  3 LEU A  39       19.42    -68.45
REMARK 500  3 ASP A 129       97.96    -68.57
REMARK 500  3 THR A 146       52.36    -94.04
REMARK 500  3 VAL B 215       -9.68    -55.47
REMARK 500  4 GLN A   3     -163.79     53.61
REMARK 500  4 LEU A  39       15.73    -66.72
REMARK 500  4 ASP A 129       97.37    -68.05
REMARK 500  4 LYS B 212     -106.14    -97.68
REMARK 500  5 LEU A  39       23.25    -69.71
REMARK 500  5 THR A  79      -73.01    -95.26
REMARK 500  5 THR A 146       56.39    -97.27
REMARK 500  5 GLU B 213      -93.46   -173.16
REMARK 500  5 VAL B 215       -5.09    -57.66
REMARK 500  6 LEU A  39       13.48    -69.92
REMARK 500  6 THR A  79      -65.10    -91.97
REMARK 500  6 GLU B 213      -52.32     71.70
REMARK 500  7 LEU A  39       20.28    -69.39
REMARK 500  7 THR A  79       47.20   -141.90
REMARK 500  7 GLU B 213     -104.05   -177.85
REMARK 500  8 LEU A  39       16.24    -65.33
REMARK 500  8 THR A 146       55.71    -96.36
REMARK 500  9 LEU A  39       18.15    -67.55
REMARK 500  9 GLU B 213     -103.77    177.62
REMARK 500  9 ALA B 217       30.00    -73.16
REMARK 500 10 LEU A  39       22.04    -69.03
REMARK 500 10 THR A  79      -77.20   -102.05
REMARK 500 10 THR A 146       42.65    -74.21
REMARK 500 10 VAL B 203       -6.54    -59.19
REMARK 500 10 VAL B 215       -7.83    -57.89
REMARK 500 10 ALA B 217       21.29    -70.29
REMARK 500 11 LEU A  39       22.18    -66.76
REMARK 500 11 THR A  79      -67.97    -97.82
REMARK 500 11 THR A 146       42.15    -73.53
REMARK 500 12 LEU A  39       21.65    -66.95
REMARK 500 12 THR A  79      -69.77    -94.21
REMARK 500 12 ASP A 133      -20.06     62.24
REMARK 500 12 LYS B 212      -32.59   -156.97
REMARK 500 12 ALA B 217        8.32    -63.25
REMARK 500 13 LEU A  39       18.21    -67.53
REMARK 500 13 ASP A  78     -178.95   -170.39
REMARK 500 13 ASP A 129       97.81    -68.80
REMARK 500 13 LYS B 212      -73.97    -97.76
REMARK 500 14 LEU A  39       21.82    -66.45
REMARK 500 14 ASP A  80      -34.27     75.81
REMARK 500 14 LYS B 212      -71.60   -106.97
REMARK 500
REMARK 500 THIS ENTRY HAS      77 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                           1  CA A 303  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129   OD1
REMARK 620 2 GLU A 140   OE1 142.3
REMARK 620 3 ASP A 131   OD1  85.7  90.0
REMARK 620 4 GLN A 135   O   143.3  71.3 114.6
REMARK 620 5 GLU A 140   OE2  97.2  50.2  58.5 119.4
REMARK 620 6 ASP A 133   OD1 102.5 112.6  75.8  57.9 128.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                           1  CA A 300  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A  26   O
REMARK 620 2 GLU A  31   OE2 101.8
REMARK 620 3 ASP A  24   OD2  98.3 145.8
REMARK 620 4 ASP A  22   OD2 163.3  63.4  98.4
REMARK 620 5 ASP A  20   OD1  56.4  55.5 118.4 114.3
REMARK 620 6 GLU A  31   OE1 101.0  49.5 150.3  63.8  91.2
REMARK 620 7 ASP A  24   OD1  65.6 121.0  46.1 127.7  73.2 163.2
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                           1  CA A 301  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A  58   OD2
REMARK 620 2 THR A  62   O   109.6
REMARK 620 3 ASN A  60   OD1  71.2  67.9
REMARK 620 4 ASP A  56   OD1 110.5 125.1  91.8
REMARK 620 5 GLU A  67   OE2  72.5 124.5 143.7 102.3
REMARK 620 6 ASP A  58   OD1  51.1 129.0  61.2  61.5  96.5
REMARK 620 7 GLU A  67   OE1 108.3  83.0 147.8 116.9  47.9 144.3
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                           1  CA A 302  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A  93   OD1
REMARK 620 2 ASN A  97   OD1  68.9
REMARK 620 3 TYR A  99   O    73.9  50.9
REMARK 620 4 ASP A  95   OD2 134.8 125.8 150.9
REMARK 620 5 GLU A 104   OE2  72.9 133.7 137.5  68.9
REMARK 620 6 GLU A 104   OE1  70.8 134.3  97.5  98.0  46.4
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 19036   RELATED DB: BMRB
DBREF  2M55 A    1   148  UNP    P62158   CALM_HUMAN       2    149
DBREF  2M55 B  201   219  UNP    P37840   SYUA_HUMAN       1     19
SEQADV 2M55 ACE B  200  UNP  P37840              ACETYLATION
SEQADV 2M55 NH2 B  220  UNP  P37840              AMIDATION
SEQRES   1 A  148  ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES   2 A  148  GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES   3 A  148  ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES   4 A  148  GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES   5 A  148  ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES   6 A  148  PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP
SEQRES   7 A  148  THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL
SEQRES   8 A  148  PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU
SEQRES   9 A  148  LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR
SEQRES  10 A  148  ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE
SEQRES  11 A  148  ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN
SEQRES  12 A  148  MET MET THR ALA LYS
SEQRES   1 B   21  ACE MET ASP VAL PHE MET LYS GLY LEU SER LYS ALA LYS
SEQRES   2 B   21  GLU GLY VAL VAL ALA ALA ALA NH2
HET    ACE  B 200       6
HET    NH2  B 220       3
HET     CA  A 300       1
HET     CA  A 301       1
HET     CA  A 302       1
HET     CA  A 303       1
HETNAM     ACE ACETYL GROUP
HETNAM     NH2 AMINO GROUP
HETNAM      CA CALCIUM ION
FORMUL   2  ACE    C2 H4 O
FORMUL   2  NH2    H2 N
FORMUL   3   CA    4(CA 2+)
HELIX    1   1 THR A    5  ASP A   20  1                                  16
HELIX    2   2 THR A   28  LEU A   39  1                                  12
HELIX    3   3 THR A   44  ASP A   56  1                                  13
HELIX    4   4 PHE A   65  ASP A   78  1                                  14
HELIX    5   5 ASP A   80  ASP A   93  1                                  14
HELIX    6   6 SER A  101  LEU A  112  1                                  12
HELIX    7   7 THR A  117  ASP A  129  1                                  13
HELIX    8   8 TYR A  138  THR A  146  1                                   9
HELIX    9   9 MET B  201  ALA B  217  1                                  17
SHEET    1   A 2 THR A  26  ILE A  27  0
SHEET    2   A 2 ILE A  63  ASP A  64 -1  O  ILE A  63   N  ILE A  27
SHEET    1   B 2 TYR A  99  ILE A 100  0
SHEET    2   B 2 VAL A 136  ASN A 137 -1  O  VAL A 136   N  ILE A 100
LINK         C   ACE B 200                 N   MET B 201     1555   1555  1.30
LINK         C   ALA B 219                 N   NH2 B 220     1555   1555  1.31
LINK         OD1 ASP A 129                CA    CA A 303     1555   1555  2.20
LINK         O   THR A  26                CA    CA A 300     1555   1555  2.22
LINK         OE2 GLU A  31                CA    CA A 300     1555   1555  2.76
LINK         OD2 ASP A  58                CA    CA A 301     1555   1555  2.66
LINK         OE1 GLU A 140                CA    CA A 303     1555   1555  2.29
LINK         O   THR A  62                CA    CA A 301     1555   1555  2.32
LINK         OD1 ASP A 131                CA    CA A 303     1555   1555  2.39
LINK         OD1 ASP A  93                CA    CA A 302     1555   1555  2.56
LINK         OD1 ASN A  60                CA    CA A 301     1555   1555  2.56
LINK         OD1 ASP A  56                CA    CA A 301     1555   1555  2.57
LINK         O   GLN A 135                CA    CA A 303     1555   1555  2.61
LINK         OE2 GLU A  67                CA    CA A 301     1555   1555  2.61
LINK         OD1 ASN A  97                CA    CA A 302     1555   1555  2.67
LINK         O   TYR A  99                CA    CA A 302     1555   1555  2.68
LINK         OD2 ASP A  24                CA    CA A 300     1555   1555  2.68
LINK         OD2 ASP A  22                CA    CA A 300     1555   1555  2.69
LINK         OD1 ASP A  20                CA    CA A 300     1555   1555  2.69
LINK         OD2 ASP A  95                CA    CA A 302     1555   1555  2.70
LINK         OE2 GLU A 104                CA    CA A 302     1555   1555  2.76
LINK         OE2 GLU A 140                CA    CA A 303     1555   1555  2.71
LINK         OE1 GLU A  31                CA    CA A 300     1555   1555  2.27
LINK         OD1 ASP A  58                CA    CA A 301     1555   1555  2.27
LINK         OD1 ASP A 133                CA    CA A 303     1555   1555  2.32
LINK         OE1 GLU A  67                CA    CA A 301     1555   1555  2.70
LINK         OE1 GLU A 104                CA    CA A 302     1555   1555  2.71
LINK         OD1 ASP A  24                CA    CA A 300     1555   1555  2.82
SITE     1 AC1  6 ASP A  20  ASP A  22  ASP A  24  THR A  26
SITE     2 AC1  6 THR A  28  GLU A  31
SITE     1 AC2  5 ASP A  56  ASP A  58  ASN A  60  THR A  62
SITE     2 AC2  5 GLU A  67
SITE     1 AC3  5 ASP A  93  ASP A  95  ASN A  97  TYR A  99
SITE     2 AC3  5 GLU A 104
SITE     1 AC4  5 ASP A 129  ASP A 131  ASP A 133  GLN A 135
SITE     2 AC4  5 GLU A 140
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
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 References