HEADER DNA BINDING PROTEIN 23-MAR-06 2GFU
TITLE NMR SOLUTION STRUCTURE OF THE PWWP DOMAIN OF MISMATCH REPAIR PROTEIN
TITLE 2 HMSH6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA MISMATCH REPAIR PROTEIN MSH6;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PWWP DOMAIN;
COMPND 5 SYNONYM: MUTS-ALPHA 160 KDA SUBUNIT, G/T MISMATCH BINDING PROTEIN,
COMPND 6 GTBP, GTMBP, P160;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 STAR;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET M30
KEYWDS PWWP DOMAIN, TUDOR DOMAIN, DNA BINDING, MISMATCH REPAIR, DNA BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.LAGURI,N.FRIEDRICH,M.AXT,B.GILQUIN,S.ZINN-JUSTIN,J.COUPRIE
REVDAT 3 10-NOV-21 2GFU 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2GFU 1 VERSN
REVDAT 1 10-APR-07 2GFU 0
JRNL AUTH C.LAGURI,I.DUBAND-GOULET,N.FRIEDRICH,M.AXT,P.BELIN,
JRNL AUTH 2 B.GILQUIN,S.ZINN-JUSTIN,J.COUPRIE
JRNL TITL THE PWWP DOMAIN OF MISMATCH REPAIR PROTEIN HMSH6 IS INVOLVED
JRNL TITL 2 IN DOUBLE STRANDED AND SINGLE STRANDED DNA BINDING
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : INCA 1.0
REMARK 3 AUTHORS : P. SAVARIN, B. GILQUIN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2GFU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037064.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.9
REMARK 210 IONIC STRENGTH : 225MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM PROTEIN CONCENTRATION, 225MM
REMARK 210 NACL, 50MM NAPHOSPHATE PH 6.9,
REMARK 210 1MM TSP 10% D2O, PROTEASE
REMARK 210 INHIBITORS (SIGMA)
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2000, NMRPIPE 1.0, INCA
REMARK 210 1.0
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 VAL A 96 HG SER A 108 1.58
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 1 PRO A 114 C - N - CA ANGL. DEV. = 11.1 DEGREES
REMARK 500 1 PHE A 133 CB - CG - CD2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 1 PHE A 133 CB - CG - CD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 1 PHE A 165 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 1 LEU A 183 CB - CG - CD2 ANGL. DEV. = 12.8 DEGREES
REMARK 500 2 SER A 87 N - CA - CB ANGL. DEV. = 9.2 DEGREES
REMARK 500 2 SER A 91 CB - CA - C ANGL. DEV. = 11.9 DEGREES
REMARK 500 2 TRP A 106 CB - CG - CD2 ANGL. DEV. = -8.3 DEGREES
REMARK 500 2 TRP A 106 CB - CG - CD1 ANGL. DEV. = 7.9 DEGREES
REMARK 500 3 TRP A 106 CB - CG - CD2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 3 TYR A 151 CB - CG - CD1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 PHE A 165 CB - CG - CD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 4 TRP A 105 CB - CG - CD2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 4 TRP A 106 CB - CG - CD2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 4 PHE A 133 CB - CG - CD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 4 TYR A 151 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 4 TYR A 151 CB - CG - CD1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 4 PHE A 165 CB - CG - CD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 4 LEU A 183 CB - CG - CD2 ANGL. DEV. = 12.4 DEGREES
REMARK 500 4 ARG A 190 CB - CA - C ANGL. DEV. = 12.1 DEGREES
REMARK 500 4 ARG A 190 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 5 PHE A 115 CB - CG - CD1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 5 HIS A 130 CA - CB - CG ANGL. DEV. = 11.1 DEGREES
REMARK 500 5 PHE A 133 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 5 PHE A 133 CB - CG - CD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 6 SER A 88 N - CA - CB ANGL. DEV. = 10.5 DEGREES
REMARK 500 6 TRP A 106 CB - CG - CD2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 6 PHE A 165 CB - CG - CD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 7 TRP A 106 N - CA - CB ANGL. DEV. = -11.1 DEGREES
REMARK 500 7 TRP A 106 CB - CG - CD2 ANGL. DEV. = -10.2 DEGREES
REMARK 500 7 TRP A 106 CB - CG - CD1 ANGL. DEV. = 9.3 DEGREES
REMARK 500 8 PHE A 133 CB - CG - CD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 8 PHE A 165 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 8 MET A 176 N - CA - CB ANGL. DEV. = 10.9 DEGREES
REMARK 500 9 TYR A 151 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 9 TYR A 151 CB - CG - CD1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 9 PHE A 165 CB - CG - CD1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 10 TRP A 106 CB - CG - CD2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 10 PHE A 134 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 10 PHE A 165 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 11 TRP A 105 CB - CG - CD2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 11 PHE A 133 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 11 PHE A 165 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 11 PHE A 165 CB - CG - CD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 12 SER A 91 CB - CA - C ANGL. DEV. = 12.4 DEGREES
REMARK 500 12 TYR A 103 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 12 TYR A 103 CB - CG - CD1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 12 PHE A 133 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 12 TYR A 151 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 12 THR A 152 C - N - CA ANGL. DEV. = 15.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 87 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 1 ALA A 69 40.51 -80.83
REMARK 500 1 LYS A 70 80.36 -159.14
REMARK 500 1 LEU A 72 -87.42 68.84
REMARK 500 1 LEU A 76 -113.82 -135.72
REMARK 500 1 ARG A 78 29.18 -148.17
REMARK 500 1 SER A 79 -59.94 67.64
REMARK 500 1 PRO A 82 -104.11 -82.03
REMARK 500 1 ALA A 83 -156.49 177.18
REMARK 500 1 THR A 86 23.46 -146.93
REMARK 500 1 SER A 88 89.58 66.52
REMARK 500 1 GLU A 101 80.70 -59.73
REMARK 500 1 PRO A 114 1.62 -47.66
REMARK 500 1 PHE A 115 31.65 -98.89
REMARK 500 1 ASP A 135 -102.92 -95.70
REMARK 500 1 ASP A 136 -62.69 -106.72
REMARK 500 1 TYR A 151 92.35 -44.09
REMARK 500 1 SER A 154 -11.76 -45.41
REMARK 500 1 LYS A 185 -100.79 -123.43
REMARK 500 1 ALA A 194 -95.11 42.97
REMARK 500 1 VAL A 195 58.07 -160.74
REMARK 500 1 SER A 196 48.71 -99.26
REMARK 500 2 ARG A 78 -60.13 143.19
REMARK 500 2 SER A 79 2.74 83.71
REMARK 500 2 VAL A 80 -11.50 92.53
REMARK 500 2 ALA A 83 -86.52 -114.60
REMARK 500 2 PRO A 85 37.98 -90.13
REMARK 500 2 THR A 86 67.80 -69.59
REMARK 500 2 SER A 87 29.55 115.02
REMARK 500 2 SER A 88 -73.43 79.03
REMARK 500 2 ASP A 89 60.15 66.96
REMARK 500 2 PHE A 115 40.01 -104.69
REMARK 500 2 PHE A 119 -25.63 -154.72
REMARK 500 2 LYS A 125 38.34 -146.62
REMARK 500 2 PHE A 134 63.77 -68.54
REMARK 500 2 ASP A 135 -118.22 -91.91
REMARK 500 2 THR A 152 -45.58 -173.08
REMARK 500 2 SER A 154 -18.78 -46.50
REMARK 500 2 SER A 167 90.94 -14.53
REMARK 500 2 LYS A 185 -98.70 -110.64
REMARK 500 2 ALA A 194 -114.34 58.97
REMARK 500 2 ASP A 197 16.38 91.23
REMARK 500 3 LEU A 72 176.80 77.51
REMARK 500 3 SER A 79 -102.35 66.77
REMARK 500 3 ALA A 83 -56.23 -147.73
REMARK 500 3 SER A 87 53.38 -93.27
REMARK 500 3 PRO A 114 0.62 -47.67
REMARK 500 3 PHE A 115 34.96 -99.57
REMARK 500 3 PHE A 119 -9.65 -148.42
REMARK 500 3 ASP A 135 -113.66 -102.46
REMARK 500 3 TYR A 151 -107.69 -18.56
REMARK 500
REMARK 500 THIS ENTRY HAS 349 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 152 GLY A 153 2 135.31
REMARK 500 TRP A 106 PRO A 107 4 149.34
REMARK 500 THR A 152 GLY A 153 6 140.65
REMARK 500 TRP A 106 PRO A 107 13 147.60
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 2 TYR A 111 0.12 SIDE CHAIN
REMARK 500 2 TYR A 151 0.08 SIDE CHAIN
REMARK 500 3 ARG A 190 0.08 SIDE CHAIN
REMARK 500 4 HIS A 130 0.10 SIDE CHAIN
REMARK 500 4 PHE A 134 0.08 SIDE CHAIN
REMARK 500 4 TYR A 151 0.09 SIDE CHAIN
REMARK 500 6 TYR A 151 0.10 SIDE CHAIN
REMARK 500 6 ARG A 190 0.10 SIDE CHAIN
REMARK 500 8 TYR A 166 0.07 SIDE CHAIN
REMARK 500 9 HIS A 130 0.10 SIDE CHAIN
REMARK 500 10 TYR A 111 0.15 SIDE CHAIN
REMARK 500 10 TYR A 151 0.12 SIDE CHAIN
REMARK 500 11 TYR A 103 0.07 SIDE CHAIN
REMARK 500 14 TYR A 111 0.10 SIDE CHAIN
REMARK 500 14 PHE A 134 0.08 SIDE CHAIN
REMARK 500 14 ARG A 190 0.13 SIDE CHAIN
REMARK 500 15 TYR A 111 0.10 SIDE CHAIN
REMARK 500 15 TYR A 151 0.07 SIDE CHAIN
REMARK 500 16 PHE A 134 0.08 SIDE CHAIN
REMARK 500 17 TYR A 111 0.07 SIDE CHAIN
REMARK 500 17 PHE A 134 0.09 SIDE CHAIN
REMARK 500 17 TYR A 151 0.14 SIDE CHAIN
REMARK 500 17 ARG A 190 0.09 SIDE CHAIN
REMARK 500 18 TYR A 103 0.07 SIDE CHAIN
REMARK 500 18 HIS A 130 0.10 SIDE CHAIN
REMARK 500 18 PHE A 133 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2GFU A 68 201 UNP P52701 MSH6_HUMAN 68 201
SEQADV 2GFU SER A 88 UNP P52701 CYS 88 ENGINEERED MUTATION
SEQADV 2GFU SER A 108 UNP P52701 CYS 108 ENGINEERED MUTATION
SEQADV 2GFU SER A 196 UNP P52701 CYS 196 ENGINEERED MUTATION
SEQRES 1 A 134 LYS ALA LYS ASN LEU ASN GLY GLY LEU ARG ARG SER VAL
SEQRES 2 A 134 ALA PRO ALA ALA PRO THR SER SER ASP PHE SER PRO GLY
SEQRES 3 A 134 ASP LEU VAL TRP ALA LYS MET GLU GLY TYR PRO TRP TRP
SEQRES 4 A 134 PRO SER LEU VAL TYR ASN HIS PRO PHE ASP GLY THR PHE
SEQRES 5 A 134 ILE ARG GLU LYS GLY LYS SER VAL ARG VAL HIS VAL GLN
SEQRES 6 A 134 PHE PHE ASP ASP SER PRO THR ARG GLY TRP VAL SER LYS
SEQRES 7 A 134 ARG LEU LEU LYS PRO TYR THR GLY SER LYS SER LYS GLU
SEQRES 8 A 134 ALA GLN LYS GLY GLY HIS PHE TYR SER ALA LYS PRO GLU
SEQRES 9 A 134 ILE LEU ARG ALA MET GLN ARG ALA ASP GLU ALA LEU ASN
SEQRES 10 A 134 LYS ASP LYS ILE LYS ARG LEU GLU LEU ALA VAL SER ASP
SEQRES 11 A 134 GLU PRO SER GLU
HELIX 1 1 LYS A 145 LEU A 148 5 4
HELIX 2 2 SER A 156 GLN A 160 5 5
HELIX 3 3 LYS A 169 LYS A 185 1 17
HELIX 4 4 LYS A 187 LEU A 193 1 7
SHEET 1 A 3 ARG A 121 LYS A 123 0
SHEET 2 A 3 SER A 126 PHE A 133 -1 O SER A 126 N ARG A 121
SHEET 3 A 3 THR A 139 SER A 144 -1 O THR A 139 N PHE A 133
SHEET 1 B 5 ARG A 121 LYS A 123 0
SHEET 2 B 5 SER A 126 PHE A 133 -1 O SER A 126 N ARG A 121
SHEET 3 B 5 TRP A 106 VAL A 110 -1 N VAL A 110 O PHE A 133
SHEET 4 B 5 LEU A 95 ALA A 98 -1 N ALA A 98 O TRP A 106
SHEET 5 B 5 LEU A 148 PRO A 150 -1 O LYS A 149 N TRP A 97
CISPEP 1 SER A 137 PRO A 138 1 -0.37
CISPEP 2 SER A 137 PRO A 138 2 -1.91
CISPEP 3 SER A 137 PRO A 138 3 0.75
CISPEP 4 SER A 137 PRO A 138 4 -1.57
CISPEP 5 SER A 137 PRO A 138 5 -0.67
CISPEP 6 SER A 137 PRO A 138 6 0.81
CISPEP 7 SER A 137 PRO A 138 7 -4.02
CISPEP 8 SER A 137 PRO A 138 8 -0.89
CISPEP 9 SER A 137 PRO A 138 9 1.25
CISPEP 10 SER A 137 PRO A 138 10 -5.30
CISPEP 11 SER A 137 PRO A 138 11 -2.02
CISPEP 12 SER A 137 PRO A 138 12 1.28
CISPEP 13 SER A 137 PRO A 138 13 -1.39
CISPEP 14 SER A 137 PRO A 138 14 3.18
CISPEP 15 SER A 137 PRO A 138 15 -3.76
CISPEP 16 SER A 137 PRO A 138 16 -2.42
CISPEP 17 SER A 137 PRO A 138 17 -5.63
CISPEP 18 SER A 137 PRO A 138 18 -2.71
CISPEP 19 SER A 137 PRO A 138 19 -1.09
CISPEP 20 SER A 137 PRO A 138 20 -2.07
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
(ATOM LINES ARE NOT SHOWN.)
END
