HEADER UNKNOWN FUNCTION 14-DEC-06 2JMZ
TITLE SOLUTION STRUCTURE OF A KLBA INTEIN PRECURSOR FROM METHANOCOCCUS
TITLE 2 JANNASCHII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN MJ0781;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MJA KLBA INTEIN, RESIDUES 1-180;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOCALDOCOCCUS JANNASCHII;
SOURCE 3 ORGANISM_TAXID: 2190;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PMJAKLBA
KEYWDS PROTEIN, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.A.JOHNSON,M.W.SOUTHWORTH,T.HERRMANN,L.BRACE,F.B.PERLER,K.A.WUTHRICH
REVDAT 4 20-DEC-23 2JMZ 1 REMARK
REVDAT 3 20-OCT-21 2JMZ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2JMZ 1 VERSN
REVDAT 1 10-JUL-07 2JMZ 0
JRNL AUTH M.A.JOHNSON,M.W.SOUTHWORTH,T.HERRMANN,L.BRACE,F.B.PERLER,
JRNL AUTH 2 K.WUTHRICH
JRNL TITL NMR STRUCTURE OF A KLBA INTEIN PRECURSOR FROM METHANOCOCCUS
JRNL TITL 2 JANNASCHII
JRNL REF PROTEIN SCI. V. 16 1316 2007
JRNL REFN ISSN 0961-8368
JRNL PMID 17586768
JRNL DOI 10.1110/PS.072816707
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ATNOS/CANDID 1.2, OPAL 1.2
REMARK 3 AUTHORS : HERRMANN, GUNTERT AND WUTHRICH (ATNOS/CANDID),
REMARK 3 LUGINBUHL, GUNTERT, BILLETER AND WUTHRICH (OPAL)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2JMZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-DEC-06.
REMARK 100 THE DEPOSITION ID IS D_1000100035.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 5.3
REMARK 210 IONIC STRENGTH : 0.12
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM [U-98% 15N] KLBA INTEIN
REMARK 210 PRECURSOR, 20 MM SODIUM
REMARK 210 PHOSPHATE, 100 MM SODIUM
REMARK 210 CHLORIDE, 2 MM SODIUM AZIDE, 90%
REMARK 210 H2O, 10% D2O; 2 MM [U-98% 13C, U-
REMARK 210 98% 15N] KLBA INTEIN PRECURSOR,
REMARK 210 20 MM SODIUM PHOSPHATE, 100 MM
REMARK 210 SODIUM CHLORIDE, 2 MM SODIUM
REMARK 210 AZIDE, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 1H-15N NOESY; 3D 1H-13C NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA 1.0.3
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 : TARGET 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 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
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 ARG A 95 CD - NE - CZ ANGL. DEV. = 8.7 DEGREES
REMARK 500 1 ARG A 95 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 ARG A 79 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 2 ARG A 95 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 2 HIS A 101 C - N - CA ANGL. DEV. = 17.1 DEGREES
REMARK 500 3 TYR A 126 CB - CG - CD1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 4 ARG A 95 CD - NE - CZ ANGL. DEV. = 9.9 DEGREES
REMARK 500 4 ARG A 95 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 7 TYR A 126 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 9 ARG A 73 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 9 VAL A 105 CA - CB - CG1 ANGL. DEV. = 10.2 DEGREES
REMARK 500 11 ARG A 79 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 15 VAL A 29 CA - CB - CG2 ANGL. DEV. = 10.9 DEGREES
REMARK 500 16 ARG A 95 CD - NE - CZ ANGL. DEV. = 13.3 DEGREES
REMARK 500 16 ARG A 95 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 16 ARG A 95 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 18 ASP A 138 CA - CB - CG ANGL. DEV. = 14.9 DEGREES
REMARK 500 20 ARG A 95 CD - NE - CZ ANGL. DEV. = 9.2 DEGREES
REMARK 500 20 ARG A 95 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
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 HIS A 5 -174.18 60.99
REMARK 500 1 ASP A 6 84.48 58.40
REMARK 500 1 TYR A 16 76.87 47.64
REMARK 500 1 SER A 18 0.32 -61.59
REMARK 500 1 ILE A 22 66.92 35.85
REMARK 500 1 TYR A 36 43.02 -90.13
REMARK 500 1 ILE A 40 95.88 -59.47
REMARK 500 1 ASN A 45 2.62 -68.91
REMARK 500 1 PHE A 47 -100.26 -86.64
REMARK 500 1 ASN A 56 -6.42 61.56
REMARK 500 1 SER A 61 -166.42 -107.43
REMARK 500 1 SER A 66 10.47 -149.10
REMARK 500 1 ASN A 93 20.03 -72.31
REMARK 500 1 ARG A 94 27.08 49.23
REMARK 500 1 ASP A 102 39.27 -91.63
REMARK 500 1 LYS A 109 78.06 -109.10
REMARK 500 1 VAL A 123 -1.55 -58.82
REMARK 500 1 LYS A 131 -145.59 -125.21
REMARK 500 1 ASN A 132 -82.02 -59.99
REMARK 500 1 ILE A 141 -88.58 29.32
REMARK 500 1 ASN A 149 24.35 -146.82
REMARK 500 1 ASN A 168 -85.13 68.31
REMARK 500 1 SER A 176 -149.68 -149.27
REMARK 500 1 SER A 177 -106.30 -149.41
REMARK 500 1 THR A 179 -172.03 68.23
REMARK 500 1 LEU A 180 81.68 -67.64
REMARK 500 1 HIS A 183 92.65 31.71
REMARK 500 1 HIS A 185 -128.22 -128.77
REMARK 500 2 ASN A 2 178.64 152.19
REMARK 500 2 HIS A 5 -70.84 -140.53
REMARK 500 2 ASP A 6 -171.94 59.16
REMARK 500 2 ALA A 8 165.94 161.80
REMARK 500 2 TYR A 36 39.31 -94.44
REMARK 500 2 PHE A 47 -90.80 -67.01
REMARK 500 2 ASN A 56 13.84 51.14
REMARK 500 2 ARG A 76 -166.05 -127.08
REMARK 500 2 SER A 83 104.29 -167.12
REMARK 500 2 HIS A 101 -23.98 96.33
REMARK 500 2 VAL A 123 0.06 -55.48
REMARK 500 2 ILE A 141 -77.85 26.51
REMARK 500 2 VAL A 157 64.66 23.12
REMARK 500 2 ASN A 168 -85.53 63.11
REMARK 500 2 ALA A 175 49.30 -144.11
REMARK 500 2 SER A 177 8.62 -60.77
REMARK 500 2 LEU A 180 121.86 66.05
REMARK 500 2 HIS A 184 52.38 -157.98
REMARK 500 2 HIS A 185 178.24 63.63
REMARK 500 3 ASN A 2 -179.56 80.77
REMARK 500 3 ALA A 10 -176.67 -68.38
REMARK 500 3 TYR A 16 66.09 29.78
REMARK 500
REMARK 500 THIS ENTRY HAS 413 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 ASP A 71 LYS A 72 1 140.99
REMARK 500 LEU A 99 THR A 100 2 -147.47
REMARK 500 HIS A 184 HIS A 185 2 -141.62
REMARK 500 GLY A 7 ALA A 8 3 140.88
REMARK 500 LYS A 88 ILE A 89 3 148.67
REMARK 500 TYR A 82 SER A 83 5 139.93
REMARK 500 PRO A 130 LYS A 131 6 149.93
REMARK 500 SER A 177 GLY A 178 8 145.62
REMARK 500 SER A 108 LYS A 109 9 148.15
REMARK 500 ASN A 133 THR A 134 9 -139.66
REMARK 500 HIS A 185 HIS A 186 9 143.55
REMARK 500 ASP A 154 LEU A 155 12 -149.05
REMARK 500 HIS A 101 ASP A 102 13 149.47
REMARK 500 ILE A 164 ALA A 165 16 149.12
REMARK 500 ASP A 71 LYS A 72 19 141.55
REMARK 500 SER A 174 ALA A 175 19 144.77
REMARK 500 ALA A 175 SER A 176 19 145.57
REMARK 500 HIS A 185 HIS A 186 19 -144.80
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 11 0.08 SIDE CHAIN
REMARK 500 2 TYR A 16 0.08 SIDE CHAIN
REMARK 500 2 TYR A 36 0.08 SIDE CHAIN
REMARK 500 2 ARG A 73 0.12 SIDE CHAIN
REMARK 500 2 ARG A 94 0.10 SIDE CHAIN
REMARK 500 3 TYR A 16 0.07 SIDE CHAIN
REMARK 500 3 ARG A 94 0.10 SIDE CHAIN
REMARK 500 3 TYR A 163 0.08 SIDE CHAIN
REMARK 500 4 TYR A 58 0.07 SIDE CHAIN
REMARK 500 4 TYR A 148 0.07 SIDE CHAIN
REMARK 500 5 TYR A 16 0.11 SIDE CHAIN
REMARK 500 5 ARG A 73 0.15 SIDE CHAIN
REMARK 500 6 TYR A 36 0.12 SIDE CHAIN
REMARK 500 6 ARG A 94 0.10 SIDE CHAIN
REMARK 500 7 TYR A 11 0.09 SIDE CHAIN
REMARK 500 7 TYR A 16 0.08 SIDE CHAIN
REMARK 500 7 TYR A 163 0.07 SIDE CHAIN
REMARK 500 8 TYR A 36 0.07 SIDE CHAIN
REMARK 500 9 TYR A 16 0.08 SIDE CHAIN
REMARK 500 10 TYR A 16 0.09 SIDE CHAIN
REMARK 500 10 ARG A 73 0.10 SIDE CHAIN
REMARK 500 10 TYR A 163 0.08 SIDE CHAIN
REMARK 500 11 TYR A 163 0.13 SIDE CHAIN
REMARK 500 12 TYR A 163 0.11 SIDE CHAIN
REMARK 500 13 TYR A 16 0.09 SIDE CHAIN
REMARK 500 13 ARG A 73 0.10 SIDE CHAIN
REMARK 500 13 ARG A 79 0.13 SIDE CHAIN
REMARK 500 13 TYR A 148 0.08 SIDE CHAIN
REMARK 500 14 TYR A 58 0.08 SIDE CHAIN
REMARK 500 14 ARG A 73 0.11 SIDE CHAIN
REMARK 500 15 TYR A 16 0.07 SIDE CHAIN
REMARK 500 16 ARG A 73 0.08 SIDE CHAIN
REMARK 500 17 TYR A 16 0.07 SIDE CHAIN
REMARK 500 17 TYR A 36 0.09 SIDE CHAIN
REMARK 500 17 TYR A 58 0.07 SIDE CHAIN
REMARK 500 18 TYR A 16 0.08 SIDE CHAIN
REMARK 500 18 TYR A 36 0.10 SIDE CHAIN
REMARK 500 19 TYR A 36 0.13 SIDE CHAIN
REMARK 500 19 ARG A 79 0.10 SIDE CHAIN
REMARK 500 19 ARG A 95 0.11 SIDE CHAIN
REMARK 500 19 TYR A 148 0.10 SIDE CHAIN
REMARK 500 19 TYR A 163 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 15061 RELATED DB: BMRB
DBREF 2JMZ A 1 180 UNP Q58191 Y781_METJA 398 577
SEQADV 2JMZ ALA A 175 UNP Q58191 ASN 572 ENGINEERED MUTATION
SEQADV 2JMZ SER A 176 UNP Q58191 CYS 573 ENGINEERED MUTATION
SEQADV 2JMZ HIS A 181 UNP Q58191 EXPRESSION TAG
SEQADV 2JMZ HIS A 182 UNP Q58191 EXPRESSION TAG
SEQADV 2JMZ HIS A 183 UNP Q58191 EXPRESSION TAG
SEQADV 2JMZ HIS A 184 UNP Q58191 EXPRESSION TAG
SEQADV 2JMZ HIS A 185 UNP Q58191 EXPRESSION TAG
SEQADV 2JMZ HIS A 186 UNP Q58191 EXPRESSION TAG
SEQRES 1 A 186 MET ASN THR GLY HIS ASP GLY ALA LEU ALA TYR ASP GLU
SEQRES 2 A 186 PRO ILE TYR LEU SER ASP GLY ASN ILE ILE ASN ILE GLY
SEQRES 3 A 186 GLU PHE VAL ASP LYS PHE PHE LYS LYS TYR LYS ASN SER
SEQRES 4 A 186 ILE LYS LYS GLU ASP ASN GLY PHE GLY TRP ILE ASP ILE
SEQRES 5 A 186 GLY ASN GLU ASN ILE TYR ILE LYS SER PHE ASN LYS LEU
SEQRES 6 A 186 SER LEU ILE ILE GLU ASP LYS ARG ILE LEU ARG VAL TRP
SEQRES 7 A 186 ARG LYS LYS TYR SER GLY LYS LEU ILE LYS ILE THR THR
SEQRES 8 A 186 LYS ASN ARG ARG GLU ILE THR LEU THR HIS ASP HIS PRO
SEQRES 9 A 186 VAL TYR ILE SER LYS THR GLY GLU VAL LEU GLU ILE ASN
SEQRES 10 A 186 ALA GLU MET VAL LYS VAL GLY ASP TYR ILE TYR ILE PRO
SEQRES 11 A 186 LYS ASN ASN THR ILE ASN LEU ASP GLU VAL ILE LYS VAL
SEQRES 12 A 186 GLU THR VAL ASP TYR ASN GLY HIS ILE TYR ASP LEU THR
SEQRES 13 A 186 VAL GLU ASP ASN HIS THR TYR ILE ALA GLY LYS ASN GLU
SEQRES 14 A 186 GLY PHE ALA VAL SER ALA SER SER GLY THR LEU HIS HIS
SEQRES 15 A 186 HIS HIS HIS HIS
HELIX 1 1 ASN A 24 TYR A 36 1 13
HELIX 2 2 GLU A 119 VAL A 121 5 3
SHEET 1 A 4 LEU A 9 ALA A 10 0
SHEET 2 A 4 ILE A 152 THR A 156 -1 O TYR A 153 N LEU A 9
SHEET 3 A 4 ARG A 76 LYS A 80 -1 N TRP A 78 O ASP A 154
SHEET 4 A 4 TRP A 49 ASP A 51 -1 N ILE A 50 O VAL A 77
SHEET 1 B 2 TYR A 58 LYS A 60 0
SHEET 2 B 2 ASP A 71 ARG A 73 -1 O LYS A 72 N ILE A 59
SHEET 1 C 2 GLY A 84 ILE A 87 0
SHEET 2 C 2 THR A 145 TYR A 148 -1 O TYR A 148 N GLY A 84
SHEET 1 D 2 PRO A 104 LYS A 109 0
SHEET 2 D 2 GLU A 112 ASN A 117 -1 O GLU A 112 N LYS A 109
SHEET 1 E 2 TYR A 126 PRO A 130 0
SHEET 2 E 2 ILE A 135 GLU A 139 -1 O ASN A 136 N ILE A 129
SHEET 1 F 2 THR A 162 ALA A 165 0
SHEET 2 F 2 PHE A 171 SER A 174 -1 O PHE A 171 N ALA A 165
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
