Header list of 1e1g.pdb file
Complete list - r 25 2 Bytes
HEADER PRION PROTEIN 04-MAY-00 1E1G
TITLE HUMAN PRION PROTEIN VARIANT M166V
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PRION PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GLOBULAR DOMAIN 125-228;
COMPND 5 ENGINEERED: YES;
COMPND 6 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
KEYWDS PRION PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR L.CALZOLAI,D.A.LYSEK,P.GUNTERT,C.VON SCHROETTER,R.ZAHN,
AUTHOR 2 R.RIEK,K.WUTHRICH
REVDAT 2 24-FEB-09 1E1G 1 VERSN
REVDAT 1 20-JUL-00 1E1G 0
JRNL AUTH L.CALZOLAI,D.A.LYSEK,P.GUNTERT,C.VON SCHROETTER,
JRNL AUTH 2 R.ZAHN,R.RIEK,K.WUTHRICH
JRNL TITL NMR STRUCTURES OF THREE SINGLE-RESIDUE VARIANTS OF
JRNL TITL 2 THE HUMAN PRION PROTEIN
JRNL REF PROC.NATL.ACAD.SCI.USA V. 97 8340 2000
JRNL REFN ISSN 0027-8424
JRNL PMID 10900000
JRNL DOI 10.1073/PNAS.97.15.8340
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : OPALP
REMARK 3 AUTHORS : R.KORADI,M.BILLETER,P.GUNTERT
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1E1G COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-MAY-00.
REMARK 100 THE PDBE ID CODE IS EBI-4813.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : 50 MM SODIUM ACETATE
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 750
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 12
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 400
REMARK 400 COMPOUND
REMARK 400 THE CHAIN A ENGINEERED MUTATION MET166VAL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 HG1 THR A 199 - OD2 ASP A 202 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 3 TYR A 157 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 6 ARG A 148 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 7 ARG A 164 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 9 ARG A 148 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 9 TYR A 149 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 10 ARG A 148 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 13 TYR A 169 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 18 TYR A 157 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 19 ARG A 156 NE - CZ - NH1 ANGL. DEV. = 3.2 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 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 155 0.73 -67.64
REMARK 500 1 ASP A 167 -47.18 -148.54
REMARK 500 1 GLU A 168 -80.32 -95.66
REMARK 500 1 GLN A 172 -96.22 -92.78
REMARK 500 1 TYR A 225 -57.34 -127.57
REMARK 500 2 PRO A 165 -95.83 -70.66
REMARK 500 2 ASP A 167 -57.38 -168.72
REMARK 500 2 GLN A 172 -95.40 -85.52
REMARK 500 2 PHE A 198 172.62 -47.68
REMARK 500 2 GLU A 219 13.28 -67.86
REMARK 500 2 ARG A 220 -67.41 -108.75
REMARK 500 2 TYR A 225 -48.68 -154.40
REMARK 500 3 SER A 132 151.61 -49.67
REMARK 500 3 SER A 135 92.97 -69.68
REMARK 500 3 ARG A 136 77.78 37.49
REMARK 500 3 ASP A 167 -67.82 -107.22
REMARK 500 3 GLU A 168 -84.07 -111.34
REMARK 500 3 ASN A 171 -172.35 44.91
REMARK 500 3 GLN A 172 -96.93 -122.56
REMARK 500 3 TYR A 225 -71.14 -139.05
REMARK 500 4 ALA A 133 94.95 -69.83
REMARK 500 4 ASP A 167 -39.55 -160.09
REMARK 500 4 TYR A 169 -70.57 -134.61
REMARK 500 4 SER A 170 46.72 39.48
REMARK 500 4 GLN A 172 -77.52 -100.23
REMARK 500 4 TYR A 225 -57.74 -144.50
REMARK 500 5 ASP A 167 -73.69 -128.31
REMARK 500 5 TYR A 169 -37.44 -166.79
REMARK 500 5 GLN A 172 -80.29 -65.74
REMARK 500 5 ARG A 220 -76.99 -113.99
REMARK 500 5 TYR A 225 -56.96 -154.07
REMARK 500 6 TYR A 128 158.82 53.55
REMARK 500 6 SER A 135 -139.05 34.74
REMARK 500 6 HIS A 155 -74.37 53.30
REMARK 500 6 ARG A 156 47.12 -160.00
REMARK 500 6 ASN A 159 -1.75 -141.80
REMARK 500 6 VAL A 166 32.92 -79.58
REMARK 500 6 SER A 170 70.31 35.32
REMARK 500 6 GLN A 172 -95.90 -108.93
REMARK 500 6 PHE A 198 150.76 -49.71
REMARK 500 6 TYR A 225 -66.00 -140.56
REMARK 500 7 ARG A 156 -71.45 -74.15
REMARK 500 7 VAL A 166 40.49 -65.70
REMARK 500 7 ASP A 167 -71.49 -110.12
REMARK 500 7 TYR A 169 -95.68 -151.69
REMARK 500 7 SER A 170 122.30 65.49
REMARK 500 7 GLN A 172 -102.37 -96.98
REMARK 500 7 ASN A 197 80.17 -164.78
REMARK 500 7 TYR A 225 -51.20 -141.59
REMARK 500 8 ARG A 136 105.82 -46.68
REMARK 500 8 GLU A 152 -77.21 -75.26
REMARK 500 8 HIS A 155 -72.46 53.91
REMARK 500 8 ARG A 156 -46.26 -132.05
REMARK 500 8 TYR A 157 170.59 55.97
REMARK 500 8 ASN A 171 138.15 -175.06
REMARK 500 8 GLN A 172 -62.74 -24.68
REMARK 500 8 THR A 188 0.93 -69.89
REMARK 500 8 TYR A 225 -59.37 -144.27
REMARK 500 9 ARG A 136 99.93 -30.74
REMARK 500 9 PRO A 165 5.82 -66.09
REMARK 500 9 VAL A 166 40.47 81.11
REMARK 500 9 GLU A 168 -7.60 -152.22
REMARK 500 9 SER A 170 48.00 -168.43
REMARK 500 9 ASN A 171 177.18 -59.57
REMARK 500 9 GLN A 172 -103.18 -81.27
REMARK 500 9 GLU A 219 28.88 -70.62
REMARK 500 9 TYR A 225 -71.04 -143.96
REMARK 500 10 ASP A 167 -48.41 -145.84
REMARK 500 10 SER A 170 100.08 -43.30
REMARK 500 10 ASN A 171 -163.72 -112.93
REMARK 500 10 GLN A 172 -102.24 -111.40
REMARK 500 10 ASN A 197 83.99 -153.28
REMARK 500 10 ALA A 224 30.16 -70.43
REMARK 500 10 TYR A 225 -66.26 -147.26
REMARK 500 11 SER A 135 -141.92 49.32
REMARK 500 11 HIS A 155 45.43 -78.08
REMARK 500 11 ARG A 156 -15.46 -163.86
REMARK 500 11 PRO A 165 -162.15 -65.04
REMARK 500 11 ASP A 167 -0.77 -149.18
REMARK 500 11 GLU A 168 -61.45 -137.18
REMARK 500 11 GLN A 172 -102.63 -77.20
REMARK 500 11 ALA A 224 29.53 -71.87
REMARK 500 11 TYR A 225 -63.25 -140.79
REMARK 500 12 GLU A 168 -55.20 -154.14
REMARK 500 12 SER A 170 76.56 34.69
REMARK 500 12 GLN A 172 -94.52 -96.63
REMARK 500 12 ASN A 197 82.99 -156.42
REMARK 500 12 TYR A 225 -52.15 -142.28
REMARK 500 13 ARG A 136 109.88 -57.48
REMARK 500 13 PRO A 165 -94.93 -65.85
REMARK 500 13 ASP A 167 -66.74 -147.82
REMARK 500 13 TYR A 169 -70.41 -54.46
REMARK 500 13 SER A 170 45.68 36.96
REMARK 500 13 ASN A 197 23.96 -148.80
REMARK 500 13 PHE A 198 -167.17 44.91
REMARK 500 13 TYR A 225 -70.68 -135.72
REMARK 500 14 ASP A 167 -49.19 -142.99
REMARK 500 14 TYR A 169 -43.48 -164.84
REMARK 500 14 GLN A 172 -78.08 -52.72
REMARK 500 14 ASN A 197 83.55 -150.51
REMARK 500 14 TYR A 225 -68.05 -142.09
REMARK 500 15 SER A 132 -177.63 58.63
REMARK 500 15 SER A 135 -158.80 45.57
REMARK 500 15 ASP A 167 -42.45 -156.21
REMARK 500 15 TYR A 169 25.94 -154.37
REMARK 500 15 SER A 170 70.51 -58.58
REMARK 500 15 GLN A 172 -101.39 -78.83
REMARK 500 15 ASN A 197 89.73 -155.12
REMARK 500 15 GLU A 219 13.92 -68.30
REMARK 500 15 TYR A 225 -67.08 -135.49
REMARK 500 16 TYR A 128 118.94 -24.71
REMARK 500 16 TYR A 163 -174.18 -172.43
REMARK 500 16 TYR A 169 55.12 -159.51
REMARK 500 16 ASN A 197 86.94 -150.92
REMARK 500 16 PHE A 198 117.84 -39.28
REMARK 500 16 TYR A 225 -74.47 -128.89
REMARK 500 17 ASP A 167 -45.53 -153.81
REMARK 500 17 GLU A 168 71.66 -152.90
REMARK 500 17 TYR A 169 -134.04 -161.79
REMARK 500 17 GLN A 172 -89.36 -73.96
REMARK 500 17 TYR A 225 -63.85 -133.60
REMARK 500 18 ARG A 136 101.05 -41.15
REMARK 500 18 PRO A 165 -95.57 -73.18
REMARK 500 18 VAL A 166 12.76 -153.29
REMARK 500 18 GLU A 168 -46.19 -145.76
REMARK 500 18 ASN A 171 -158.70 41.34
REMARK 500 18 GLN A 172 -68.85 -121.69
REMARK 500 18 THR A 183 -60.97 -102.89
REMARK 500 18 ASN A 197 61.05 -156.17
REMARK 500 18 GLU A 200 -25.47 -36.96
REMARK 500 18 TYR A 225 -64.15 -136.80
REMARK 500 19 ARG A 136 86.88 60.05
REMARK 500 19 ASP A 167 -41.38 -153.43
REMARK 500 19 GLU A 168 -53.53 -146.68
REMARK 500 19 SER A 170 -50.43 -120.09
REMARK 500 19 ASN A 171 -173.55 55.55
REMARK 500 19 TYR A 225 -60.91 -146.19
REMARK 500 20 GLU A 152 -82.13 -73.32
REMARK 500 20 ASN A 153 57.59 -110.88
REMARK 500 20 HIS A 155 46.65 -83.00
REMARK 500 20 ARG A 156 -26.49 -145.77
REMARK 500 20 ASP A 167 -55.55 -138.42
REMARK 500 20 SER A 170 -83.89 96.16
REMARK 500 20 ASN A 171 -168.59 53.13
REMARK 500 20 GLN A 172 -76.24 -64.06
REMARK 500 20 ASN A 197 88.93 -156.42
REMARK 500 20 TYR A 225 -61.82 -140.97
REMARK 500 20 GLN A 227 11.02 -140.28
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 167 GLU A 168 9 -137.73
REMARK 500 VAL A 166 ASP A 167 13 146.03
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 TYR A 128 0.11 SIDE CHAIN
REMARK 500 1 ARG A 148 0.10 SIDE CHAIN
REMARK 500 1 ARG A 151 0.08 SIDE CHAIN
REMARK 500 2 ARG A 156 0.08 SIDE CHAIN
REMARK 500 2 ARG A 164 0.11 SIDE CHAIN
REMARK 500 2 PHE A 198 0.09 SIDE CHAIN
REMARK 500 2 TYR A 218 0.07 SIDE CHAIN
REMARK 500 2 ARG A 220 0.10 SIDE CHAIN
REMARK 500 3 TYR A 225 0.08 SIDE CHAIN
REMARK 500 4 TYR A 149 0.07 SIDE CHAIN
REMARK 500 4 TYR A 150 0.08 SIDE CHAIN
REMARK 500 4 ARG A 151 0.08 SIDE CHAIN
REMARK 500 4 TYR A 169 0.10 SIDE CHAIN
REMARK 500 7 ARG A 208 0.18 SIDE CHAIN
REMARK 500 7 ARG A 220 0.10 SIDE CHAIN
REMARK 500 7 TYR A 225 0.09 SIDE CHAIN
REMARK 500 9 TYR A 218 0.07 SIDE CHAIN
REMARK 500 10 ARG A 148 0.09 SIDE CHAIN
REMARK 500 10 TYR A 150 0.08 SIDE CHAIN
REMARK 500 10 ARG A 220 0.10 SIDE CHAIN
REMARK 500 10 TYR A 225 0.08 SIDE CHAIN
REMARK 500 11 TYR A 128 0.08 SIDE CHAIN
REMARK 500 11 ARG A 228 0.10 SIDE CHAIN
REMARK 500 12 TYR A 128 0.08 SIDE CHAIN
REMARK 500 12 TYR A 169 0.09 SIDE CHAIN
REMARK 500 13 TYR A 150 0.07 SIDE CHAIN
REMARK 500 13 ARG A 156 0.09 SIDE CHAIN
REMARK 500 13 TYR A 163 0.12 SIDE CHAIN
REMARK 500 13 ARG A 164 0.09 SIDE CHAIN
REMARK 500 15 ARG A 164 0.10 SIDE CHAIN
REMARK 500 16 ARG A 148 0.10 SIDE CHAIN
REMARK 500 17 TYR A 225 0.07 SIDE CHAIN
REMARK 500 18 TYR A 128 0.07 SIDE CHAIN
REMARK 500 18 ARG A 136 0.08 SIDE CHAIN
REMARK 500 18 ARG A 148 0.14 SIDE CHAIN
REMARK 500 18 TYR A 162 0.12 SIDE CHAIN
REMARK 500 18 TYR A 163 0.11 SIDE CHAIN
REMARK 500 18 ARG A 164 0.08 SIDE CHAIN
REMARK 500 18 TYR A 218 0.10 SIDE CHAIN
REMARK 500 19 ARG A 151 0.12 SIDE CHAIN
REMARK 500 19 TYR A 226 0.07 SIDE CHAIN
REMARK 500 20 TYR A 128 0.08 SIDE CHAIN
REMARK 500 20 ARG A 220 0.12 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E1J RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT M166V
REMARK 900 RELATED ID: 1E1P RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT S170N
REMARK 900 RELATED ID: 1E1S RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT S170N
REMARK 900 RELATED ID: 1E1U RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT R220K
REMARK 900 RELATED ID: 1E1W RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT R220K
DBREF 1E1G A 125 228 UNP P78446 P78446 118 221
SEQADV 1E1G VAL A 166 UNP P78446 MET 166 ENGINEERED
SEQRES 1 A 104 LEU GLY GLY TYR MET LEU GLY SER ALA MET SER ARG PRO
SEQRES 2 A 104 ILE ILE HIS PHE GLY SER ASP TYR GLU ASP ARG TYR TYR
SEQRES 3 A 104 ARG GLU ASN MET HIS ARG TYR PRO ASN GLN VAL TYR TYR
SEQRES 4 A 104 ARG PRO VAL ASP GLU TYR SER ASN GLN ASN ASN PHE VAL
SEQRES 5 A 104 HIS ASP CYS VAL ASN ILE THR ILE LYS GLN HIS THR VAL
SEQRES 6 A 104 THR THR THR THR LYS GLY GLU ASN PHE THR GLU THR ASP
SEQRES 7 A 104 VAL LYS MET MET GLU ARG VAL VAL GLU GLN MET CYS ILE
SEQRES 8 A 104 THR GLN TYR GLU ARG GLU SER GLN ALA TYR TYR GLN ARG
HELIX 1 H1 ASP A 144 MET A 154 1 11
HELIX 2 H2 ASN A 173 LYS A 194 1 22
HELIX 3 H3 GLU A 200 TYR A 226 1 27
SHEET 1 S1 2 TYR A 128 GLY A 131 0
SHEET 2 S1 2 VAL A 161 ARG A 164 -1 O TYR A 163 N MET A 129
SSBOND 1 CYS A 179 CYS A 214 1555 1555 2.03
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
MODEL 1
Complete list - r 25 2 Bytes