Header list of 1q56.pdb file
Complete list - r 2 2 Bytes
HEADER METAL BINDING PROTEIN 06-AUG-03 1Q56
TITLE NMR STRUCTURE OF THE B0 ISOFORM OF THE AGRIN G3 DOMAIN IN ITS CA2+
TITLE 2 BOUND STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AGRIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: 195 A.A. C-TERMINAL DOMAIN, G3 DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: B0 ISOFORM
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 GENE: AGRN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGSTHIS, A DERIVATIVE OF PGEX-1
SOURCE 11 (AMERSHAM)
KEYWDS NMJ SYNAPSE, MRNA SPLICING, ACHR AGGREGATION, LAMININ-G LIKE DOMAIN,
KEYWDS 2 CONFORMATIONAL FLEXIBILITY, MUSK ACTIVATION, CA2+ REGULATION, METAL
KEYWDS 3 BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR J.STETEFELD,A.T.ALEXANDRESCU,M.W.MACIEJEWSKI,M.JENNY,K.RATHGEB-SZABO,
AUTHOR 2 T.SCHULTHESS,R.LANDWEHR,S.FRANK,M.A.RUEGG,R.A.KAMMERER
REVDAT 3 02-MAR-22 1Q56 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1Q56 1 VERSN
REVDAT 1 13-APR-04 1Q56 0
JRNL AUTH J.STETEFELD,A.T.ALEXANDRESCU,M.W.MACIEJEWSKI,M.JENNY,
JRNL AUTH 2 K.RATHGEB-SZABO,T.SCHULTHESS,R.LANDWEHR,S.FRANK,M.A.RUEGG,
JRNL AUTH 3 R.A.KAMMERER
JRNL TITL MODULATION OF AGRIN FUNCTION BY ALTERNATIVE SPLICING AND
JRNL TITL 2 CA2+ BINDING
JRNL REF STRUCTURE V. 12 503 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15016366
JRNL DOI 10.1016/J.STR.2004.02.001
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, X-PLOR 3.851
REMARK 3 AUTHORS : GNTERT (DYANA), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGEN BOND RESTRAINTS WERE ASSIGNED
REMARK 3 BASED ON PROTECTION FROM SOLVENT EXCHANGE, AND CONSISTENCY OF
REMARK 3 HYDROGEN BONDS WITH PRELIMINARY STRUCTURES. BACKBONE PHI AND PSI
REMARK 3 DIHEDRAL RESTRAINTS WERE OBTAINED FROM 1HA, 13CA, 13CB, 13C AND
REMARK 3 15N CHEMICAL SHIFTS USING THE PROGRAM TALOS (CORNILESCU ET AL.,
REMARK 3 1993). SIDE-CHAIN CHI1 RESTRAINTS WERE FROM 3D HNHB DATA, IN
REMARK 3 CONJUNCTION WITH HN-HBETA 2/HN-HBETA 3 AND HALPHA-HBETA 2/HALPHA-
REMARK 3 HBETA 3 NOE INTENSITY RATIOS. THESE DATA WERE ALSO USED TO
REMARK 3 OBTAIN STEREOSPECIFIC ASSIGNMENTS FOR THE C-BETA PROTONS OF 37
REMARK 3 RESIDUES. NOES INVOLVING THE REMAINDER OF PROCHIRAL GROUPS WITH
REMARK 3 NON-DEGENERATE CHEMICAL SHIFTS WERE TREATED AS AMBIGUOUS WITH
REMARK 3 RESPECT TO STEREOSPECIFIC ASSIGNMENTS, AND REPRESENTED AS 1/<
REMARK 3 SUM(R^-6)>^-1/6 SUMS USING XPLOR 3.851 (BRUNGER, 1992). INITIAL
REMARK 3 STRUCTURES CALCULATED WITH THIS APPROACH, WERE USED TO IDENTIFY
REMARK 3 SITES IN WHICH ONE OF THE STEREOSPECIFIC ASSIGNMENTS WAS MORE
REMARK 3 CONSISTENT WITH THE REMAINING DISTANCE AND DIHEDRAL RESTRAINTS.
REMARK 3 THIS ENABLED STEREOSPECIFIC ASSIGNMENT OF A FURTHER 13 METHYLENE
REMARK 3 GROUPS, AND 13 VALINE AND LEUCINE PROCHIRAL METHYL GROUPS. FOR
REMARK 3 THE FINAL NMR CALCULATIONS, 400 RANDOM CONFORMATIONS WERE
REMARK 3 SUBJECTED TO RESTRAINED TORSION ANGLE DYNAMICS WITH THE PROGRAM
REMARK 3 DYANA 1.5 (GUENTERT ET AL., 1997). THE 40 STRUCTURES WITH THE
REMARK 3 SMALLEST DYANA TARGET FUNCTIONS WERE REFINED WITH A PUBLISHED
REMARK 3 SIMULATED ANNEALING PROTOCOL (NILGES ET AL., 1991), USING THE
REMARK 3 PROGRAM XPLOR 3.851 (BRUNGER, 1992). THE 15 LOWEST-ENERGY
REMARK 3 SIMULATED ANNEALING STRUCTURES WITH NO DISTANCE OR DIHEDRAL
REMARK 3 VIOLATIONS LARGER THAN 4 WERE KEPT FOR ANALYSIS.
REMARK 4
REMARK 4 1Q56 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1000019929.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 5 MM CACL2
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM PROTEIN, 5 MM CACL2, 10 MM
REMARK 210 D4-IMMIDAZOLE; 1 MM PROTEIN, 5
REMARK 210 MM CACL2, 10 MM D4-IMMIDAZOLE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY (100 MS);
REMARK 210 HNHB (CHI RESTRAINTS); HSQC-
REMARK 210 NOESY-HSQC (TM = 200 MS /
REMARK 210 PERDEUTERATED PROTEIN); HNCACB
REMARK 210 (TALOS RESTRAINTS FROM HN,CA, CB
REMARK 210 SHIFTS ), HNCO (TALOS C' SHIFTS),
REMARK 210 3D-15N SEP TOCSY (TALOS HA
REMARK 210 SHIFTS); 3D-13C SEPARATED NOESY
REMARK 210 (TM = 125 MS) AND ISOTOPE
REMARK 210 EXCHANGE EXPERIMENTS TO DERIVE H-
REMARK 210 BOND RESTRAINTS
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2000?
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS (DYANA
REMARK 210 1.5) FOLLOWED BY SIMULATED
REMARK 210 ANNEALING (X-PLOR 3.851)
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
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: SAMPLE FOR 15N HSQC-NOESY 15N HSQC WAS 2H/13C/15N LABELED.
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 H LYS A 48 O CYS A 166 1.49
REMARK 500 H VAL A 74 O PHE A 77 1.54
REMARK 500 O ALA A 183 H ASN A 186 1.56
REMARK 500 O GLY A 54 H ILE A 73 1.57
REMARK 500 H TRP A 58 O TRP A 142 1.59
REMARK 500 H HIS A 42 OD1 ASP A 173 1.60
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 LYS A 4 -172.85 66.91
REMARK 500 1 GLU A 15 71.31 -60.60
REMARK 500 1 THR A 32 110.54 -163.21
REMARK 500 1 LYS A 33 97.30 -62.91
REMARK 500 1 SER A 34 -51.65 175.25
REMARK 500 1 GLU A 35 -67.30 -101.70
REMARK 500 1 LYS A 36 77.23 63.01
REMARK 500 1 ALA A 37 44.44 172.58
REMARK 500 1 LEU A 38 173.63 -47.75
REMARK 500 1 LEU A 45 150.22 179.89
REMARK 500 1 GLU A 50 29.84 -145.39
REMARK 500 1 ALA A 51 -96.68 -162.24
REMARK 500 1 THR A 52 -35.86 176.07
REMARK 500 1 LYS A 61 90.67 61.05
REMARK 500 1 ARG A 65 27.13 -168.66
REMARK 500 1 ASP A 67 89.73 33.53
REMARK 500 1 SER A 86 -18.75 178.18
REMARK 500 1 ARG A 92 178.88 -59.16
REMARK 500 1 THR A 94 31.16 -99.82
REMARK 500 1 ASN A 100 18.76 51.67
REMARK 500 1 GLN A 111 -90.65 29.74
REMARK 500 1 GLU A 121 -158.18 -105.08
REMARK 500 1 ALA A 122 99.90 -37.34
REMARK 500 1 PRO A 129 62.36 -68.83
REMARK 500 1 LEU A 130 50.79 16.55
REMARK 500 1 ALA A 132 84.98 -161.85
REMARK 500 1 ALA A 140 170.22 -57.77
REMARK 500 1 MET A 146 130.86 -170.74
REMARK 500 1 ARG A 148 67.95 -113.14
REMARK 500 1 LEU A 149 37.78 -66.32
REMARK 500 1 HIS A 153 -85.84 83.38
REMARK 500 1 LYS A 154 -7.17 -143.91
REMARK 500 1 PRO A 156 -165.67 -68.96
REMARK 500 1 LYS A 157 -9.97 -56.25
REMARK 500 1 GLU A 176 -121.35 65.18
REMARK 500 1 LEU A 177 7.31 57.62
REMARK 500 1 HIS A 178 56.53 -110.14
REMARK 500 1 LEU A 179 -61.45 -28.24
REMARK 500 1 HIS A 191 -82.23 -110.60
REMARK 500 1 ALA A 194 37.46 75.23
REMARK 500 2 SER A 2 79.31 50.79
REMARK 500 2 LYS A 4 108.98 55.33
REMARK 500 2 ALA A 14 59.07 -118.36
REMARK 500 2 GLU A 15 70.54 -66.31
REMARK 500 2 VAL A 31 -79.61 -40.03
REMARK 500 2 SER A 34 -26.58 174.97
REMARK 500 2 GLU A 35 120.53 65.83
REMARK 500 2 ALA A 37 49.08 -179.16
REMARK 500 2 GLN A 39 -113.75 39.77
REMARK 500 2 THR A 49 162.27 52.68
REMARK 500
REMARK 500 THIS ENTRY HAS 601 RAMACHANDRAN OUTLIERS.
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 ARG A 22 0.29 SIDE CHAIN
REMARK 500 1 ARG A 65 0.29 SIDE CHAIN
REMARK 500 1 ARG A 92 0.32 SIDE CHAIN
REMARK 500 1 ARG A 109 0.29 SIDE CHAIN
REMARK 500 1 ARG A 112 0.29 SIDE CHAIN
REMARK 500 1 ARG A 148 0.27 SIDE CHAIN
REMARK 500 1 ARG A 168 0.21 SIDE CHAIN
REMARK 500 1 ARG A 174 0.32 SIDE CHAIN
REMARK 500 2 ARG A 22 0.09 SIDE CHAIN
REMARK 500 2 ARG A 65 0.21 SIDE CHAIN
REMARK 500 2 ARG A 92 0.32 SIDE CHAIN
REMARK 500 2 ARG A 109 0.23 SIDE CHAIN
REMARK 500 2 ARG A 112 0.23 SIDE CHAIN
REMARK 500 2 ARG A 148 0.16 SIDE CHAIN
REMARK 500 2 ARG A 168 0.23 SIDE CHAIN
REMARK 500 2 ARG A 174 0.09 SIDE CHAIN
REMARK 500 3 ARG A 22 0.12 SIDE CHAIN
REMARK 500 3 ARG A 65 0.23 SIDE CHAIN
REMARK 500 3 ARG A 92 0.08 SIDE CHAIN
REMARK 500 3 ARG A 109 0.25 SIDE CHAIN
REMARK 500 3 ARG A 112 0.29 SIDE CHAIN
REMARK 500 3 ARG A 148 0.17 SIDE CHAIN
REMARK 500 3 ARG A 168 0.14 SIDE CHAIN
REMARK 500 3 ARG A 174 0.12 SIDE CHAIN
REMARK 500 4 ARG A 22 0.20 SIDE CHAIN
REMARK 500 4 ARG A 65 0.20 SIDE CHAIN
REMARK 500 4 ARG A 92 0.31 SIDE CHAIN
REMARK 500 4 ARG A 109 0.16 SIDE CHAIN
REMARK 500 4 ARG A 112 0.17 SIDE CHAIN
REMARK 500 4 ARG A 148 0.15 SIDE CHAIN
REMARK 500 4 ARG A 168 0.22 SIDE CHAIN
REMARK 500 4 ARG A 174 0.15 SIDE CHAIN
REMARK 500 5 ARG A 22 0.32 SIDE CHAIN
REMARK 500 5 ARG A 65 0.23 SIDE CHAIN
REMARK 500 5 ARG A 92 0.22 SIDE CHAIN
REMARK 500 5 ARG A 109 0.12 SIDE CHAIN
REMARK 500 5 ARG A 112 0.09 SIDE CHAIN
REMARK 500 5 ARG A 148 0.21 SIDE CHAIN
REMARK 500 5 ARG A 168 0.15 SIDE CHAIN
REMARK 500 5 ARG A 174 0.17 SIDE CHAIN
REMARK 500 6 ARG A 22 0.31 SIDE CHAIN
REMARK 500 6 ARG A 65 0.31 SIDE CHAIN
REMARK 500 6 ARG A 92 0.31 SIDE CHAIN
REMARK 500 6 ARG A 109 0.27 SIDE CHAIN
REMARK 500 6 ARG A 112 0.32 SIDE CHAIN
REMARK 500 6 ARG A 148 0.31 SIDE CHAIN
REMARK 500 6 ARG A 168 0.32 SIDE CHAIN
REMARK 500 6 ARG A 174 0.30 SIDE CHAIN
REMARK 500 7 ARG A 22 0.32 SIDE CHAIN
REMARK 500 7 ARG A 65 0.23 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 116 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PZ7 RELATED DB: PDB
REMARK 900 MODULATION OF AGRIN FUNCTION BY ALTERNATIVE SPLICING AND CA2+
REMARK 900 BINDING
REMARK 900 RELATED ID: 1PZ8 RELATED DB: PDB
REMARK 900 MODULATION OF AGRIN FUNCTION BY ALTERNATIVE SPLICING AND CA2+
REMARK 900 BINDING
REMARK 900 RELATED ID: 1PZ9 RELATED DB: PDB
REMARK 900 MODULATION OF AGRIN FUNCTION BY ALTERNATIVE SPLICING AND CA2+
REMARK 900 BINDING
DBREF 1Q56 A 1 195 UNP P31696 AGRN_CHICK 624 816
SEQADV 1Q56 GLY A 1 UNP P31696 CLONING ARTIFACT
SEQADV 1Q56 SER A 2 UNP P31696 CLONING ARTIFACT
SEQRES 1 A 195 GLY SER GLU LYS VAL ILE ILE GLU LYS ALA ALA GLY ASP
SEQRES 2 A 195 ALA GLU ALA ILE ALA PHE ASP GLY ARG THR TYR MET GLU
SEQRES 3 A 195 TYR HIS ASN ALA VAL THR LYS SER GLU LYS ALA LEU GLN
SEQRES 4 A 195 SER ASN HIS PHE GLU LEU SER ILE LYS THR GLU ALA THR
SEQRES 5 A 195 GLN GLY LEU ILE LEU TRP SER GLY LYS GLY LEU GLU ARG
SEQRES 6 A 195 SER ASP TYR ILE ALA LEU ALA ILE VAL ASP GLY PHE VAL
SEQRES 7 A 195 GLN MET MET TYR ASP LEU GLY SER LYS PRO VAL VAL LEU
SEQRES 8 A 195 ARG SER THR VAL PRO ILE ASN THR ASN HIS TRP THR HIS
SEQRES 9 A 195 ILE LYS ALA TYR ARG VAL GLN ARG GLU GLY SER LEU GLN
SEQRES 10 A 195 VAL GLY ASN GLU ALA PRO ILE THR GLY SER SER PRO LEU
SEQRES 11 A 195 GLY ALA THR GLN LEU ASP THR ASP GLY ALA LEU TRP LEU
SEQRES 12 A 195 GLY GLY MET GLU ARG LEU SER VAL ALA HIS LYS LEU PRO
SEQRES 13 A 195 LYS ALA TYR SER THR GLY PHE ILE GLY CYS ILE ARG ASP
SEQRES 14 A 195 VAL ILE VAL ASP ARG GLN GLU LEU HIS LEU VAL GLU ASP
SEQRES 15 A 195 ALA LEU ASN ASN PRO THR ILE LEU HIS CYS SER ALA LYS
HELIX 1 1 ARG A 148 ALA A 152 5 5
HELIX 2 2 PRO A 156 THR A 161 1 6
HELIX 3 3 HIS A 178 LEU A 184 1 7
SHEET 1 A 6 ILE A 17 ALA A 18 0
SHEET 2 A 6 CYS A 166 VAL A 172 -1 O ILE A 167 N ILE A 17
SHEET 3 A 6 SER A 40 LYS A 48 -1 N LYS A 48 O CYS A 166
SHEET 4 A 6 THR A 103 VAL A 110 -1 O ILE A 105 N LEU A 45
SHEET 5 A 6 GLU A 113 VAL A 118 -1 O GLU A 113 N VAL A 110
SHEET 6 A 6 ILE A 124 SER A 127 -1 O GLY A 126 N GLY A 114
SHEET 1 B 3 ILE A 17 ALA A 18 0
SHEET 2 B 3 CYS A 166 VAL A 172 -1 O ILE A 167 N ILE A 17
SHEET 3 B 3 GLN A 175 GLU A 176 -1 O GLN A 175 N VAL A 172
SHEET 1 C 6 MET A 25 TYR A 27 0
SHEET 2 C 6 LEU A 141 LEU A 143 -1 O LEU A 141 N TYR A 27
SHEET 3 C 6 GLY A 54 SER A 59 -1 N TRP A 58 O TRP A 142
SHEET 4 C 6 TYR A 68 VAL A 74 -1 O ILE A 73 N GLY A 54
SHEET 5 C 6 PHE A 77 ASP A 83 -1 O PHE A 77 N VAL A 74
SHEET 6 C 6 VAL A 89 ARG A 92 -1 O LEU A 91 N MET A 80
SSBOND 1 CYS A 166 CYS A 192 1555 1555 2.02
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 2 2 Bytes