Header list of 1so9.pdb file
Complete list - r 2 2 Bytes
HEADER METAL TRANSPORT 13-MAR-04 1SO9
TITLE SOLUTION STRUCTURE OF APOCOX11, 30 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C OXIDASE ASSEMBLY PROTEIN CTAG;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL SOLUBLE DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SINORHIZOBIUM MELILOTI;
SOURCE 3 ORGANISM_TAXID: 382;
SOURCE 4 GENE: CTAG, R00908, SMC00012;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS IMMUNOGLOBULIN-LIKE FOLD, COPPER PROTEIN, CYTOCHROME C OXIDASE
KEYWDS 2 ASSEMBLY, STRUCTURAL PROTEOMICS IN EUROPE, SPINE, STRUCTURAL
KEYWDS 3 GENOMICS, METAL TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR L.BANCI,I.BERTINI,F.CANTINI,S.CIOFI-BAFFONI,L.GONNELLI,S.MANGANI,
AUTHOR 2 STRUCTURAL PROTEOMICS IN EUROPE (SPINE)
REVDAT 4 02-MAR-22 1SO9 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1SO9 1 VERSN
REVDAT 2 17-AUG-04 1SO9 1 JRNL
REVDAT 1 10-AUG-04 1SO9 0
JRNL AUTH L.BANCI,I.BERTINI,F.CANTINI,S.CIOFI-BAFFONI,L.GONNELLI,
JRNL AUTH 2 S.MANGANI
JRNL TITL SOLUTION STRUCTURE OF COX11, A NOVEL TYPE OF
JRNL TITL 2 {BETA}-IMMUNOGLOBULIN-LIKE FOLD INVOLVED IN CUB SITE
JRNL TITL 3 FORMATION OF CYTOCHROME C OXIDASE.
JRNL REF J.BIOL.CHEM. V. 279 34833 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15181013
JRNL DOI 10.1074/JBC.M403655200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, AMBER 5.0
REMARK 3 AUTHORS :
REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH,
REMARK 3 WEINER,KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES WERE BASED ON A TOTAL OF
REMARK 3 2867 MEANINGFUL DISTANCE CONSTRAINTS, 130 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS.
REMARK 4
REMARK 4 1SO9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000021871.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 20 MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5 MM APOCOX11 U-15N; 5MM DTT;
REMARK 210 20 MM PHOSPHATE BUFFER NA; 1 MM
REMARK 210 APOCOX11 U-95% 13C,U-98% 15N; 5
REMARK 210 MM DTT; 20 MM PHOSPHATE BUFFER
REMARK 210 NA; 2 MM UNLABELLED APOCOX11; 5
REMARK 210 MM DTT; 20 MM PHOSPHATE BUFFER NA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; 3D_13C-
REMARK 210 SEPARATED_NOESY; 13C (H)CCH-
REMARK 210 TOCSY; CBCA(CO)NH; CBCANH; HNCO;
REMARK 210 HN(CA)CO
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3, DYANA 1.5, CYANA 1.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS COUPLED
REMARK 210 WITH SIMULATED ANNEALING
REMARK 210 FOLLOWED BY RESTRAINED ENERGY
REMARK 210 MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK:
REMARK 210 THIS STRUCTURE WAS DETERMINED USING 3D HETERONUCLEAR TECHNIQUES.
REMARK 210 THE 500 MHZ SPECTROMETER WAS EQUIPPED WITH A TRIPLE RESONANCE
REMARK 210 CRYOPROBE. ALL THE TRIPLE RESONANCE (TXI 5-MM) PROBES USED WERE
REMARK 210 EQUIPPED WITH PULSED FIELD GRADIENTS ALONG THE Z-AXIS.
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-30
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 VAL A 2
REMARK 465 PRO A 3
REMARK 465 LEU A 4
REMARK 465 TYR A 5
REMARK 465 ASP A 6
REMARK 465 MET A 7
REMARK 465 PHE A 8
REMARK 465 CYS A 9
REMARK 465 ARG A 10
REMARK 465 VAL A 11
REMARK 465 THR A 12
REMARK 465 GLY A 13
REMARK 465 TYR A 14
REMARK 465 ASN A 15
REMARK 465 GLY A 16
REMARK 465 THR A 17
REMARK 465 THR A 18
REMARK 465 GLN A 19
REMARK 465 ARG A 20
REMARK 465 PRO A 152
REMARK 465 VAL A 153
REMARK 465 ALA A 154
REMARK 465 GLN A 155
REMARK 465 VAL A 156
REMARK 465 LYS A 157
REMARK 465 ALA A 158
REMARK 465 LYS A 159
REMARK 465 ALA A 160
REMARK 465 GLU A 161
REMARK 465 ASN A 162
REMARK 465 LYS A 163
REMARK 465 LEU A 164
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 2 ARG A 54 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 14 ARG A 54 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 15 ARG A 69 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 18 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 21 ARG A 54 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 25 ARG A 59 NE - CZ - NH1 ANGL. DEV. = 3.3 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 GLU A 22 29.27 47.50
REMARK 500 1 SER A 25 38.82 -152.41
REMARK 500 1 ASP A 26 -49.06 -159.07
REMARK 500 1 ILE A 28 83.26 -69.87
REMARK 500 1 PRO A 46 42.33 -82.32
REMARK 500 1 ILE A 60 63.39 21.76
REMARK 500 1 GLU A 62 104.87 -40.81
REMARK 500 1 GLN A 81 62.62 -112.38
REMARK 500 1 MET A 89 -74.92 179.81
REMARK 500 1 ALA A 91 -101.67 -78.60
REMARK 500 1 LYS A 97 57.93 73.12
REMARK 500 1 CYS A 102 67.51 61.43
REMARK 500 1 THR A 106 -71.28 -160.04
REMARK 500 1 LYS A 128 -68.31 -127.07
REMARK 500 1 GLN A 133 53.12 29.17
REMARK 500 1 LYS A 136 62.95 -156.93
REMARK 500 1 TYR A 145 52.40 -154.43
REMARK 500 1 PRO A 146 -87.75 -75.20
REMARK 500 1 SER A 150 91.24 -175.47
REMARK 500 2 GLN A 23 168.98 156.11
REMARK 500 2 ALA A 24 15.46 -144.06
REMARK 500 2 SER A 25 22.01 -79.03
REMARK 500 2 LEU A 27 -103.82 -92.21
REMARK 500 2 ILE A 28 71.59 31.95
REMARK 500 2 ARG A 59 -103.87 -59.44
REMARK 500 2 ILE A 60 43.60 -148.76
REMARK 500 2 GLU A 62 105.58 -51.04
REMARK 500 2 ALA A 70 78.57 -156.03
REMARK 500 2 VAL A 86 55.21 -104.47
REMARK 500 2 THR A 87 147.90 -178.79
REMARK 500 2 MET A 89 -72.41 177.62
REMARK 500 2 ALA A 91 -102.54 -86.44
REMARK 500 2 GLN A 99 62.69 29.50
REMARK 500 2 CYS A 100 -37.52 -179.00
REMARK 500 2 PHE A 101 -32.85 -39.32
REMARK 500 2 PHE A 103 79.44 -62.66
REMARK 500 2 GLU A 105 -66.31 -150.05
REMARK 500 2 THR A 106 -81.70 57.84
REMARK 500 2 PRO A 110 92.24 -64.20
REMARK 500 2 LYS A 128 -67.03 -134.70
REMARK 500 2 GLN A 133 52.02 26.51
REMARK 500 2 LYS A 136 57.20 -157.21
REMARK 500 2 PHE A 144 88.11 -69.30
REMARK 500 2 TYR A 145 44.46 -149.07
REMARK 500 2 PRO A 146 -82.98 -73.97
REMARK 500 2 SER A 150 138.33 158.62
REMARK 500 3 GLU A 22 44.01 36.12
REMARK 500 3 SER A 25 35.09 -152.46
REMARK 500 3 ASP A 26 -56.41 -159.33
REMARK 500 3 ASP A 30 30.51 -80.73
REMARK 500
REMARK 500 THIS ENTRY HAS 638 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 GLU A 22 GLN A 23 1 148.24
REMARK 500 ALA A 82 THR A 83 5 141.08
REMARK 500 GLN A 23 ALA A 24 7 138.07
REMARK 500 ALA A 24 SER A 25 7 144.81
REMARK 500 ARG A 59 ILE A 60 7 -147.12
REMARK 500 THR A 139 LEU A 140 7 146.48
REMARK 500 GLN A 23 ALA A 24 10 -143.13
REMARK 500 PHE A 84 ASN A 85 10 149.36
REMARK 500 GLN A 23 ALA A 24 11 147.82
REMARK 500 GLN A 23 ALA A 24 12 -107.58
REMARK 500 VAL A 21 GLU A 22 14 -149.44
REMARK 500 GLN A 23 ALA A 24 15 136.78
REMARK 500 SER A 25 ASP A 26 15 131.15
REMARK 500 ALA A 82 THR A 83 15 146.57
REMARK 500 LYS A 136 THR A 137 15 141.40
REMARK 500 GLN A 23 ALA A 24 16 -92.72
REMARK 500 LEU A 29 ASP A 30 16 145.65
REMARK 500 ILE A 56 ASP A 57 16 149.00
REMARK 500 GLY A 111 GLU A 112 17 -146.61
REMARK 500 GLN A 23 ALA A 24 20 149.30
REMARK 500 ALA A 82 THR A 83 20 144.26
REMARK 500 GLN A 23 ALA A 24 21 126.92
REMARK 500 ALA A 24 SER A 25 22 -147.20
REMARK 500 GLU A 62 THR A 63 22 -146.11
REMARK 500 ILE A 56 ASP A 57 23 149.88
REMARK 500 ARG A 59 ILE A 60 23 -148.24
REMARK 500 VAL A 21 GLU A 22 24 -146.31
REMARK 500 ILE A 56 ASP A 57 24 146.91
REMARK 500 GLY A 111 GLU A 112 24 -139.61
REMARK 500 GLN A 23 ALA A 24 26 -135.26
REMARK 500 ALA A 24 SER A 25 26 149.37
REMARK 500 ALA A 24 SER A 25 28 -147.20
REMARK 500 GLU A 62 THR A 63 28 -146.11
REMARK 500 ILE A 56 ASP A 57 29 149.88
REMARK 500 ARG A 59 ILE A 60 29 -148.24
REMARK 500 VAL A 21 GLU A 22 30 -146.31
REMARK 500 ILE A 56 ASP A 57 30 146.91
REMARK 500 GLY A 111 GLU A 112 30 -139.61
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 59 0.20 SIDE CHAIN
REMARK 500 1 TYR A 94 0.11 SIDE CHAIN
REMARK 500 2 PHE A 37 0.08 SIDE CHAIN
REMARK 500 2 ARG A 59 0.08 SIDE CHAIN
REMARK 500 2 TYR A 94 0.10 SIDE CHAIN
REMARK 500 3 ARG A 59 0.10 SIDE CHAIN
REMARK 500 3 ARG A 69 0.10 SIDE CHAIN
REMARK 500 3 PHE A 84 0.12 SIDE CHAIN
REMARK 500 3 TYR A 94 0.08 SIDE CHAIN
REMARK 500 3 PHE A 144 0.10 SIDE CHAIN
REMARK 500 5 ARG A 54 0.10 SIDE CHAIN
REMARK 500 5 PHE A 84 0.11 SIDE CHAIN
REMARK 500 5 TYR A 94 0.16 SIDE CHAIN
REMARK 500 5 TYR A 142 0.10 SIDE CHAIN
REMARK 500 5 PHE A 144 0.09 SIDE CHAIN
REMARK 500 6 ARG A 54 0.12 SIDE CHAIN
REMARK 500 6 ARG A 59 0.15 SIDE CHAIN
REMARK 500 6 TYR A 94 0.12 SIDE CHAIN
REMARK 500 6 PHE A 103 0.12 SIDE CHAIN
REMARK 500 6 TYR A 142 0.14 SIDE CHAIN
REMARK 500 7 PHE A 49 0.08 SIDE CHAIN
REMARK 500 7 PHE A 120 0.13 SIDE CHAIN
REMARK 500 8 TYR A 142 0.07 SIDE CHAIN
REMARK 500 9 TYR A 68 0.07 SIDE CHAIN
REMARK 500 9 TYR A 94 0.10 SIDE CHAIN
REMARK 500 10 PHE A 120 0.12 SIDE CHAIN
REMARK 500 11 ARG A 59 0.08 SIDE CHAIN
REMARK 500 11 TYR A 94 0.07 SIDE CHAIN
REMARK 500 11 PHE A 103 0.10 SIDE CHAIN
REMARK 500 11 TYR A 142 0.11 SIDE CHAIN
REMARK 500 11 PHE A 144 0.10 SIDE CHAIN
REMARK 500 12 PHE A 49 0.09 SIDE CHAIN
REMARK 500 12 ARG A 59 0.09 SIDE CHAIN
REMARK 500 12 TYR A 68 0.11 SIDE CHAIN
REMARK 500 12 PHE A 84 0.10 SIDE CHAIN
REMARK 500 12 TYR A 94 0.12 SIDE CHAIN
REMARK 500 12 PHE A 120 0.09 SIDE CHAIN
REMARK 500 12 TYR A 142 0.09 SIDE CHAIN
REMARK 500 13 PHE A 120 0.14 SIDE CHAIN
REMARK 500 14 ARG A 59 0.11 SIDE CHAIN
REMARK 500 14 PHE A 120 0.10 SIDE CHAIN
REMARK 500 14 TYR A 142 0.14 SIDE CHAIN
REMARK 500 15 TYR A 68 0.07 SIDE CHAIN
REMARK 500 15 PHE A 120 0.09 SIDE CHAIN
REMARK 500 16 TYR A 94 0.07 SIDE CHAIN
REMARK 500 16 PHE A 95 0.08 SIDE CHAIN
REMARK 500 17 ARG A 59 0.14 SIDE CHAIN
REMARK 500 17 TYR A 94 0.12 SIDE CHAIN
REMARK 500 17 TYR A 142 0.10 SIDE CHAIN
REMARK 500 18 ARG A 59 0.11 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 100 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SP0 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF APOCOX11, MINIMIZED AVERAGE STRUCTURE
REMARK 900 RELATED ID: CIRMMP18 RELATED DB: TARGETDB
DBREF 1SO9 A 2 164 UNP Q92RG6 COXZ_RHIME 36 198
SEQADV 1SO9 MET A 1 UNP Q92RG6 INITIATING METHIONINE
SEQRES 1 A 164 MET VAL PRO LEU TYR ASP MET PHE CYS ARG VAL THR GLY
SEQRES 2 A 164 TYR ASN GLY THR THR GLN ARG VAL GLU GLN ALA SER ASP
SEQRES 3 A 164 LEU ILE LEU ASP GLU LYS ILE LYS VAL THR PHE ASP ALA
SEQRES 4 A 164 ASN VAL ALA ALA GLY LEU PRO TRP GLU PHE VAL PRO VAL
SEQRES 5 A 164 GLN ARG ASP ILE ASP VAL ARG ILE GLY GLU THR VAL GLN
SEQRES 6 A 164 ILE MET TYR ARG ALA LYS ASN LEU ALA SER THR PRO THR
SEQRES 7 A 164 THR GLY GLN ALA THR PHE ASN VAL THR PRO MET ALA ALA
SEQRES 8 A 164 GLY ALA TYR PHE ASN LYS VAL GLN CYS PHE CYS PHE THR
SEQRES 9 A 164 GLU THR THR LEU GLU PRO GLY GLU GLU MET GLU MET PRO
SEQRES 10 A 164 VAL VAL PHE PHE VAL ASP PRO GLU ILE VAL LYS PRO VAL
SEQRES 11 A 164 GLU THR GLN GLY ILE LYS THR LEU THR LEU SER TYR THR
SEQRES 12 A 164 PHE TYR PRO ARG GLU PRO SER LYS PRO VAL ALA GLN VAL
SEQRES 13 A 164 LYS ALA LYS ALA GLU ASN LYS LEU
HELIX 1 1 ASP A 123 LYS A 128 5 6
SHEET 1 A 4 ASP A 55 VAL A 58 0
SHEET 2 A 4 ILE A 33 VAL A 41 -1 N ILE A 33 O VAL A 58
SHEET 3 A 4 LEU A 140 PHE A 144 1 O PHE A 144 N ASN A 40
SHEET 4 A 4 THR A 83 VAL A 86 -1 N THR A 83 O THR A 143
SHEET 1 B 3 TRP A 47 VAL A 50 0
SHEET 2 B 3 ILE A 66 ASN A 72 -1 O LYS A 71 N GLU A 48
SHEET 3 B 3 GLU A 113 VAL A 118 -1 O MET A 114 N ALA A 70
SHEET 1 C 2 THR A 78 THR A 79 0
SHEET 2 C 2 THR A 107 LEU A 108 -1 O LEU A 108 N THR A 78
CISPEP 1 ALA A 24 SER A 25 11 13.60
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