Header list of 1buq.pdb file
Complete list - v 3 2 Bytes
HEADER ISOMERASE 04-SEP-98 1BUQ
TITLE SOLUTION STRUCTURE OF DELTA-5-3-KETOSTEROID ISOMERASE COMPLEXED WITH
TITLE 2 THE STEROID 19-NORTESTOSTERONE-HEMISUCCINATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (3-KETOSTEROID ISOMERASE-19-NORTESTOSTERONE-
COMPND 3 HEMISUCCINATE);
COMPND 4 CHAIN: A, B;
COMPND 5 SYNONYM: KSI;
COMPND 6 EC: 5.3.3.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 OTHER_DETAILS: KSI COMPLEXED WITH 19-NORTESTOSTERONE-HEMISUCCINATE, A
COMPND 10 SUBSTRATE ANALOG.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: COMAMONAS TESTOSTERONI;
SOURCE 3 ORGANISM_TAXID: 285;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: BL21/DE3;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIAL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: E.COLI;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-25B;
SOURCE 10 OTHER_DETAILS: PET-25B+GENE
KEYWDS KETOSTEROID ISOMERASE-19NTHS, ENZYME-SUBSTRATE COMPLEX, ENZYMES,
KEYWDS 2 ISOMERASE
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR M.A.MASSIAH,C.ABEYGUNAWARDANA,A.G.GITTIS,A.S.MILDVAN
REVDAT 6 03-NOV-21 1BUQ 1 REMARK SEQADV
REVDAT 5 29-NOV-17 1BUQ 1 REMARK HELIX
REVDAT 4 24-FEB-09 1BUQ 1 VERSN
REVDAT 3 22-MAY-02 1BUQ 1 SOURCE REMARK SHEET
REVDAT 2 29-DEC-99 1BUQ 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 20-JAN-99 1BUQ 0
JRNL AUTH M.A.MASSIAH,C.ABEYGUNAWARDANA,A.G.GITTIS,A.S.MILDVAN
JRNL TITL SOLUTION STRUCTURE OF DELTA 5-3-KETOSTEROID ISOMERASE
JRNL TITL 2 COMPLEXED WITH THE STEROID 19-NORTESTOSTERONE HEMISUCCINATE.
JRNL REF BIOCHEMISTRY V. 37 14701 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9778345
JRNL DOI 10.1021/BI981447B
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 DURING THE REFINEMENT, THE NON-BONDED INTERACTIONS WERE MODELED
REMARK 3 ONLY BY A
REMARK 3 QUADRATIC REPULSIVE ENERGY TERM, WHILE THE ATTRACTIVE COMPONENT OF
REMARK 3 THE LENNARD-
REMARK 3 JONES POTENTIAL AND THE ELECTROSTATIC ENERGY WERE TURNED OFF. AT
REMARK 3 THE FINAL
REMARK 3 STAGES OF REFINEMENT, A SQUARE-WELL POTENTIAL ENERGY FUNCTION WAS
REMARK 3 USED FOR THE
REMARK 3 NOE AND THE DIHEDRAL ANGLE RESTRANTS WITH A FORCE OF 500 KCAL MOL-
REMARK 3 1 ANG-2 AND
REMARK 3 200 KCAL MOL-1 RAD-2, RESPECTIVELY. OF THE 120 EMBEDDED
REMARK 3 SUBSTRUCTURES, 60
REMARK 3 CONVERGED TO ACCEPTABLE STRUCTURES WITH NOE VIOLATION EQUAL OR
REMARK 3 LESS THAN
REMARK 3 0.5ANG. OF THESE, 15 BEST STRUCTURES WITH NOE VIOLATIONS EQUAL OR
REMARK 3 LESS THAN
REMARK 3 0.35 ANG AND DIHEDRAL VIOLATION < 5 DEG WERE SELECTED. MODEL 1
REMARK 3 (STRUCTURE 1)
REMARK 3 OF THE 15 STRUCTURES OF THE KSI-19NTHS COMPLEX IS THE LOWEST
REMARK 3 ENERGY STRUCTURE.
REMARK 4
REMARK 4 1BUQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008324.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 30 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 2D 1H-15N
REMARK 210 HSQC; 2D 1H-13C CT-HSQC; 3D 1H-
REMARK 210 13C-FILTERED NOESY-HSQC; 3D 1H-
REMARK 210 15N TOCSY-HSQC; 3D 1H-13C-NOESY-
REMARK 210 HSQC; 3D 1H-15N HMQC-NOESY-HSQC;
REMARK 210 3D HCCH-TOCSY; 3D 1H-13C HMQC-
REMARK 210 NOESY-HSQC; 3D HNCO; 3D HNCACB
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.8
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING AND REFINEMENT
REMARK 210 CALCULATIONS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 120
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : NOE VIOLATION =< 0.35A AND
REMARK 210 DIHEDRAL VIOLATION < 5 DEG.
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE STRUCTURE OF THE 3-KETOSTEROID ISOMERASE 19-NORTESTOSTERONE
REMARK 210 HEMISUCCINATE (
REMARK 210 19-NTHS) COMPLEX WAS DETERMINED FROM BOTH 2D NOESY, 3D NOESY AND
REMARK 210 TRIPLE
REMARK 210 RESONANCE NMR SPECTRA ON AN UNLABELED SAMPLE (2D NOESY), 15N-
REMARK 210 LABELED, 13C-,
REMARK 210 15N-UNIFORMLY LABELED, AND/OR 13C-,15N/15N-HETEROLABELED ISOMERASE
REMARK 210 WITH 1.1 MM
REMARK 210 19-NTHS. 3D NOESY AND TRIPLE RESONACE SPECTRA ON THE 15N-UNIFORMLY
REMARK 210 LABELED AND
REMARK 210 13C-,15N-UNIFORMLY SAMPLES WERE USED FOR 1H, 15N,13C ASSIGNMENTS
REMARK 210 AS WELL AS
REMARK 210 STRUCTURAL INFORMATION FOR EACH SUBUNIT. THE 1H-13C-FILTERED NOESY-
REMARK 210 HSQC OF A
REMARK 210 13C, 15N/15N-HETEROLABELED SAMPLE PROVIDED CRITICAL NOES BETWEEN
REMARK 210 THE IDENTICAL
REMARK 210 MONOMERS OF THE HOMODIMER WHICH LED TO THE SOLUTION STRUCTURE OF
REMARK 210 KSI COMPLEXED
REMARK 210 TO 19-NTHS.
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 GLN B 212 H ALA B 216 1.50
REMARK 500 HG1 THR B 235 OG SER B 311 1.51
REMARK 500 O PHE B 280 H ASP B 299 1.51
REMARK 500 O ARG B 252 H ALA B 256 1.52
REMARK 500 O ALA B 217 H ASP B 222 1.54
REMARK 500 O GLN A 12 H ALA A 16 1.55
REMARK 500 O LEU A 18 H GLY A 21 1.56
REMARK 500 H HIS A 100 O ARG A 113 1.56
REMARK 500 H HIS B 300 O ARG B 313 1.57
REMARK 500 O ARG A 52 H ALA A 56 1.58
REMARK 500 O PRO A 4 H THR A 8 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 GLN A 12 -75.13 -63.17
REMARK 500 1 ALA A 31 -178.06 -51.12
REMARK 500 1 ASP A 33 45.55 -148.37
REMARK 500 1 ALA A 34 -178.54 -51.61
REMARK 500 1 VAL A 40 87.58 -159.06
REMARK 500 1 SER A 42 55.98 72.92
REMARK 500 1 PHE A 54 -70.28 -84.10
REMARK 500 1 LEU A 67 166.53 -42.81
REMARK 500 1 THR A 68 -39.90 -149.67
REMARK 500 1 GLN A 69 -146.01 -81.77
REMARK 500 1 ALA A 75 -147.42 43.64
REMARK 500 1 GLU A 77 -163.55 -104.85
REMARK 500 1 ALA A 78 166.33 178.37
REMARK 500 1 PHE A 82 -159.23 177.05
REMARK 500 1 PHE A 88 -161.31 -116.84
REMARK 500 1 ALA A 106 35.83 176.05
REMARK 500 1 VAL A 110 -54.21 -132.60
REMARK 500 1 PHE A 116 -155.88 171.95
REMARK 500 1 ASN B 202 98.50 72.60
REMARK 500 1 GLN B 212 -75.40 -62.63
REMARK 500 1 ALA B 231 172.86 -47.00
REMARK 500 1 ASP B 233 45.55 -150.24
REMARK 500 1 ASP B 238 141.92 -179.17
REMARK 500 1 SER B 242 -155.41 -116.59
REMARK 500 1 PRO B 244 -169.94 -65.25
REMARK 500 1 PHE B 254 -71.14 -86.22
REMARK 500 1 LEU B 267 174.90 -47.15
REMARK 500 1 THR B 268 -38.92 -148.49
REMARK 500 1 GLN B 269 -147.06 -99.69
REMARK 500 1 ALA B 275 -145.89 42.35
REMARK 500 1 ALA B 278 160.80 178.15
REMARK 500 1 SER B 285 76.62 -101.25
REMARK 500 1 PHE B 288 -166.09 -100.94
REMARK 500 1 GLN B 289 43.51 -93.90
REMARK 500 1 LYS B 308 -161.47 83.05
REMARK 500 1 VAL B 310 -71.45 -108.78
REMARK 500 1 PHE B 316 -156.48 173.57
REMARK 500 1 ALA B 323 81.46 -155.26
REMARK 500 2 ASN A 2 -167.20 45.57
REMARK 500 2 GLN A 12 -73.54 -63.35
REMARK 500 2 ALA A 31 -166.70 -55.00
REMARK 500 2 ASP A 33 39.45 -144.37
REMARK 500 2 ALA A 34 177.71 -54.09
REMARK 500 2 ASP A 38 137.05 -178.92
REMARK 500 2 PRO A 39 -148.97 -71.91
REMARK 500 2 VAL A 40 -140.04 -52.80
REMARK 500 2 SER A 42 -93.70 -29.56
REMARK 500 2 GLU A 43 122.32 169.42
REMARK 500 2 PRO A 44 -167.85 -66.24
REMARK 500 2 PHE A 54 -71.50 -81.82
REMARK 500
REMARK 500 THIS ENTRY HAS 591 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 13 0.26 SIDE CHAIN
REMARK 500 1 ARG A 45 0.29 SIDE CHAIN
REMARK 500 1 ARG A 52 0.24 SIDE CHAIN
REMARK 500 1 ARG A 72 0.26 SIDE CHAIN
REMARK 500 1 ARG A 91 0.32 SIDE CHAIN
REMARK 500 1 ARG A 102 0.13 SIDE CHAIN
REMARK 500 1 ARG A 113 0.21 SIDE CHAIN
REMARK 500 1 ARG B 213 0.32 SIDE CHAIN
REMARK 500 1 ARG B 245 0.29 SIDE CHAIN
REMARK 500 1 ARG B 252 0.17 SIDE CHAIN
REMARK 500 1 ARG B 272 0.08 SIDE CHAIN
REMARK 500 1 ARG B 291 0.16 SIDE CHAIN
REMARK 500 1 ARG B 302 0.24 SIDE CHAIN
REMARK 500 1 ARG B 313 0.32 SIDE CHAIN
REMARK 500 2 ARG A 13 0.26 SIDE CHAIN
REMARK 500 2 ARG A 45 0.29 SIDE CHAIN
REMARK 500 2 ARG A 52 0.32 SIDE CHAIN
REMARK 500 2 ARG A 72 0.32 SIDE CHAIN
REMARK 500 2 ARG A 91 0.21 SIDE CHAIN
REMARK 500 2 ARG A 102 0.20 SIDE CHAIN
REMARK 500 2 ARG A 113 0.32 SIDE CHAIN
REMARK 500 2 ARG B 213 0.29 SIDE CHAIN
REMARK 500 2 ARG B 245 0.20 SIDE CHAIN
REMARK 500 2 ARG B 252 0.26 SIDE CHAIN
REMARK 500 2 ARG B 272 0.31 SIDE CHAIN
REMARK 500 2 ARG B 291 0.21 SIDE CHAIN
REMARK 500 2 ARG B 302 0.30 SIDE CHAIN
REMARK 500 2 ARG B 313 0.14 SIDE CHAIN
REMARK 500 3 ARG A 13 0.22 SIDE CHAIN
REMARK 500 3 ARG A 45 0.28 SIDE CHAIN
REMARK 500 3 ARG A 52 0.32 SIDE CHAIN
REMARK 500 3 ARG A 72 0.24 SIDE CHAIN
REMARK 500 3 ARG A 91 0.20 SIDE CHAIN
REMARK 500 3 ARG A 102 0.11 SIDE CHAIN
REMARK 500 3 ARG A 113 0.09 SIDE CHAIN
REMARK 500 3 ARG B 213 0.22 SIDE CHAIN
REMARK 500 3 ARG B 245 0.26 SIDE CHAIN
REMARK 500 3 ARG B 252 0.12 SIDE CHAIN
REMARK 500 3 ARG B 272 0.25 SIDE CHAIN
REMARK 500 3 ARG B 291 0.29 SIDE CHAIN
REMARK 500 3 ARG B 302 0.24 SIDE CHAIN
REMARK 500 3 ARG B 313 0.21 SIDE CHAIN
REMARK 500 4 ARG A 13 0.32 SIDE CHAIN
REMARK 500 4 ARG A 45 0.26 SIDE CHAIN
REMARK 500 4 ARG A 52 0.23 SIDE CHAIN
REMARK 500 4 ARG A 72 0.32 SIDE CHAIN
REMARK 500 4 ARG A 91 0.32 SIDE CHAIN
REMARK 500 4 ARG A 102 0.29 SIDE CHAIN
REMARK 500 4 ARG A 113 0.30 SIDE CHAIN
REMARK 500 4 ARG B 213 0.29 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 203 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: SBA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: SBB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NTH A 126
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NTH B 326
DBREF 1BUQ A 1 125 UNP P00947 SDIS_COMTE 1 125
DBREF 1BUQ B 201 325 UNP P00947 SDIS_COMTE 1 125
SEQADV 1BUQ PHE A 55 UNP P00947 TYR 55 ENGINEERED MUTATION
SEQADV 1BUQ PHE A 88 UNP P00947 TYR 88 ENGINEERED MUTATION
SEQADV 1BUQ PHE B 255 UNP P00947 TYR 55 ENGINEERED MUTATION
SEQADV 1BUQ PHE B 288 UNP P00947 TYR 88 ENGINEERED MUTATION
SEQRES 1 A 125 MET ASN THR PRO GLU HIS MET THR ALA VAL VAL GLN ARG
SEQRES 2 A 125 TYR VAL ALA ALA LEU ASN ALA GLY ASP LEU ASP GLY ILE
SEQRES 3 A 125 VAL ALA LEU PHE ALA ASP ASP ALA THR VAL GLU ASP PRO
SEQRES 4 A 125 VAL GLY SER GLU PRO ARG SER GLY THR ALA ALA ILE ARG
SEQRES 5 A 125 GLU PHE PHE ALA ASN SER LEU LYS LEU PRO LEU ALA VAL
SEQRES 6 A 125 GLU LEU THR GLN GLU VAL ARG ALA VAL ALA ASN GLU ALA
SEQRES 7 A 125 ALA PHE ALA PHE THR VAL SER PHE GLU PHE GLN GLY ARG
SEQRES 8 A 125 LYS THR VAL VAL ALA PRO ILE ASP HIS PHE ARG PHE ASN
SEQRES 9 A 125 GLY ALA GLY LYS VAL VAL SER MET ARG ALA LEU PHE GLY
SEQRES 10 A 125 GLU LYS ASN ILE HIS ALA GLY ALA
SEQRES 1 B 125 MET ASN THR PRO GLU HIS MET THR ALA VAL VAL GLN ARG
SEQRES 2 B 125 TYR VAL ALA ALA LEU ASN ALA GLY ASP LEU ASP GLY ILE
SEQRES 3 B 125 VAL ALA LEU PHE ALA ASP ASP ALA THR VAL GLU ASP PRO
SEQRES 4 B 125 VAL GLY SER GLU PRO ARG SER GLY THR ALA ALA ILE ARG
SEQRES 5 B 125 GLU PHE PHE ALA ASN SER LEU LYS LEU PRO LEU ALA VAL
SEQRES 6 B 125 GLU LEU THR GLN GLU VAL ARG ALA VAL ALA ASN GLU ALA
SEQRES 7 B 125 ALA PHE ALA PHE THR VAL SER PHE GLU PHE GLN GLY ARG
SEQRES 8 B 125 LYS THR VAL VAL ALA PRO ILE ASP HIS PHE ARG PHE ASN
SEQRES 9 B 125 GLY ALA GLY LYS VAL VAL SER MET ARG ALA LEU PHE GLY
SEQRES 10 B 125 GLU LYS ASN ILE HIS ALA GLY ALA
HET NTH A 126 56
HET NTH B 326 56
HETNAM NTH SUCCINIC ACID MONO-(13-METHYL-3-OXO-2,3,6,7,8,9,10,11,
HETNAM 2 NTH 12,13,14,15,16,17-TETRADECAHYDRO-1H-
HETNAM 3 NTH CYCLOPENTA[A]PHENANTHREN-17-YL) ESTER
FORMUL 3 NTH 2(C22 H30 O5)
HELIX 1 H1 GLU A 5 GLY A 21 1 17
HELIX 2 H2 LEU A 23 PHE A 30 1 8
HELIX 3 H3 THR A 48 LYS A 60 1 13
HELIX 4 H1 GLU B 205 GLY B 221 1 17
HELIX 5 H2 LEU B 223 PHE B 230 1 8
HELIX 6 H3 THR B 248 LYS B 260 1 13
SHEET 1 SA1 1 ALA A 34 ASP A 38 0
SHEET 1 SA2 1 PRO A 44 GLY A 47 0
SHEET 1 SA3 1 LEU A 63 LEU A 67 0
SHEET 1 SA4 1 VAL A 71 ALA A 73 0
SHEET 1 SA5 1 ALA A 78 GLU A 87 0
SHEET 1 SA6 1 LYS A 92 ASN A 104 0
SHEET 1 SA7 1 SER A 111 PHE A 116 0
SHEET 1 SA8 1 ILE A 121 GLY A 124 0
SHEET 1 SB1 1 ALA B 234 ASP B 238 0
SHEET 1 SB2 1 PRO B 244 GLY B 247 0
SHEET 1 SB3 1 LEU B 263 LEU B 267 0
SHEET 1 SB4 1 VAL B 271 ALA B 273 0
SHEET 1 SB5 1 ALA B 278 GLU B 287 0
SHEET 1 SB6 1 LYS B 292 ASN B 304 0
SHEET 1 SB7 1 SER B 311 PHE B 316 0
SHEET 1 SB8 1 ILE B 321 GLY B 324 0
CISPEP 1 ASP A 38 PRO A 39 1 0.29
CISPEP 2 ASP B 238 PRO B 239 1 -0.29
CISPEP 3 ASP A 38 PRO A 39 2 0.15
CISPEP 4 ASP B 238 PRO B 239 2 -0.40
CISPEP 5 ASP A 38 PRO A 39 3 -0.05
CISPEP 6 ASP B 238 PRO B 239 3 -0.30
CISPEP 7 ASP A 38 PRO A 39 4 -0.19
CISPEP 8 ASP B 238 PRO B 239 4 0.05
CISPEP 9 ASP A 38 PRO A 39 5 -0.29
CISPEP 10 ASP B 238 PRO B 239 5 -0.06
CISPEP 11 ASP A 38 PRO A 39 6 -0.11
CISPEP 12 ASP B 238 PRO B 239 6 -0.05
CISPEP 13 ASP A 38 PRO A 39 7 0.30
CISPEP 14 ASP B 238 PRO B 239 7 -0.31
CISPEP 15 ASP A 38 PRO A 39 8 0.13
CISPEP 16 ASP B 238 PRO B 239 8 0.22
CISPEP 17 ASP A 38 PRO A 39 9 -0.43
CISPEP 18 ASP B 238 PRO B 239 9 0.02
CISPEP 19 ASP A 38 PRO A 39 10 -0.24
CISPEP 20 ASP B 238 PRO B 239 10 0.05
CISPEP 21 ASP A 38 PRO A 39 11 -0.86
CISPEP 22 ASP B 238 PRO B 239 11 -0.29
CISPEP 23 ASP A 38 PRO A 39 12 -0.08
CISPEP 24 ASP B 238 PRO B 239 12 -0.18
CISPEP 25 ASP A 38 PRO A 39 13 -0.60
CISPEP 26 ASP B 238 PRO B 239 13 -0.42
CISPEP 27 ASP A 38 PRO A 39 14 -0.26
CISPEP 28 ASP B 238 PRO B 239 14 -0.54
CISPEP 29 ASP A 38 PRO A 39 15 -0.43
CISPEP 30 ASP B 238 PRO B 239 15 -0.17
SITE 1 SBA 3 TYR A 14 ASP A 38 ASP A 99
SITE 1 SBB 3 TYR B 214 ASP B 238 ASP B 299
SITE 1 AC1 8 TYR A 14 ASP A 38 SER A 58 LEU A 61
SITE 2 AC1 8 PHE A 86 PHE A 88 ASP A 99 PHE A 116
SITE 1 AC2 9 TYR B 214 ASP B 238 SER B 258 LEU B 261
SITE 2 AC2 9 PHE B 282 PHE B 286 PHE B 288 VAL B 295
SITE 3 AC2 9 ASP B 299
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 - v 3 2 Bytes