HEADER SERINE PROTEASE 16-OCT-96 1UVU
TITLE BOVINE THROMBIN--BM12.1700 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THROMBIN;
COMPND 3 CHAIN: L;
COMPND 4 SYNONYM: FACTOR II;
COMPND 5 EC: 3.4.21.5;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: THROMBIN;
COMPND 8 CHAIN: H;
COMPND 9 SYNONYM: FACTOR II;
COMPND 10 EC: 3.4.21.5
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 ORGAN: BLOOD;
SOURCE 6 TISSUE: BLOOD;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 9 ORGANISM_COMMON: CATTLE;
SOURCE 10 ORGANISM_TAXID: 9913;
SOURCE 11 ORGAN: BLOOD;
SOURCE 12 TISSUE: BLOOD
KEYWDS SERINE PROTEASE, HYDROLASE, THROMBIN, BLOOD COAGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR R.A.ENGH,R.HUBER
REVDAT 3 24-FEB-09 1UVU 1 VERSN
REVDAT 2 01-APR-03 1UVU 1 JRNL
REVDAT 1 19-NOV-97 1UVU 0
JRNL AUTH R.A.ENGH,H.BRANDSTETTER,G.SUCHER,A.EICHINGER,
JRNL AUTH 2 U.BAUMANN,W.BODE,R.HUBER,T.POLL,R.RUDOLPH,
JRNL AUTH 3 W.VON DER SAAL
JRNL TITL ENZYME FLEXIBILITY, SOLVENT AND 'WEAK'
JRNL TITL 2 INTERACTIONS CHARACTERIZE THROMBIN-LIGAND
JRNL TITL 3 INTERACTIONS: IMPLICATIONS FOR DRUG DESIGN.
JRNL REF STRUCTURE V. 4 1353 1996
JRNL REFN ISSN 0969-2126
JRNL PMID 8939759
JRNL DOI 10.1016/S0969-2126(96)00142-6
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.5
REMARK 3 NUMBER OF REFLECTIONS : 13381
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2179
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.80
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.40
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 4.400 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 7.000 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 7.200 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 9.900 ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UVU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14074
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 43.52000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 43.52000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 51.60000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 43.52000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 43.52000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 51.60000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 43.52000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.52000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 51.60000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 43.52000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.52000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 51.60000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H
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. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 THR L -20
REMARK 465 SER L -19
REMARK 465 GLU L -18
REMARK 465 ASP L -17
REMARK 465 HIS L -16
REMARK 465 PHE L -15
REMARK 465 GLN L -14
REMARK 465 PRO L -13
REMARK 465 PHE L -12
REMARK 465 PHE L -11
REMARK 465 ASN L -10
REMARK 465 GLU L -9
REMARK 465 LYS L -8
REMARK 465 THR L -7
REMARK 465 PHE L -6
REMARK 465 GLY L -5
REMARK 465 ALA L -4
REMARK 465 GLY L -3
REMARK 465 GLU L -2
REMARK 465 ALA L -1
REMARK 465 ASP L 0
REMARK 465 ILE L 15
REMARK 465 GLU L 16
REMARK 465 GLY L 17
REMARK 465 ARG L 18
REMARK 465 TRP H 147A
REMARK 465 THR H 147B
REMARK 465 THR H 147C
REMARK 465 SER H 147D
REMARK 465 VAL H 147E
REMARK 465 ALA H 147F
REMARK 465 GLU H 147G
REMARK 465 LYS H 236
REMARK 465 ILE H 238
REMARK 465 GLN H 239
REMARK 465 ASP H 243
REMARK 465 ARG H 244
REMARK 465 LEU H 245
REMARK 465 GLY H 246
REMARK 465 SER H 247
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 PHE L 7 -76.47 -129.26
REMARK 500 GLN L 11 61.96 72.50
REMARK 500 GLU H 39 116.57 -169.32
REMARK 500 SER H 48 162.93 168.03
REMARK 500 ARG H 50 11.54 -140.30
REMARK 500 TYR H 60A 81.40 -151.56
REMARK 500 ASP H 60E 75.02 16.46
REMARK 500 HIS H 71 -55.26 -130.43
REMARK 500 VAL H 79 -51.18 -120.14
REMARK 500 LYS H 87 149.48 -174.80
REMARK 500 LYS H 97 60.54 -102.75
REMARK 500 GLU H 97A -61.63 177.17
REMARK 500 ASN H 98 26.41 -156.98
REMARK 500 LEU H 130 75.33 -61.60
REMARK 500 ALA H 132 126.15 -38.43
REMARK 500 ARG H 145 176.47 179.48
REMARK 500 SER H 171 32.58 -83.01
REMARK 500 THR H 172 147.13 -178.90
REMARK 500 ARG H 175 99.22 -68.78
REMARK 500 PRO H 186 98.52 -62.30
REMARK 500 ASP H 189 145.62 173.66
REMARK 500 SER H 214 -80.85 -109.75
REMARK 500 CYS H 220 106.12 -163.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 DCH H 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCH H 1
DBREF 1UVU L -20 18 UNP P00735 THRB_BOVIN 318 366
DBREF 1UVU H 16 247 UNP P00735 THRB_BOVIN 367 625
SEQRES 1 L 49 THR SER GLU ASP HIS PHE GLN PRO PHE PHE ASN GLU LYS
SEQRES 2 L 49 THR PHE GLY ALA GLY GLU ALA ASP CYS GLY LEU ARG PRO
SEQRES 3 L 49 LEU PHE GLU LYS LYS GLN VAL GLN ASP GLN THR GLU LYS
SEQRES 4 L 49 GLU LEU PHE GLU SER TYR ILE GLU GLY ARG
SEQRES 1 H 259 ILE VAL GLU GLY GLN ASP ALA GLU VAL GLY LEU SER PRO
SEQRES 2 H 259 TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU
SEQRES 3 H 259 LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU
SEQRES 4 H 259 THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS
SEQRES 5 H 259 ASN PHE THR VAL ASP ASP LEU LEU VAL ARG ILE GLY LYS
SEQRES 6 H 259 HIS SER ARG THR ARG TYR GLU ARG LYS VAL GLU LYS ILE
SEQRES 7 H 259 SER MET LEU ASP LYS ILE TYR ILE HIS PRO ARG TYR ASN
SEQRES 8 H 259 TRP LYS GLU ASN LEU ASP ARG ASP ILE ALA LEU LEU LYS
SEQRES 9 H 259 LEU LYS ARG PRO ILE GLU LEU SER ASP TYR ILE HIS PRO
SEQRES 10 H 259 VAL CYS LEU PRO ASP LYS GLN THR ALA ALA LYS LEU LEU
SEQRES 11 H 259 HIS ALA GLY PHE LYS GLY ARG VAL THR GLY TRP GLY ASN
SEQRES 12 H 259 ARG ARG GLU THR TRP THR THR SER VAL ALA GLU VAL GLN
SEQRES 13 H 259 PRO SER VAL LEU GLN VAL VAL ASN LEU PRO LEU VAL GLU
SEQRES 14 H 259 ARG PRO VAL CYS LYS ALA SER THR ARG ILE ARG ILE THR
SEQRES 15 H 259 ASP ASN MET PHE CYS ALA GLY TYR LYS PRO GLY GLU GLY
SEQRES 16 H 259 LYS ARG GLY ASP ALA CYS GLU GLY ASP SER GLY GLY PRO
SEQRES 17 H 259 PHE VAL MET LYS SER PRO TYR ASN ASN ARG TRP TYR GLN
SEQRES 18 H 259 MET GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG ASP
SEQRES 19 H 259 GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS
SEQRES 20 H 259 LYS TRP ILE GLN LYS VAL ILE ASP ARG LEU GLY SER
HET DCH H 1 24
HETNAM DCH 3-(7-DIAMINOMETHYL-NAPHTHALEN-2-YL)-PROPIONIC ACID
HETNAM 2 DCH ETHYL ESTER
FORMUL 3 DCH C26 H31 N3 O3
HELIX 1 1 GLU L 14C TYR L 14J 1 8
HELIX 2 2 ALA H 56 CYS H 58 5 3
HELIX 3 3 PRO H 60B TRP H 60D 5 3
HELIX 4 4 VAL H 61 ASP H 63 5 3
HELIX 5 5 LYS H 126 LEU H 129C 1 7
HELIX 6 6 ARG H 165 SER H 171 1 7
HELIX 7 7 PHE H 232 ILE H 242 5 8
SHEET 1 A 4 LYS H 81 SER H 83 0
SHEET 2 A 4 LEU H 64 ILE H 68 -1 N ILE H 68 O LYS H 81
SHEET 3 A 4 GLN H 30 ARG H 35 -1 N PHE H 34 O LEU H 65
SHEET 4 A 4 GLU H 39 SER H 45 -1 N ALA H 44 O VAL H 31
SHEET 1 B 3 TRP H 51 THR H 54 0
SHEET 2 B 3 ALA H 104 LEU H 108 -1 N LEU H 106 O VAL H 52
SHEET 3 B 3 LEU H 85 ILE H 90 -1 N TYR H 89 O LEU H 105
SHEET 1 C 2 LYS H 135 GLY H 140 0
SHEET 2 C 2 GLN H 156 PRO H 161 -1 N LEU H 160 O GLY H 136
SHEET 1 D 4 MET H 180 ALA H 183 0
SHEET 2 D 4 GLY H 226 HIS H 230 -1 N TYR H 228 O PHE H 181
SHEET 3 D 4 ARG H 206 TRP H 215 -1 N TRP H 215 O PHE H 227
SHEET 4 D 4 PRO H 198 SER H 203 -1 N SER H 203 O ARG H 206
SSBOND 1 CYS L 1 CYS H 122 1555 1555 2.03
SSBOND 2 CYS H 42 CYS H 58 1555 1555 2.02
SSBOND 3 CYS H 168 CYS H 182 1555 1555 2.02
SSBOND 4 CYS H 191 CYS H 220 1555 1555 2.03
CISPEP 1 SER H 37 PRO H 37A 0 -0.21
SITE 1 AC1 11 HIS H 57 TYR H 60A ASP H 189 ALA H 190
SITE 2 AC1 11 GLU H 192 SER H 195 SER H 214 TRP H 215
SITE 3 AC1 11 GLY H 216 GLY H 219 CYS H 220
CRYST1 87.040 87.040 103.200 90.00 90.00 90.00 P 42 21 2 8
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 0.011489 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011489 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009690 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
