HEADER HYDROLASE 14-DEC-15 5FBE
TITLE COMPLEMENT FACTOR D IN COMPLEX WITH COMPOUND2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COMPLEMENT FACTOR D;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 26-253;
COMPND 5 SYNONYM: ADIPSIN,C3 CONVERTASE ACTIVATOR,PROPERDIN FACTOR D;
COMPND 6 EC: 3.4.21.46;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CFD, DF, PFD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.OSTERMANN,F.ZINK
REVDAT 4 10-JAN-24 5FBE 1 REMARK
REVDAT 3 23-NOV-16 5FBE 1 JRNL
REVDAT 2 02-NOV-16 5FBE 1 JRNL
REVDAT 1 26-OCT-16 5FBE 0
JRNL AUTH J.MAIBAUM,S.M.LIAO,A.VULPETTI,N.OSTERMANN,S.RANDL,
JRNL AUTH 2 S.RUDISSER,E.LORTHIOIS,P.ERBEL,B.KINZEL,F.A.KOLB,S.BARBIERI,
JRNL AUTH 3 J.WAGNER,C.DURAND,K.FETTIS,S.DUSSAUGE,N.HUGHES,O.DELGADO,
JRNL AUTH 4 U.HOMMEL,T.GOULD,A.MAC SWEENEY,B.GERHARTZ,F.CUMIN,S.FLOHR,
JRNL AUTH 5 A.SCHUBART,B.JAFFEE,R.HARRISON,A.M.RISITANO,J.EDER,
JRNL AUTH 6 K.ANDERSON
JRNL TITL SMALL-MOLECULE FACTOR D INHIBITORS TARGETING THE ALTERNATIVE
JRNL TITL 2 COMPLEMENT PATHWAY.
JRNL REF NAT.CHEM.BIOL. V. 12 1105 2016
JRNL REFN ESSN 1552-4469
JRNL PMID 27775713
JRNL DOI 10.1038/NCHEMBIO.2208
REMARK 2
REMARK 2 RESOLUTION. 1.43 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.5
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.43
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 16.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 38094
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1904
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 : 19
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.43
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.47
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.35
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2972
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1978
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2824
REMARK 3 BIN R VALUE (WORKING SET) : 0.1956
REMARK 3 BIN FREE R VALUE : 0.2354
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.98
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 148
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 : 1711
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 204
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.18
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.43950
REMARK 3 B22 (A**2) : 0.11330
REMARK 3 B33 (A**2) : 0.32620
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.34680
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.143
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.064
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.063
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.063
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.062
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 1871 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2563 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 647 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 40 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 288 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 1871 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 230 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 2366 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.11
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.95
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 14.46
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5FBE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216335.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-NOV-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9999
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38106
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.430
REMARK 200 RESOLUTION RANGE LOW (A) : 16.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.43
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.47
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.39000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1BIO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 MICROLITER PROTEIN SOLUTION WAS
REMARK 280 MIXED WITH 1 MICROLITER RESERVOIR SOLUTION. PROTEIN SOLUTION: 18
REMARK 280 MG/ML FD, 10 MM TRIS PH 7.0, 100 MM NACL; RESERVOIR SOLUTION: 22%
REMARK 280 PEG3350, 100 MM HEPES PH 7.5; SOAKING AND CRYO: ADDITION OF 10
REMARK 280 MM COMPOUND2 FOR 45 MIN FOLLOWED BY THE ADDITION OF 0.5
REMARK 280 MICROLITER GLYCEROL AND FLASH FREEZING IN LIQUIT NITROGEN.,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-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 25.00000
REMARK 290 SMTRY3 2 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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. (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 SER A 244
REMARK 465 ALA A 245
REMARK 465 ALA A 246
REMARK 465 ALA A 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 ASP A 61 17.97 54.73
REMARK 500 ALA A 61B 109.18 -45.13
REMARK 500 ASP A 61C -32.02 104.84
REMARK 500 HIS A 71 -60.15 -122.22
REMARK 500 HIS A 171 -110.50 -103.91
REMARK 500 ARG A 187 -12.51 69.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5W5 A 302
DBREF 5FBE A 16 243 UNP P00746 CFAD_HUMAN 26 253
SEQADV 5FBE SER A 244 UNP P00746 EXPRESSION TAG
SEQADV 5FBE ALA A 245 UNP P00746 EXPRESSION TAG
SEQADV 5FBE ALA A 246 UNP P00746 EXPRESSION TAG
SEQADV 5FBE ALA A 247 UNP P00746 EXPRESSION TAG
SEQRES 1 A 232 ILE LEU GLY GLY ARG GLU ALA GLU ALA HIS ALA ARG PRO
SEQRES 2 A 232 TYR MET ALA SER VAL GLN LEU ASN GLY ALA HIS LEU CYS
SEQRES 3 A 232 GLY GLY VAL LEU VAL ALA GLU GLN TRP VAL LEU SER ALA
SEQRES 4 A 232 ALA HIS CYS LEU GLU ASP ALA ALA ASP GLY LYS VAL GLN
SEQRES 5 A 232 VAL LEU LEU GLY ALA HIS SER LEU SER GLN PRO GLU PRO
SEQRES 6 A 232 SER LYS ARG LEU TYR ASP VAL LEU ARG ALA VAL PRO HIS
SEQRES 7 A 232 PRO ASP SER GLN PRO ASP THR ILE ASP HIS ASP LEU LEU
SEQRES 8 A 232 LEU LEU GLN LEU SER GLU LYS ALA THR LEU GLY PRO ALA
SEQRES 9 A 232 VAL ARG PRO LEU PRO TRP GLN ARG VAL ASP ARG ASP VAL
SEQRES 10 A 232 ALA PRO GLY THR LEU CYS ASP VAL ALA GLY TRP GLY ILE
SEQRES 11 A 232 VAL ASN HIS ALA GLY ARG ARG PRO ASP SER LEU GLN HIS
SEQRES 12 A 232 VAL LEU LEU PRO VAL LEU ASP ARG ALA THR CYS ASN ARG
SEQRES 13 A 232 ARG THR HIS HIS ASP GLY ALA ILE THR GLU ARG LEU MET
SEQRES 14 A 232 CYS ALA GLU SER ASN ARG ARG ASP SER CYS LYS GLY ASP
SEQRES 15 A 232 SER GLY GLY PRO LEU VAL CYS GLY GLY VAL LEU GLU GLY
SEQRES 16 A 232 VAL VAL THR SER GLY SER ARG VAL CYS GLY ASN ARG LYS
SEQRES 17 A 232 LYS PRO GLY ILE TYR THR ARG VAL ALA SER TYR ALA ALA
SEQRES 18 A 232 TRP ILE ASP SER VAL LEU ALA SER ALA ALA ALA
HET GOL A 301 6
HET 5W5 A 302 33
HETNAM GOL GLYCEROL
HETNAM 5W5 METHYL 2-[[[(2~{S})-2-[[3-(TRIFLUOROMETHYLOXY)
HETNAM 2 5W5 PHENYL]CARBAMOYL]PYRROLIDIN-1-
HETNAM 3 5W5 YL]CARBONYLAMINO]METHYL]BENZOATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL C3 H8 O3
FORMUL 3 5W5 C22 H22 F3 N3 O5
FORMUL 4 HOH *204(H2 O)
HELIX 1 AA1 ALA A 55 GLU A 60 5 6
HELIX 2 AA2 ASP A 164 ASN A 169 1 6
HELIX 3 AA3 TYR A 234 ALA A 243 1 10
SHEET 1 AA1 8 ARG A 20 GLU A 21 0
SHEET 2 AA1 8 GLN A 156 LEU A 163 -1 O HIS A 157 N ARG A 20
SHEET 3 AA1 8 LEU A 180 ALA A 183 -1 O CYS A 182 N LEU A 163
SHEET 4 AA1 8 GLY A 226 ARG A 230 -1 O TYR A 228 N MET A 181
SHEET 5 AA1 8 VAL A 208 VAL A 213 -1 N VAL A 212 O THR A 229
SHEET 6 AA1 8 PRO A 198 CYS A 201 -1 N LEU A 199 O GLU A 210
SHEET 7 AA1 8 LEU A 135 GLY A 140 -1 N ASP A 137 O VAL A 200
SHEET 8 AA1 8 GLN A 156 LEU A 163 -1 O LEU A 160 N CYS A 136
SHEET 1 AA2 7 MET A 30 LEU A 35 0
SHEET 2 AA2 7 ALA A 39 ALA A 48 -1 O CYS A 42 N VAL A 33
SHEET 3 AA2 7 TRP A 51 SER A 54 -1 O LEU A 53 N VAL A 45
SHEET 4 AA2 7 LEU A 104 LEU A 108 -1 O LEU A 106 N VAL A 52
SHEET 5 AA2 7 ARG A 81 PRO A 90 -1 N VAL A 89 O LEU A 105
SHEET 6 AA2 7 VAL A 64 LEU A 68 -1 N VAL A 66 O TYR A 83
SHEET 7 AA2 7 MET A 30 LEU A 35 -1 N GLN A 34 O GLN A 65
SSBOND 1 CYS A 42 CYS A 58 1555 1555 2.02
SSBOND 2 CYS A 136 CYS A 201 1555 1555 2.05
SSBOND 3 CYS A 168 CYS A 182 1555 1555 2.03
SSBOND 4 CYS A 191 CYS A 220 1555 1555 2.03
SITE 1 AC1 9 ASP A 129A VAL A 130 VAL A 162 LEU A 163
SITE 2 AC1 9 ASP A 164 ARG A 165 MET A 181 CYS A 182
SITE 3 AC1 9 HOH A 465
SITE 1 AC2 19 HIS A 40 LEU A 41 CYS A 42 HIS A 57
SITE 2 AC2 19 CYS A 58 TRP A 141 GLY A 142 ILE A 143
SITE 3 AC2 19 ARG A 151 SER A 190 CYS A 191 LYS A 192
SITE 4 AC2 19 GLY A 193 SER A 195 VAL A 213 SER A 215
SITE 5 AC2 19 ARG A 218 CYS A 220 HOH A 452
CRYST1 55.400 50.000 39.358 90.00 105.75 90.00 P 1 21 1 2
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 0.018051 0.000000 0.005091 0.00000
SCALE2 0.000000 0.020000 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026399 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
