HEADER OXIDOREDUCTASE 02-SEP-98 1BT3
TITLE CATECHOL OXIDASE FROM IPOMOEA BATATAS (SWEET POTATOES) IN THE NATIVE
TITLE 2 CU(II)-CU(II) STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (CATECHOL OXIDASE);
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: O-DIPHENOL OXIDASE;
COMPND 5 EC: 1.10.3.1;
COMPND 6 OTHER_DETAILS: COVALENT THIOETHER BOND BETWEEN H109 AND C92
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IPOMOEA BATATAS;
SOURCE 3 ORGANISM_COMMON: SWEET POTATO;
SOURCE 4 ORGANISM_TAXID: 4120;
SOURCE 5 ORGAN: MATURE TUBER
KEYWDS CATECHOL OXIDASE, DICOPPER ENZYME, IPOMOEA BATATAS, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.KLABUNDE,C.EICKEN,J.C.SACCHETTINI,B.KREBS
REVDAT 4 27-DEC-23 1BT3 1 REMARK LINK
REVDAT 3 24-FEB-09 1BT3 1 VERSN
REVDAT 2 01-MAR-05 1BT3 1 DBREF
REVDAT 1 02-SEP-99 1BT3 0
JRNL AUTH T.KLABUNDE,C.EICKEN,J.C.SACCHETTINI,B.KREBS
JRNL TITL CRYSTAL STRUCTURE OF A PLANT CATECHOL OXIDASE CONTAINING A
JRNL TITL 2 DICOPPER CENTER.
JRNL REF NAT.STRUCT.BIOL. V. 5 1084 1998
JRNL REFN ISSN 1072-8368
JRNL PMID 9846879
JRNL DOI 10.1038/4193
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.6
REMARK 3 NUMBER OF REFLECTIONS : 12028
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) : 0.167
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
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 : 2666
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 82
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.40
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) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.810
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; 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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BT3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-99.
REMARK 100 THE DEPOSITION ID IS D_1000007312.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-AUG-97
REMARK 200 TEMPERATURE (KELVIN) : 291
REMARK 200 PH : 7.0
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 : NI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MACSCIENCE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13446
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.3
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.22600
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN AT 277 K FROM
REMARK 280 SOLUTIONS CONTAINING 14 MG/ML PROTEIN, 120 MG/ML PEG6000, 500 MM
REMARK 280 NACL, 50 MM HEPES, PH 7.0, EQUILIBRATED AGAINST A SOLUTION
REMARK 280 CONTAINING 200 MG/ML PEG6000., VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 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 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 23.06000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 78.37500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.06000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 78.37500
REMARK 290 SMTRY3 4 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 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 GLY A 289
REMARK 465 LYS A 290
REMARK 465 PRO A 291
REMARK 465 ARG A 292
REMARK 465 LYS A 293
REMARK 465 ASP A 342
REMARK 465 SER A 343
REMARK 465 LYS A 344
REMARK 465 PRO A 345
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 ILE A 8 -36.99 -38.40
REMARK 500 SER A 33 -70.96 -67.23
REMARK 500 MET A 151 49.62 -82.06
REMARK 500 PRO A 175 -67.91 -4.15
REMARK 500 ASP A 189 45.34 -102.70
REMARK 500 VAL A 208 -70.94 -125.69
REMARK 500 GLU A 256 136.76 -38.22
REMARK 500 ASP A 257 -109.28 88.09
REMARK 500 LEU A 338 77.69 -108.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 C2O A 500 CU2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 88 NE2
REMARK 620 2 C2O A 500 O1 140.2
REMARK 620 3 HIS A 109 NE2 92.1 94.0
REMARK 620 4 HIS A 118 NE2 104.1 114.4 94.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 C2O A 500 CU3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 240 NE2
REMARK 620 2 C2O A 500 O1 90.8
REMARK 620 3 HIS A 244 NE2 93.9 122.7
REMARK 620 4 HIS A 274 NE2 94.8 123.3 113.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CUA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR COPPER A
REMARK 800
REMARK 800 SITE_IDENTIFIER: CUB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR COPPER B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE C2O A 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BUG RELATED DB: PDB
REMARK 900 RELATED ID: 1BT1 RELATED DB: PDB
REMARK 900 RELATED ID: 1BT2 RELATED DB: PDB
DBREF 1BT3 A 1 345 UNP Q9ZP19 PPO1_IPOBA 1 345
SEQRES 1 A 345 ALA PRO ILE GLN ALA PRO GLU ILE SER LYS CYS VAL VAL
SEQRES 2 A 345 PRO PRO ALA ASP LEU PRO PRO GLY ALA VAL VAL ASP ASN
SEQRES 3 A 345 CYS CYS PRO PRO VAL ALA SER ASN ILE VAL ASP TYR LYS
SEQRES 4 A 345 LEU PRO ALA VAL THR THR MET LYS VAL ARG PRO ALA ALA
SEQRES 5 A 345 HIS THR MET ASP LYS ASP ALA ILE ALA LYS PHE ALA LYS
SEQRES 6 A 345 ALA VAL GLU LEU MET LYS ALA LEU PRO ALA ASP ASP PRO
SEQRES 7 A 345 ARG ASN PHE TYR GLN GLN ALA LEU VAL HIS CYS ALA TYR
SEQRES 8 A 345 CYS ASN GLY GLY TYR ASP GLN VAL ASN PHE PRO ASP GLN
SEQRES 9 A 345 GLU ILE GLN VAL HIS ASN SER TRP LEU PHE PHE PRO PHE
SEQRES 10 A 345 HIS ARG TRP TYR LEU TYR PHE TYR GLU ARG ILE LEU GLY
SEQRES 11 A 345 LYS LEU ILE GLY ASP PRO SER PHE GLY LEU PRO PHE TRP
SEQRES 12 A 345 ASN TRP ASP ASN PRO GLY GLY MET VAL LEU PRO ASP PHE
SEQRES 13 A 345 LEU ASN ASP SER THR SER SER LEU TYR ASP SER ASN ARG
SEQRES 14 A 345 ASN GLN SER HIS LEU PRO PRO VAL VAL VAL ASP LEU GLY
SEQRES 15 A 345 TYR ASN GLY ALA ASP THR ASP VAL THR ASP GLN GLN ARG
SEQRES 16 A 345 ILE THR ASP ASN LEU ALA LEU MET TYR LYS GLN MET VAL
SEQRES 17 A 345 THR ASN ALA GLY THR ALA GLU LEU PHE LEU GLY LYS ALA
SEQRES 18 A 345 TYR ARG ALA GLY ASP ALA PRO SER PRO GLY ALA GLY SER
SEQRES 19 A 345 ILE GLU THR SER PRO HIS ILE PRO ILE HIS ARG TRP VAL
SEQRES 20 A 345 GLY ASP PRO ARG ASN THR ASN ASN GLU ASP MET GLY ASN
SEQRES 21 A 345 PHE TYR SER ALA GLY ARG ASP ILE ALA PHE TYR CYS HIS
SEQRES 22 A 345 HIS SER ASN VAL ASP ARG MET TRP THR ILE TRP GLN GLN
SEQRES 23 A 345 LEU ALA GLY LYS PRO ARG LYS ARG ASP TYR THR ASP SER
SEQRES 24 A 345 ASP TRP LEU ASN ALA THR PHE LEU PHE TYR ASP GLU ASN
SEQRES 25 A 345 GLY GLN ALA VAL LYS VAL ARG ILE GLY ASP SER LEU ASP
SEQRES 26 A 345 ASN GLN LYS MET GLY TYR LYS TYR ALA LYS THR PRO LEU
SEQRES 27 A 345 PRO TRP LEU ASP SER LYS PRO
HET C2O A 500 3
HETNAM C2O CU-O-CU LINKAGE
FORMUL 2 C2O CU2 O
FORMUL 3 HOH *82(H2 O)
HELIX 1 1 ILE A 8 LYS A 10 5 3
HELIX 2 2 ALA A 52 THR A 54 5 3
HELIX 3 3 LYS A 57 LYS A 71 1 15
HELIX 4 4 PHE A 81 CYS A 92 1 12
HELIX 5 5 PHE A 114 ILE A 133 1 20
HELIX 6 6 PRO A 148 GLY A 150 5 3
HELIX 7 7 ASP A 155 ASN A 158 5 4
HELIX 8 8 GLN A 171 HIS A 173 5 3
HELIX 9 9 ASP A 192 MET A 207 1 16
HELIX 10 10 ALA A 214 LEU A 218 1 5
HELIX 11 11 SER A 234 SER A 238 1 5
HELIX 12 12 HIS A 240 VAL A 247 1 8
HELIX 13 13 ALA A 264 ARG A 266 5 3
HELIX 14 14 ILE A 268 LEU A 287 5 20
HELIX 15 15 SER A 299 LEU A 302 1 4
HELIX 16 16 ILE A 320 ASP A 322 5 3
HELIX 17 17 ASN A 326 MET A 329 1 4
SHEET 1 A 3 ILE A 35 ASP A 37 0
SHEET 2 A 3 ALA A 315 ARG A 319 1 N ALA A 315 O VAL A 36
SHEET 3 A 3 THR A 305 TYR A 309 -1 N PHE A 308 O VAL A 316
SHEET 1 B 2 LYS A 47 ARG A 49 0
SHEET 2 B 2 TYR A 331 TYR A 333 1 N LYS A 332 O LYS A 47
SSBOND 1 CYS A 11 CYS A 28 1555 1555 2.04
SSBOND 2 CYS A 27 CYS A 89 1555 1555 2.02
LINK SG CYS A 92 CE1 HIS A 109 1555 1555 1.82
LINK NE2 HIS A 88 CU2 C2O A 500 1555 1555 2.17
LINK NE2 HIS A 109 CU2 C2O A 500 1555 1555 2.33
LINK NE2 HIS A 118 CU2 C2O A 500 1555 1555 2.29
LINK NE2 HIS A 240 CU3 C2O A 500 1555 1555 2.08
LINK NE2 HIS A 244 CU3 C2O A 500 1555 1555 2.23
LINK NE2 HIS A 274 CU3 C2O A 500 1555 1555 2.23
CISPEP 1 VAL A 13 PRO A 14 0 -0.60
SITE 1 CUA 3 HIS A 88 HIS A 109 HIS A 118
SITE 1 CUB 3 HIS A 240 HIS A 244 HIS A 274
SITE 1 AC1 6 HIS A 88 HIS A 109 HIS A 118 HIS A 240
SITE 2 AC1 6 HIS A 244 HIS A 274
CRYST1 46.120 156.750 56.070 90.00 90.00 90.00 P 21 21 2 4
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 0.021683 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006380 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017835 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
