HEADER OXIDOREDUCTASE 03-JUN-16 5KBM
TITLE CANDIDA ALBICANS SUPEROXIDE DISMUTASE 5 (SOD5), D113N MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELL SURFACE CU-ONLY SUPEROXIDE DISMUTASE 5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 27-181;
COMPND 5 SYNONYM: PREDICTED GPI-ANCHORED PROTEIN 3;
COMPND 6 EC: 1.15.1.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDA ALBICANS (STRAIN SC5314 / ATCC MYA-
SOURCE 3 2876);
SOURCE 4 ORGANISM_COMMON: YEAST;
SOURCE 5 ORGANISM_TAXID: 237561;
SOURCE 6 STRAIN: SC5314 / ATCC MYA-2876;
SOURCE 7 GENE: SOD5, PGA3, SOD31, CAO19.2060, CAO19.9607;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PAG8H
KEYWDS ANTIOXIDANT, OXIDATIVE BURST, OXIDOREDUCTASE, ZINC LOOP,
KEYWDS 2 EXTRACELLULAR
EXPDTA X-RAY DIFFRACTION
AUTHOR A.GALALELDEEN,R.L.PETERSON,J.VILLARREAL,A.B.TAYLOR,P.J.HART
REVDAT 4 27-SEP-23 5KBM 1 JRNL REMARK
REVDAT 3 19-OCT-16 5KBM 1 JRNL
REVDAT 2 31-AUG-16 5KBM 1 JRNL
REVDAT 1 24-AUG-16 5KBM 0
JRNL AUTH R.L.PETERSON,A.GALALELDEEN,J.VILLARREAL,A.B.TAYLOR,
JRNL AUTH 2 D.E.CABELLI,P.J.HART,V.C.CULOTTA
JRNL TITL THE PHYLOGENY AND ACTIVE SITE DESIGN OF EUKARYOTIC
JRNL TITL 2 COPPER-ONLY SUPEROXIDE DISMUTASES.
JRNL REF J.BIOL.CHEM. V. 291 20911 2016
JRNL REFN ESSN 1083-351X
JRNL PMID 27535222
JRNL DOI 10.1074/JBC.M116.748251
REMARK 2
REMARK 2 RESOLUTION. 1.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2155)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.68
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.0
REMARK 3 NUMBER OF REFLECTIONS : 23994
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.330
REMARK 3 FREE R VALUE TEST SET COUNT : 1999
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 28.6844 - 3.4105 0.98 1925 176 0.1990 0.2237
REMARK 3 2 3.4105 - 2.7077 0.98 1824 165 0.2170 0.2256
REMARK 3 3 2.7077 - 2.3656 0.98 1789 163 0.2212 0.2432
REMARK 3 4 2.3656 - 2.1494 0.96 1752 159 0.2513 0.3037
REMARK 3 5 2.1494 - 1.9954 0.99 1771 161 0.2133 0.2292
REMARK 3 6 1.9954 - 1.8778 0.94 1678 152 0.2532 0.2895
REMARK 3 7 1.8778 - 1.7837 0.97 1743 158 0.2265 0.2942
REMARK 3 8 1.7837 - 1.7061 0.98 1754 160 0.2207 0.2624
REMARK 3 9 1.7061 - 1.6404 0.98 1741 158 0.2221 0.2420
REMARK 3 10 1.6404 - 1.5838 0.97 1722 157 0.1997 0.2681
REMARK 3 11 1.5838 - 1.5343 0.88 1581 143 0.1826 0.2291
REMARK 3 12 1.5343 - 1.4904 0.73 1293 118 0.1864 0.2497
REMARK 3 13 1.4904 - 1.4512 0.53 932 85 0.2063 0.2692
REMARK 3 14 1.4512 - 1.4158 0.28 490 44 0.1890 0.2233
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.74
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 1139
REMARK 3 ANGLE : 1.037 1550
REMARK 3 CHIRALITY : 0.082 172
REMARK 3 PLANARITY : 0.006 204
REMARK 3 DIHEDRAL : 11.547 413
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5KBM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1000221985.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26998
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.410
REMARK 200 RESOLUTION RANGE LOW (A) : 39.460
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.41
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.41100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 4N3T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.0, 2.4 M AMMONIUM
REMARK 280 SULFATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 17.27500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.42500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 19.72500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.42500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.27500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 19.72500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 23
REMARK 465 ALA A 24
REMARK 465 MET A 25
REMARK 465 VAL A 26
REMARK 465 TYR A 97
REMARK 465 ASN A 98
REMARK 465 GLY A 99
REMARK 465 THR A 100
REMARK 465 VAL A 101
REMARK 465 ARG A 102
REMARK 465 MET A 179
REMARK 465 SER A 180
REMARK 465 ASN A 181
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 HOH A 423 O HOH A 425 1.85
REMARK 500 O HOH A 393 O HOH A 425 1.97
REMARK 500 O HOH A 411 O HOH A 422 2.06
REMARK 500 OH TYR A 144 O HOH A 301 2.13
REMARK 500 O HOH A 305 O HOH A 397 2.14
REMARK 500 O HOH A 385 O HOH A 410 2.16
REMARK 500 O HOH A 341 O HOH A 409 2.17
REMARK 500 O HOH A 378 O HOH A 399 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 415 O HOH A 420 3754 1.96
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 GLU A 91 -136.55 63.22
REMARK 500 ASN A 95 62.41 -118.63
REMARK 500 LEU A 148 -156.66 -92.43
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 CU1 A 201 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 75 ND1
REMARK 620 2 HIS A 77 NE2 135.9
REMARK 620 3 HIS A 153 NE2 108.3 115.7
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CU1 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5KBL RELATED DB: PDB
REMARK 900 RELATED ID: 5KBK RELATED DB: PDB
DBREF 5KBM A 27 181 UNP Q5AD07 SOD5_CANAL 27 181
SEQADV 5KBM GLY A 23 UNP Q5AD07 EXPRESSION TAG
SEQADV 5KBM ALA A 24 UNP Q5AD07 EXPRESSION TAG
SEQADV 5KBM MET A 25 UNP Q5AD07 EXPRESSION TAG
SEQADV 5KBM VAL A 26 UNP Q5AD07 EXPRESSION TAG
SEQADV 5KBM ASN A 113 UNP Q5AD07 ASP 113 ENGINEERED MUTATION
SEQRES 1 A 159 GLY ALA MET VAL SER PRO SER LEU ILE ALA LYS PHE GLU
SEQRES 2 A 159 LYS THR SER LYS SER ASN ILE GLU GLY THR ILE LYS PHE
SEQRES 3 A 159 THR PRO ALA ASN ASN GLY THR VAL SER VAL SER VAL ASP
SEQRES 4 A 159 LEU LYS GLY LEU PRO SER ASP ILE GLY PRO PHE PRO TYR
SEQRES 5 A 159 HIS VAL HIS GLU LYS PRO VAL PRO ALA SER LYS ASN CYS
SEQRES 6 A 159 SER ALA THR GLU ASN HIS PHE ASN PRO TYR ASN GLY THR
SEQRES 7 A 159 VAL ARG ALA ALA THR PRO ALA ALA HIS GLU VAL GLY ASN
SEQRES 8 A 159 LEU ALA GLY LYS HIS GLY ASN ILE MET GLY GLU SER TYR
SEQRES 9 A 159 LYS THR GLU TYR ASP ASP SER TYR ILE SER LEU ASN GLU
SEQRES 10 A 159 LYS SER ARG SER TYR ILE GLY GLY LEU SER ILE VAL ILE
SEQRES 11 A 159 HIS ALA ASN ASN GLY THR ARG LEU ASN CYS ALA ASN ILE
SEQRES 12 A 159 THR LEU LEU ASP GLU GLY HIS GLY ASN ALA ASN THR THR
SEQRES 13 A 159 MET SER ASN
HET CU1 A 201 1
HET SO4 A 202 5
HET SO4 A 203 5
HETNAM CU1 COPPER (I) ION
HETNAM SO4 SULFATE ION
FORMUL 2 CU1 CU 1+
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *125(H2 O)
HELIX 1 AA1 PRO A 66 GLY A 70 5 5
HELIX 2 AA2 ASN A 86 GLU A 91 5 6
HELIX 3 AA3 THR A 105 HIS A 109 5 5
HELIX 4 AA4 ASN A 113 GLY A 119 1 7
SHEET 1 AA1 7 TYR A 74 HIS A 77 0
SHEET 2 AA1 7 SER A 149 HIS A 153 -1 O SER A 149 N HIS A 77
SHEET 3 AA1 7 ARG A 159 LEU A 167 -1 O ASN A 161 N ILE A 152
SHEET 4 AA1 7 LEU A 30 PHE A 34 -1 N ILE A 31 O THR A 166
SHEET 5 AA1 7 GLU A 43 ALA A 51 -1 O PHE A 48 N LEU A 30
SHEET 6 AA1 7 THR A 55 LYS A 63 -1 O SER A 57 N THR A 49
SHEET 7 AA1 7 TYR A 126 ASP A 132 -1 O TYR A 130 N VAL A 58
SSBOND 1 CYS A 87 CYS A 162 1555 1555 2.09
LINK ND1 HIS A 75 CU CU1 A 201 1555 1555 1.98
LINK NE2 HIS A 77 CU CU1 A 201 1555 1555 1.95
LINK NE2 HIS A 153 CU CU1 A 201 1555 1555 2.05
CISPEP 1 GLY A 70 PRO A 71 0 1.00
SITE 1 AC1 4 HIS A 75 HIS A 77 HIS A 93 HIS A 153
SITE 1 AC2 7 ASN A 41 SER A 84 ASN A 86 HOH A 316
SITE 2 AC2 7 HOH A 336 HOH A 344 HOH A 351
SITE 1 AC3 3 THR A 37 SER A 38 ASN A 156
CRYST1 34.550 39.450 102.850 90.00 90.00 90.00 P 21 21 21 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 0.028944 0.000000 0.000000 0.00000
SCALE2 0.000000 0.025349 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009723 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
