HEADER HYDROLASE 29-JUL-10 2XMW
TITLE PACS, N-TERMINAL DOMAIN, FROM SYNECHOCYSTIS PCC6803
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATION-TRANSPORTING ATPASE PACS;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL, COPPER-BINDING DOMAIN, RESIDUES 1-71;
COMPND 5 SYNONYM: PACS-N;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. PCC 6803;
SOURCE 3 ORGANISM_TAXID: 1148;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET29A
KEYWDS HYDROLASE, CU(I)-BINDING, TRAFFICKING
EXPDTA X-RAY DIFFRACTION
AUTHOR A.BADARAU,S.J.FIRBANK,A.A.MCCARTHY,M.J.BANFIELD,C.DENNISON
REVDAT 2 18-MAY-11 2XMW 1 JRNL REMARK
REVDAT 1 18-AUG-10 2XMW 0
JRNL AUTH A.BADARAU,S.J.FIRBANK,A.A.MCCARTHY,M.J.BANFIELD,
JRNL AUTH 2 C.DENNISON
JRNL TITL VISUALIZING THE METAL-BINDING VERSATILITY OF
JRNL TITL 2 COPPER TRAFFICKING SITES .
JRNL REF BIOCHEMISTRY V. 49 7798 2010
JRNL REFN ISSN 0006-2960
JRNL PMID 20726513
JRNL DOI 10.1021/BI101064W
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0035
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.47
REMARK 3 NUMBER OF REFLECTIONS : 5475
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) : 0.24496
REMARK 3 R VALUE (WORKING SET) : 0.24332
REMARK 3 FREE R VALUE : 0.25922
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.7
REMARK 3 FREE R VALUE TEST SET COUNT : 586
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.800
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.847
REMARK 3 REFLECTION IN BIN (WORKING SET) : 386
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.08
REMARK 3 BIN R VALUE (WORKING SET) : 0.237
REMARK 3 BIN FREE R VALUE SET COUNT : 46
REMARK 3 BIN FREE R VALUE : 0.288
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 490
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 12
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.632
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.65
REMARK 3 B22 (A**2) : 0.65
REMARK 3 B33 (A**2) : -0.97
REMARK 3 B12 (A**2) : 0.32
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.172
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.146
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.069
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.233
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 493 ; 0.018 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 298 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 675 ; 1.553 ; 1.944
REMARK 3 BOND ANGLES OTHERS (DEGREES): 740 ; 0.896 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 69 ; 6.560 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 18 ;43.871 ;25.556
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 72 ;14.170 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 1 ; 1.435 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 84 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 565 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 88 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 339 ; 1.130 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 136 ; 0.250 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 538 ; 2.006 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 154 ; 2.891 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 135 ; 4.646 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY.
REMARK 4
REMARK 4 2XMW COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-JUL-10.
REMARK 100 THE PDBE ID CODE IS EBI-44870.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.37
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6085
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.80
REMARK 200 RESOLUTION RANGE LOW (A) : 39.47
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 23.5
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 39.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 23.9
REMARK 200 R MERGE FOR SHELL (I) : 0.42
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 10.30
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX.HYSS, MLPHARE, DM
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40 % (W/V) PEG 300 AND 100 MM CITRATE
REMARK 280 -PHOSPHATE PH 4.6
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 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 MET A 1
REMARK 465 GLY A 49
REMARK 465 GLU A 50
REMARK 465 THR A 51
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 27 CG CD CE NZ
REMARK 470 GLN A 32 CG CD OE1 NE2
REMARK 470 GLN A 54 CG CD OE1 NE2
REMARK 470 ILE A 55 CG1 CG2 CD1
REMARK 470 ARG A 62 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 68 NE CZ NH1 NH2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 23 CD NE CZ NH1 NH2
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 101 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 14 SG
REMARK 620 2 CYS A 14 SG 117.0
REMARK 620 3 CYS A 17 SG 141.0 101.7
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 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2GCF RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THECOPPPER(I)
REMARK 900 ATPASE PACS IN ITS APO FORM
REMARK 900 RELATED ID: 2XMT RELATED DB: PDB
REMARK 900 COPPER CHAPERONE ATX1 FROM SYNECHOCYSTIS PCC6803 (CU1 FORM)
REMARK 900 RELATED ID: 2XMV RELATED DB: PDB
REMARK 900 COPPER CHAPERONE ATX1 FROM SYNECHOCYSTIS PCC6803 (CU1,
REMARK 900 TRIMERIC FORM, HIS61TYR MUTANT)
REMARK 900 RELATED ID: 2XMM RELATED DB: PDB
REMARK 900 VISUALISING THE METAL-BINDING VERSATILITY OF COPPER
REMARK 900 TRAFFICKING SITES: H61Y ATX1 SIDE-TO-SIDE
REMARK 900 RELATED ID: 2XMK RELATED DB: PDB
REMARK 900 VISUALISING THE METAL-BINDING VERSATILITY OF COPPER
REMARK 900 TRAFFICKING SITES: ATX1 SIDE-TO-SIDE (ANAEROBIC)
REMARK 900 RELATED ID: 2XMJ RELATED DB: PDB
REMARK 900 VISUALISING THE METAL-BINDING VERSATILITY OF COPPER
REMARK 900 TRAFFICKING SITES: ATX1 SIDE-TO-SIDE (AEROBIC)
REMARK 900 RELATED ID: 2XMU RELATED DB: PDB
REMARK 900 COPPER CHAPERONE ATX1 FROM SYNECHOCYSTIS PCC6803 (CU2
REMARK 900 FORM)
DBREF 2XMW A 1 71 UNP P73241 ATCS_SYNY3 1 71
SEQRES 1 A 71 MET ALA GLN THR ILE ASN LEU GLN LEU GLU GLY MET ARG
SEQRES 2 A 71 CYS ALA ALA CYS ALA SER SER ILE GLU ARG ALA ILE ALA
SEQRES 3 A 71 LYS VAL PRO GLY VAL GLN SER CYS GLN VAL ASN PHE ALA
SEQRES 4 A 71 LEU GLU GLN ALA VAL VAL SER TYR HIS GLY GLU THR THR
SEQRES 5 A 71 PRO GLN ILE LEU THR ASP ALA VAL GLU ARG ALA GLY TYR
SEQRES 6 A 71 HIS ALA ARG VAL LEU LYS
HET CU1 A 101 1
HETNAM CU1 COPPER (I) ION
FORMUL 2 CU1 CU 1+
FORMUL 3 HOH *12(H2 O)
HELIX 1 1 CYS A 14 LYS A 27 1 14
HELIX 2 2 THR A 52 GLY A 64 1 13
SHEET 1 AA 4 VAL A 31 ASN A 37 0
SHEET 2 AA 4 GLN A 42 TYR A 47 -1 O GLN A 42 N ASN A 37
SHEET 3 AA 4 GLN A 3 GLU A 10 -1 O GLN A 3 N TYR A 47
SHEET 4 AA 4 HIS A 66 LEU A 70 -1 O HIS A 66 N GLU A 10
LINK CU CU1 A 101 SG CYS A 14 1555 1555 2.17
LINK CU CU1 A 101 SG CYS A 14 1555 3655 2.39
LINK CU CU1 A 101 SG CYS A 17 1555 1555 2.16
SITE 1 AC1 2 CYS A 14 CYS A 17
CRYST1 45.580 45.580 51.831 90.00 90.00 120.00 P 3 2 1 6
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 0.021939 0.012667 0.000000 0.00000
SCALE2 0.000000 0.025333 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019293 0.00000
(ATOM LINES ARE NOT SHOWN.)
END