HEADER METAL BINDING PROTEIN 02-APR-17 5VDE
TITLE CRYSTAL STRUCTURE OF CU(I)-LOADED YEAST ATX1: CRYSTAL FORM I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METAL HOMEOSTASIS FACTOR ATX1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 STRAIN: ATCC 204508 / S288C;
SOURCE 7 GENE: ATX1, YNL259C, N0840;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS ATX1, METALLOCHAPERONE, COPPER TRANSFER, METAL-BINDING DOMAIN,
KEYWDS 2 FERREDOXIN-LIKE FOLD, METAL BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.LEE,M.J.MAHER
REVDAT 3 04-OCT-23 5VDE 1 LINK
REVDAT 2 26-FEB-20 5VDE 1 REMARK
REVDAT 1 07-FEB-18 5VDE 0
JRNL AUTH M.LEE,N.D.G.COORAY,M.J.MAHER
JRNL TITL THE CRYSTAL STRUCTURES OF A COPPER-BOUND METALLOCHAPERONE
JRNL TITL 2 FROM SACCHAROMYCES CEREVISIAE.
JRNL REF J. INORG. BIOCHEM. V. 177 368 2017
JRNL REFN ISSN 1873-3344
JRNL PMID 28865724
JRNL DOI 10.1016/J.JINORGBIO.2017.08.009
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 31480
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1710
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2129
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.03
REMARK 3 BIN R VALUE (WORKING SET) : 0.2450
REMARK 3 BIN FREE R VALUE SET COUNT : 127
REMARK 3 BIN FREE R VALUE : 0.3020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2244
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 228
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.63000
REMARK 3 B22 (A**2) : 0.28000
REMARK 3 B33 (A**2) : -0.38000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.44000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.095
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.099
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.070
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.121
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2336 ; 0.020 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 2337 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3154 ; 1.980 ; 1.995
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5484 ; 1.026 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 301 ; 5.954 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 86 ;46.131 ;26.279
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 492 ;14.193 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ;28.744 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 382 ; 0.125 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2473 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 395 ; 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): 1154 ; 1.904 ; 1.618
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1153 ; 1.852 ; 1.614
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1441 ; 2.737 ; 2.406
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1442 ; 2.756 ; 2.410
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1182 ; 3.345 ; 2.112
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1182 ; 3.338 ; 2.112
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1702 ; 5.246 ; 2.971
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2607 ; 6.881 ;20.961
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2560 ; 6.798 ;20.459
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 : NULL
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: NULL
REMARK 4
REMARK 4 5VDE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1000227262.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.954
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34104
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1CC8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES (PH 7.3), 24% (W/V)
REMARK 280 PEG3350, 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 40.02700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 APPLY THE FOLLOWING TO CHAINS: A, B
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -27.23964
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -50.00558
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 ALA A 2
REMARK 465 MET B 1
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 GLU D 3
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 C 213 O HOH C 225 2.13
REMARK 500 O HOH A 258 O HOH B 211 2.19
REMARK 500 O HOH A 223 O HOH A 250 2.19
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 C 248 O HOH D 230 2847 2.09
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 101 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 15 SG
REMARK 620 2 CYS A 18 SG 120.7
REMARK 620 3 CYS B 15 SG 107.1 97.6
REMARK 620 4 CYS B 18 SG 99.0 112.0 121.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 C 101 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 15 SG
REMARK 620 2 CYS C 18 SG 119.8
REMARK 620 3 CYS D 15 SG 108.1 96.9
REMARK 620 4 CYS D 18 SG 101.6 111.5 120.2
REMARK 620 N 1 2 3
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 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CU1 C 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5VCB RELATED DB: PDB
DBREF 5VDE A 1 73 UNP P38636 ATX1_YEAST 1 73
DBREF 5VDE B 1 73 UNP P38636 ATX1_YEAST 1 73
DBREF 5VDE C 1 73 UNP P38636 ATX1_YEAST 1 73
DBREF 5VDE D 1 73 UNP P38636 ATX1_YEAST 1 73
SEQRES 1 A 73 MET ALA GLU ILE LYS HIS TYR GLN PHE ASN VAL VAL MET
SEQRES 2 A 73 THR CYS SER GLY CYS SER GLY ALA VAL ASN LYS VAL LEU
SEQRES 3 A 73 THR LYS LEU GLU PRO ASP VAL SER LYS ILE ASP ILE SER
SEQRES 4 A 73 LEU GLU LYS GLN LEU VAL ASP VAL TYR THR THR LEU PRO
SEQRES 5 A 73 TYR ASP PHE ILE LEU GLU LYS ILE LYS LYS THR GLY LYS
SEQRES 6 A 73 GLU VAL ARG SER GLY LYS GLN LEU
SEQRES 1 B 73 MET ALA GLU ILE LYS HIS TYR GLN PHE ASN VAL VAL MET
SEQRES 2 B 73 THR CYS SER GLY CYS SER GLY ALA VAL ASN LYS VAL LEU
SEQRES 3 B 73 THR LYS LEU GLU PRO ASP VAL SER LYS ILE ASP ILE SER
SEQRES 4 B 73 LEU GLU LYS GLN LEU VAL ASP VAL TYR THR THR LEU PRO
SEQRES 5 B 73 TYR ASP PHE ILE LEU GLU LYS ILE LYS LYS THR GLY LYS
SEQRES 6 B 73 GLU VAL ARG SER GLY LYS GLN LEU
SEQRES 1 C 73 MET ALA GLU ILE LYS HIS TYR GLN PHE ASN VAL VAL MET
SEQRES 2 C 73 THR CYS SER GLY CYS SER GLY ALA VAL ASN LYS VAL LEU
SEQRES 3 C 73 THR LYS LEU GLU PRO ASP VAL SER LYS ILE ASP ILE SER
SEQRES 4 C 73 LEU GLU LYS GLN LEU VAL ASP VAL TYR THR THR LEU PRO
SEQRES 5 C 73 TYR ASP PHE ILE LEU GLU LYS ILE LYS LYS THR GLY LYS
SEQRES 6 C 73 GLU VAL ARG SER GLY LYS GLN LEU
SEQRES 1 D 73 MET ALA GLU ILE LYS HIS TYR GLN PHE ASN VAL VAL MET
SEQRES 2 D 73 THR CYS SER GLY CYS SER GLY ALA VAL ASN LYS VAL LEU
SEQRES 3 D 73 THR LYS LEU GLU PRO ASP VAL SER LYS ILE ASP ILE SER
SEQRES 4 D 73 LEU GLU LYS GLN LEU VAL ASP VAL TYR THR THR LEU PRO
SEQRES 5 D 73 TYR ASP PHE ILE LEU GLU LYS ILE LYS LYS THR GLY LYS
SEQRES 6 D 73 GLU VAL ARG SER GLY LYS GLN LEU
HET CU1 A 101 1
HET CU1 C 101 1
HETNAM CU1 COPPER (I) ION
FORMUL 5 CU1 2(CU 1+)
FORMUL 7 HOH *228(H2 O)
HELIX 1 AA1 CYS A 15 LYS A 28 1 14
HELIX 2 AA2 PRO A 52 LYS A 62 1 11
HELIX 3 AA3 CYS B 15 LYS B 28 1 14
HELIX 4 AA4 PRO B 52 LYS B 62 1 11
HELIX 5 AA5 CYS C 15 LYS C 28 1 14
HELIX 6 AA6 PRO C 52 LYS C 62 1 11
HELIX 7 AA7 CYS D 15 LYS D 28 1 14
HELIX 8 AA8 PRO D 52 LYS D 62 1 11
SHEET 1 AA1 4 VAL A 33 SER A 39 0
SHEET 2 AA1 4 LEU A 44 THR A 49 -1 O ASP A 46 N ASP A 37
SHEET 3 AA1 4 LYS A 5 VAL A 11 -1 N TYR A 7 O VAL A 47
SHEET 4 AA1 4 VAL A 67 GLN A 72 -1 O LYS A 71 N GLN A 8
SHEET 1 AA2 4 VAL B 33 SER B 39 0
SHEET 2 AA2 4 LEU B 44 THR B 49 -1 O ASP B 46 N ASP B 37
SHEET 3 AA2 4 LYS B 5 VAL B 11 -1 N LYS B 5 O THR B 49
SHEET 4 AA2 4 VAL B 67 GLN B 72 -1 O LYS B 71 N GLN B 8
SHEET 1 AA3 4 VAL C 33 SER C 39 0
SHEET 2 AA3 4 LEU C 44 THR C 49 -1 O ASP C 46 N ASP C 37
SHEET 3 AA3 4 LYS C 5 VAL C 11 -1 N LYS C 5 O THR C 49
SHEET 4 AA3 4 VAL C 67 GLN C 72 -1 O LYS C 71 N GLN C 8
SHEET 1 AA4 4 VAL D 33 SER D 39 0
SHEET 2 AA4 4 LEU D 44 THR D 49 -1 O ASP D 46 N ASP D 37
SHEET 3 AA4 4 LYS D 5 VAL D 11 -1 N PHE D 9 O VAL D 45
SHEET 4 AA4 4 VAL D 67 GLN D 72 -1 O ARG D 68 N ASN D 10
LINK SG CYS A 15 CU CU1 A 101 1555 1555 2.31
LINK SG CYS A 18 CU CU1 A 101 1555 1555 2.36
LINK CU CU1 A 101 SG CYS B 15 1555 1555 2.27
LINK CU CU1 A 101 SG CYS B 18 1555 1555 2.40
LINK SG CYS C 15 CU CU1 C 101 1555 1555 2.30
LINK SG CYS C 18 CU CU1 C 101 1555 1555 2.42
LINK CU CU1 C 101 SG CYS D 15 1555 1555 2.30
LINK CU CU1 C 101 SG CYS D 18 1555 1555 2.38
CISPEP 1 GLU A 30 PRO A 31 0 3.98
CISPEP 2 GLU B 30 PRO B 31 0 15.17
CISPEP 3 GLU C 30 PRO C 31 0 8.07
CISPEP 4 GLU D 30 PRO D 31 0 4.90
SITE 1 AC1 4 CYS A 15 CYS A 18 CYS B 15 CYS B 18
SITE 1 AC2 4 CYS C 15 CYS C 18 CYS D 15 CYS D 18
CRYST1 35.976 80.054 50.763 90.00 99.91 90.00 P 1 21 1 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 0.027796 0.000000 0.004858 0.00000
SCALE2 0.000000 0.012492 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019998 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
