HEADER OXIDOREDUCTASE 07-APR-09 3GZO
TITLE HUMAN SOD1 G93A VARIANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J;
COMPND 4 EC: 1.15.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SOD1;
SOURCE 6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: EGY118;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: YEP351-HSOD
KEYWDS OXIDOREDUCTASE, HUMAN CU, ZN SUPEROXIDE DISMUTASE, ANTIOXIDANT,
KEYWDS 2 METAL-BINDING, AMYOTROPHIC LATERAL SCLEROSIS, DISEASE MUTATION,
KEYWDS 3 DISULFIDE BOND, PHOSPHOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.GALALELDEEN,A.B.TAYLOR,N.NARAYANA,L.J.WHITSON,P.J.HART
REVDAT 3 13-JUL-11 3GZO 1 VERSN
REVDAT 2 22-DEC-09 3GZO 1 JRNL
REVDAT 1 13-OCT-09 3GZO 0
JRNL AUTH A.GALALELDEEN,R.W.STRANGE,L.J.WHITSON,S.V.ANTONYUK,
JRNL AUTH 2 N.NARAYANA,A.B.TAYLOR,J.P.SCHUERMANN,S.P.HOLLOWAY,
JRNL AUTH 3 S.S.HASNAIN,P.J.HART
JRNL TITL STRUCTURAL AND BIOPHYSICAL PROPERTIES OF METAL-FREE
JRNL TITL 2 PATHOGENIC SOD1 MUTANTS A4V AND G93A.
JRNL REF ARCH.BIOCHEM.BIOPHYS. V. 492 40 2009
JRNL REFN ISSN 0003-9861
JRNL PMID 19800308
JRNL DOI 10.1016/J.ABB.2009.09.020
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.4_4)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.020
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 135446
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 6759
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 41.5006 - 6.5185 0.98 4625 226 0.1668 0.1977
REMARK 3 2 6.5185 - 5.1771 0.99 4508 217 0.1446 0.1750
REMARK 3 3 5.1771 - 4.5236 0.99 4458 228 0.1200 0.1398
REMARK 3 4 4.5236 - 4.1104 0.99 4469 231 0.1147 0.1438
REMARK 3 5 4.1104 - 3.8160 0.99 4430 217 0.1222 0.1629
REMARK 3 6 3.8160 - 3.5912 0.99 4455 231 0.1300 0.1611
REMARK 3 7 3.5912 - 3.4114 0.99 4398 242 0.1382 0.1823
REMARK 3 8 3.4114 - 3.2630 0.99 4414 237 0.1401 0.1809
REMARK 3 9 3.2630 - 3.1374 0.99 4374 220 0.1507 0.1915
REMARK 3 10 3.1374 - 3.0292 0.98 4368 241 0.1604 0.2195
REMARK 3 11 3.0292 - 2.9345 0.98 4332 243 0.1711 0.2141
REMARK 3 12 2.9345 - 2.8506 0.98 4350 223 0.1812 0.2071
REMARK 3 13 2.8506 - 2.7756 0.97 4323 219 0.1773 0.2168
REMARK 3 14 2.7756 - 2.7079 0.97 4338 217 0.1816 0.2439
REMARK 3 15 2.7079 - 2.6463 0.96 4238 217 0.1965 0.2568
REMARK 3 16 2.6463 - 2.5900 0.96 4238 243 0.2002 0.2567
REMARK 3 17 2.5900 - 2.5382 0.96 4208 257 0.2030 0.2475
REMARK 3 18 2.5382 - 2.4903 0.96 4276 214 0.2076 0.2625
REMARK 3 19 2.4903 - 2.4459 0.96 4242 229 0.2090 0.2766
REMARK 3 20 2.4459 - 2.4044 0.95 4203 248 0.2139 0.2534
REMARK 3 21 2.4044 - 2.3656 0.95 4189 221 0.2144 0.2750
REMARK 3 22 2.3656 - 2.3292 0.95 4220 213 0.2202 0.2828
REMARK 3 23 2.3292 - 2.2950 0.94 4183 221 0.2116 0.2476
REMARK 3 24 2.2950 - 2.2627 0.94 4156 187 0.2208 0.2761
REMARK 3 25 2.2627 - 2.2321 0.94 4163 237 0.2283 0.2788
REMARK 3 26 2.2321 - 2.2031 0.94 4159 232 0.2402 0.2759
REMARK 3 27 2.2031 - 2.1756 0.94 4143 223 0.2362 0.2723
REMARK 3 28 2.1756 - 2.1493 0.93 4091 214 0.2418 0.2670
REMARK 3 29 2.1493 - 2.1243 0.93 4129 210 0.2443 0.2989
REMARK 3 30 2.1243 - 2.1000 0.91 4007 201 0.2522 0.2955
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 40.00
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 1.750
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.43610
REMARK 3 B22 (A**2) : -2.06830
REMARK 3 B33 (A**2) : 3.27780
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 3GZO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-09.
REMARK 100 THE RCSB ID CODE IS RCSB052507.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-OCT-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
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 FR-D
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : CONFOCAL OPTICS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS VII
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 140272
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.50800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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: PDB ENTRY 1SOS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M SODIUM MALONATE, PH 6, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 71.65950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.65950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 83.07400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 101.63150
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 83.07400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 101.63150
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 71.65950
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 83.07400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 101.63150
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 71.65950
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 83.07400
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 101.63150
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 79 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
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 HIS A 110 17.95 -67.48
REMARK 500 ASN G 26 5.80 58.28
REMARK 500 ASN H 65 58.49 -143.09
REMARK 500 HIS H 110 -92.51 -49.62
REMARK 500 CYS H 111 137.96 75.49
REMARK 500 LYS I 128 13.82 -143.34
REMARK 500 ASP J 92 46.54 -98.87
REMARK 500 ALA J 93 14.40 57.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B1038 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH D1190 DISTANCE = 5.27 ANGSTROMS
REMARK 525 HOH D1445 DISTANCE = 5.77 ANGSTROMS
REMARK 525 HOH D1543 DISTANCE = 6.82 ANGSTROMS
REMARK 525 HOH D1559 DISTANCE = 5.77 ANGSTROMS
REMARK 525 HOH E1156 DISTANCE = 5.06 ANGSTROMS
REMARK 525 HOH E1192 DISTANCE = 5.26 ANGSTROMS
REMARK 525 HOH E1444 DISTANCE = 5.08 ANGSTROMS
REMARK 525 HOH E1456 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH E1589 DISTANCE = 7.20 ANGSTROMS
REMARK 525 HOH F1595 DISTANCE = 5.13 ANGSTROMS
REMARK 525 HOH G 522 DISTANCE = 5.10 ANGSTROMS
REMARK 525 HOH H1242 DISTANCE = 5.21 ANGSTROMS
REMARK 525 HOH I1184 DISTANCE = 5.28 ANGSTROMS
REMARK 525 HOH I1237 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH I1601 DISTANCE = 5.33 ANGSTROMS
REMARK 525 HOH J1394 DISTANCE = 5.37 ANGSTROMS
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 CU A 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 46 ND1
REMARK 620 2 HIS A 48 NE2 153.8
REMARK 620 3 HIS A 120 NE2 99.3 98.1
REMARK 620 4 HIS A 63 NE2 79.0 104.0 130.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 63 ND1
REMARK 620 2 HIS A 71 ND1 100.2
REMARK 620 3 HIS A 80 ND1 111.5 121.7
REMARK 620 4 ASP A 83 OD1 109.7 99.2 113.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU B 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 46 ND1
REMARK 620 2 HIS B 48 NE2 159.8
REMARK 620 3 HIS B 120 NE2 102.2 97.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 63 ND1
REMARK 620 2 HIS B 71 ND1 103.7
REMARK 620 3 HIS B 80 ND1 114.7 121.0
REMARK 620 4 ASP B 83 OD1 104.8 96.4 113.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU C 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 46 ND1
REMARK 620 2 HIS C 48 NE2 162.1
REMARK 620 3 HIS C 120 NE2 100.7 95.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 63 ND1
REMARK 620 2 HIS C 71 ND1 100.3
REMARK 620 3 HIS C 80 ND1 115.3 123.0
REMARK 620 4 ASP C 83 OD1 97.5 94.0 121.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU D 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 46 ND1
REMARK 620 2 HIS D 48 NE2 145.0
REMARK 620 3 HIS D 120 NE2 108.2 96.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 63 ND1
REMARK 620 2 HIS D 71 ND1 101.4
REMARK 620 3 HIS D 80 ND1 109.7 125.2
REMARK 620 4 ASP D 83 OD1 103.0 99.8 115.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU E 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 46 ND1
REMARK 620 2 HIS E 48 NE2 161.9
REMARK 620 3 HIS E 120 NE2 96.4 98.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 63 ND1
REMARK 620 2 HIS E 71 ND1 102.1
REMARK 620 3 HIS E 80 ND1 108.9 127.4
REMARK 620 4 ASP E 83 OD1 104.2 93.3 117.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU F 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 46 ND1
REMARK 620 2 HIS F 48 NE2 168.0
REMARK 620 3 HIS F 120 NE2 96.8 95.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 63 ND1
REMARK 620 2 HIS F 71 ND1 105.0
REMARK 620 3 HIS F 80 ND1 111.5 123.1
REMARK 620 4 ASP F 83 OD1 107.5 94.0 113.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU G 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 46 ND1
REMARK 620 2 HIS G 48 NE2 148.7
REMARK 620 3 HIS G 120 NE2 104.2 99.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 63 ND1
REMARK 620 2 HIS G 71 ND1 102.7
REMARK 620 3 HIS G 80 ND1 113.3 121.1
REMARK 620 4 ASP G 83 OD1 100.5 95.4 120.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU H 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 46 ND1
REMARK 620 2 HIS H 48 NE2 153.4
REMARK 620 3 HIS H 120 NE2 101.3 93.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN H 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 63 ND1
REMARK 620 2 HIS H 71 ND1 101.1
REMARK 620 3 HIS H 80 ND1 112.8 126.7
REMARK 620 4 ASP H 83 OD1 100.2 98.0 114.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU I 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS I 46 ND1
REMARK 620 2 HIS I 48 NE2 138.3
REMARK 620 3 HIS I 120 NE2 93.4 95.4
REMARK 620 4 HIS I 63 NE2 92.4 110.1 133.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS I 63 ND1
REMARK 620 2 HIS I 71 ND1 113.0
REMARK 620 3 HIS I 80 ND1 111.8 120.7
REMARK 620 4 ASP I 83 OD1 101.1 93.6 113.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU J 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS J 46 ND1
REMARK 620 2 HIS J 48 NE2 165.0
REMARK 620 3 HIS J 120 NE2 95.9 96.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN J 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS J 63 ND1
REMARK 620 2 HIS J 71 ND1 100.6
REMARK 620 3 HIS J 80 ND1 111.8 122.4
REMARK 620 4 ASP J 83 OD1 105.3 100.8 114.0
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 CU A 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU D 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU E 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU F 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU G 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU H 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU I 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU J 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI H 156
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 156
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL J 156
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GZP RELATED DB: PDB
REMARK 900 RELATED ID: 3GZQ RELATED DB: PDB
DBREF 3GZO A 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 3GZO B 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 3GZO C 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 3GZO D 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 3GZO E 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 3GZO F 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 3GZO G 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 3GZO H 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 3GZO I 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 3GZO J 1 153 UNP P00441 SODC_HUMAN 2 154
SEQADV 3GZO ACE A 0 UNP P00441 INSERTION
SEQADV 3GZO ALA A 93 UNP P00441 GLY 94 ENGINEERED
SEQADV 3GZO ACE B 0 UNP P00441 INSERTION
SEQADV 3GZO ALA B 93 UNP P00441 GLY 94 ENGINEERED
SEQADV 3GZO ACE C 0 UNP P00441 INSERTION
SEQADV 3GZO ALA C 93 UNP P00441 GLY 94 ENGINEERED
SEQADV 3GZO ACE D 0 UNP P00441 INSERTION
SEQADV 3GZO ALA D 93 UNP P00441 GLY 94 ENGINEERED
SEQADV 3GZO ACE E 0 UNP P00441 INSERTION
SEQADV 3GZO ALA E 93 UNP P00441 GLY 94 ENGINEERED
SEQADV 3GZO ACE F 0 UNP P00441 INSERTION
SEQADV 3GZO ALA F 93 UNP P00441 GLY 94 ENGINEERED
SEQADV 3GZO ACE G 0 UNP P00441 INSERTION
SEQADV 3GZO ALA G 93 UNP P00441 GLY 94 ENGINEERED
SEQADV 3GZO ACE H 0 UNP P00441 INSERTION
SEQADV 3GZO ALA H 93 UNP P00441 GLY 94 ENGINEERED
SEQADV 3GZO ACE I 0 UNP P00441 INSERTION
SEQADV 3GZO ALA I 93 UNP P00441 GLY 94 ENGINEERED
SEQADV 3GZO ACE J 0 UNP P00441 INSERTION
SEQADV 3GZO ALA J 93 UNP P00441 GLY 94 ENGINEERED
SEQRES 1 A 154 ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 A 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 A 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 A 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 A 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 A 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 A 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 A 154 LYS ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 A 154 ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR
SEQRES 10 A 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 A 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 A 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 B 154 ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 B 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 B 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 B 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 B 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 B 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 B 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 B 154 LYS ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 B 154 ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR
SEQRES 10 B 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 B 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 B 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 C 154 ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 C 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 C 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 C 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 C 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 C 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 C 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 C 154 LYS ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 C 154 ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR
SEQRES 10 C 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 C 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 C 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 D 154 ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 D 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 D 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 D 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 D 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 D 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 D 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 D 154 LYS ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 D 154 ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR
SEQRES 10 D 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 D 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 D 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 E 154 ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 E 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 E 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 E 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 E 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 E 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 E 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 E 154 LYS ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 E 154 ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR
SEQRES 10 E 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 E 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 E 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 F 154 ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 F 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 F 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 F 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 F 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 F 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 F 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 F 154 LYS ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 F 154 ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR
SEQRES 10 F 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 F 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 F 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 G 154 ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 G 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 G 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 G 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 G 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 G 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 G 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 G 154 LYS ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 G 154 ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR
SEQRES 10 G 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 G 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 G 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 H 154 ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 H 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 H 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 H 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 H 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 H 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 H 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 H 154 LYS ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 H 154 ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR
SEQRES 10 H 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 H 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 H 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 I 154 ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 I 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 I 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 I 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 I 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 I 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 I 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 I 154 LYS ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 I 154 ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR
SEQRES 10 I 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 I 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 I 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 J 154 ACE ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY
SEQRES 2 J 154 PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER
SEQRES 3 J 154 ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU
SEQRES 4 J 154 THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY
SEQRES 5 J 154 ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE
SEQRES 6 J 154 ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU
SEQRES 7 J 154 GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP
SEQRES 8 J 154 LYS ASP ALA VAL ALA ASP VAL SER ILE GLU ASP SER VAL
SEQRES 9 J 154 ILE SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR
SEQRES 10 J 154 LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY
SEQRES 11 J 154 GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER
SEQRES 12 J 154 ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
HET ACE A 0 3
HET ACE B 0 3
HET ACE C 0 3
HET ACE D 0 3
HET ACE E 0 3
HET ACE F 0 3
HET ACE G 0 3
HET ACE H 0 3
HET ACE I 0 3
HET ACE J 0 3
HET CU A 154 1
HET ZN A 155 1
HET CU B 154 1
HET ZN B 155 1
HET GOL B 156 6
HET CU C 154 1
HET ZN C 155 1
HET CU D 154 1
HET ZN D 155 1
HET CU E 154 1
HET ZN E 155 1
HET CU F 154 1
HET ZN F 155 1
HET CU G 154 1
HET ZN G 155 1
HET CU H 154 1
HET ZN H 155 1
HET MLI H 156 7
HET CU I 154 1
HET ZN I 155 1
HET CU J 154 1
HET ZN J 155 1
HET GOL J 156 6
HETNAM ACE ACETYL GROUP
HETNAM CU COPPER (II) ION
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETNAM MLI MALONATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 ACE 10(C2 H4 O)
FORMUL 11 CU 10(CU 2+)
FORMUL 12 ZN 10(ZN 2+)
FORMUL 15 GOL 2(C3 H8 O3)
FORMUL 28 MLI C3 H2 O4 2-
FORMUL 34 HOH *1621(H2 O)
HELIX 1 1 ALA A 55 GLY A 61 5 7
HELIX 2 2 ASN A 131 GLY A 138 1 8
HELIX 3 3 ALA B 55 GLY B 61 5 7
HELIX 4 4 SER B 107 CYS B 111 5 5
HELIX 5 5 GLU B 132 LYS B 136 5 5
HELIX 6 6 ALA C 55 GLY C 61 5 7
HELIX 7 7 GLU C 133 GLY C 138 1 6
HELIX 8 8 ALA D 55 GLY D 61 5 7
HELIX 9 9 SER D 107 CYS D 111 5 5
HELIX 10 10 ASN D 131 GLY D 138 1 8
HELIX 11 11 ALA E 55 GLY E 61 5 7
HELIX 12 12 GLU E 132 LYS E 136 5 5
HELIX 13 13 ALA F 55 GLY F 61 5 7
HELIX 14 14 SER F 107 CYS F 111 5 5
HELIX 15 15 GLU F 133 GLY F 138 1 6
HELIX 16 16 ALA G 55 GLY G 61 5 7
HELIX 17 17 GLU G 132 LYS G 136 5 5
HELIX 18 18 ALA H 55 GLY H 61 5 7
HELIX 19 19 GLU H 133 GLY H 138 1 6
HELIX 20 20 ALA I 55 GLY I 61 5 7
HELIX 21 21 GLU I 133 GLY I 138 1 6
HELIX 22 22 ALA J 55 GLY J 61 5 7
HELIX 23 23 ASN J 131 LYS J 136 5 6
SHEET 1 A 5 VAL A 94 ASP A 101 0
SHEET 2 A 5 VAL A 29 LYS A 36 -1 N VAL A 29 O ASP A 101
SHEET 3 A 5 GLN A 15 GLU A 21 -1 N ASN A 19 O TRP A 32
SHEET 4 A 5 LYS A 3 LEU A 8 -1 N CYS A 6 O ILE A 18
SHEET 5 A 5 GLY A 150 ILE A 151 -1 O GLY A 150 N VAL A 5
SHEET 1 B 4 ASP A 83 ALA A 89 0
SHEET 2 B 4 GLY A 41 HIS A 48 -1 N GLY A 41 O ALA A 89
SHEET 3 B 4 THR A 116 HIS A 120 -1 O THR A 116 N HIS A 48
SHEET 4 B 4 ARG A 143 VAL A 148 -1 O ALA A 145 N VAL A 119
SHEET 1 C 5 ALA B 95 ASP B 101 0
SHEET 2 C 5 VAL B 29 LYS B 36 -1 N VAL B 29 O ASP B 101
SHEET 3 C 5 GLN B 15 GLU B 21 -1 N ASN B 19 O TRP B 32
SHEET 4 C 5 LYS B 3 LEU B 8 -1 N CYS B 6 O ILE B 18
SHEET 5 C 5 GLY B 150 ILE B 151 -1 O GLY B 150 N VAL B 5
SHEET 1 D 4 ASP B 83 ALA B 89 0
SHEET 2 D 4 GLY B 41 HIS B 48 -1 N GLY B 41 O ALA B 89
SHEET 3 D 4 THR B 116 HIS B 120 -1 O THR B 116 N HIS B 48
SHEET 4 D 4 ARG B 143 VAL B 148 -1 O ALA B 145 N VAL B 119
SHEET 1 E 5 ALA C 95 ASP C 101 0
SHEET 2 E 5 VAL C 29 LYS C 36 -1 N VAL C 29 O ASP C 101
SHEET 3 E 5 GLN C 15 GLU C 21 -1 N ASN C 19 O TRP C 32
SHEET 4 E 5 LYS C 3 LEU C 8 -1 N LEU C 8 O GLY C 16
SHEET 5 E 5 GLY C 150 ILE C 151 -1 O GLY C 150 N VAL C 5
SHEET 1 F 4 ASP C 83 ALA C 89 0
SHEET 2 F 4 GLY C 41 HIS C 48 -1 N GLY C 41 O ALA C 89
SHEET 3 F 4 THR C 116 HIS C 120 -1 O THR C 116 N HIS C 48
SHEET 4 F 4 ARG C 143 VAL C 148 -1 O GLY C 147 N LEU C 117
SHEET 1 G 5 ALA D 95 ASP D 101 0
SHEET 2 G 5 VAL D 29 LYS D 36 -1 N VAL D 31 O ILE D 99
SHEET 3 G 5 GLN D 15 GLU D 21 -1 N ASN D 19 O TRP D 32
SHEET 4 G 5 LYS D 3 LEU D 8 -1 N CYS D 6 O ILE D 18
SHEET 5 G 5 GLY D 150 ILE D 151 -1 O GLY D 150 N VAL D 5
SHEET 1 H 4 ASP D 83 ALA D 89 0
SHEET 2 H 4 GLY D 41 HIS D 48 -1 N PHE D 45 O GLY D 85
SHEET 3 H 4 THR D 116 HIS D 120 -1 O THR D 116 N HIS D 48
SHEET 4 H 4 ARG D 143 VAL D 148 -1 O GLY D 147 N LEU D 117
SHEET 1 I 5 VAL E 94 ASP E 101 0
SHEET 2 I 5 VAL E 29 LYS E 36 -1 N VAL E 29 O ASP E 101
SHEET 3 I 5 GLN E 15 GLU E 21 -1 N ASN E 19 O TRP E 32
SHEET 4 I 5 LYS E 3 LYS E 9 -1 N LEU E 8 O GLY E 16
SHEET 5 I 5 GLY E 150 ILE E 151 -1 O GLY E 150 N VAL E 5
SHEET 1 J 4 ASP E 83 ALA E 89 0
SHEET 2 J 4 GLY E 41 HIS E 48 -1 N GLY E 41 O ALA E 89
SHEET 3 J 4 THR E 116 HIS E 120 -1 O THR E 116 N HIS E 48
SHEET 4 J 4 ARG E 143 VAL E 148 -1 O ALA E 145 N VAL E 119
SHEET 1 K 5 VAL F 94 ASP F 101 0
SHEET 2 K 5 VAL F 29 LYS F 36 -1 N VAL F 31 O ILE F 99
SHEET 3 K 5 GLN F 15 GLU F 21 -1 N ASN F 19 O TRP F 32
SHEET 4 K 5 LYS F 3 LEU F 8 -1 N ALA F 4 O PHE F 20
SHEET 5 K 5 GLY F 150 ILE F 151 -1 O GLY F 150 N VAL F 5
SHEET 1 L 4 ASP F 83 ALA F 89 0
SHEET 2 L 4 GLY F 41 HIS F 48 -1 N GLY F 41 O ALA F 89
SHEET 3 L 4 THR F 116 HIS F 120 -1 O THR F 116 N HIS F 48
SHEET 4 L 4 ARG F 143 VAL F 148 -1 O ALA F 145 N VAL F 119
SHEET 1 M 8 ASP G 83 ALA G 89 0
SHEET 2 M 8 GLY G 41 HIS G 48 -1 N GLY G 41 O ALA G 89
SHEET 3 M 8 THR G 116 HIS G 120 -1 O THR G 116 N HIS G 48
SHEET 4 M 8 ARG G 143 ILE G 151 -1 O GLY G 147 N LEU G 117
SHEET 5 M 8 LYS G 3 LEU G 8 -1 N VAL G 5 O GLY G 150
SHEET 6 M 8 GLN G 15 GLN G 22 -1 O GLY G 16 N LEU G 8
SHEET 7 M 8 VAL G 29 LYS G 36 -1 O TRP G 32 N ASN G 19
SHEET 8 M 8 VAL G 94 ASP G 101 -1 O VAL G 97 N GLY G 33
SHEET 1 N 5 VAL H 94 ASP H 101 0
SHEET 2 N 5 VAL H 29 LYS H 36 -1 N ILE H 35 O ALA H 95
SHEET 3 N 5 GLN H 15 GLN H 22 -1 N ASN H 19 O TRP H 32
SHEET 4 N 5 LYS H 3 LEU H 8 -1 N LEU H 8 O GLY H 16
SHEET 5 N 5 GLY H 150 ILE H 151 -1 O GLY H 150 N VAL H 5
SHEET 1 O 4 ASP H 83 ALA H 89 0
SHEET 2 O 4 GLY H 41 HIS H 48 -1 N GLY H 41 O ALA H 89
SHEET 3 O 4 THR H 116 HIS H 120 -1 O THR H 116 N HIS H 48
SHEET 4 O 4 ARG H 143 VAL H 148 -1 O GLY H 147 N LEU H 117
SHEET 1 P 5 ALA I 95 ASP I 101 0
SHEET 2 P 5 VAL I 29 LYS I 36 -1 N VAL I 29 O ASP I 101
SHEET 3 P 5 GLN I 15 GLN I 22 -1 N ASN I 19 O TRP I 32
SHEET 4 P 5 LYS I 3 LYS I 9 -1 N LEU I 8 O GLY I 16
SHEET 5 P 5 GLY I 150 ILE I 151 -1 O GLY I 150 N VAL I 5
SHEET 1 Q 4 ASP I 83 ALA I 89 0
SHEET 2 Q 4 GLY I 41 HIS I 48 -1 N GLY I 41 O ALA I 89
SHEET 3 Q 4 THR I 116 HIS I 120 -1 O THR I 116 N HIS I 48
SHEET 4 Q 4 ARG I 143 VAL I 148 -1 O ALA I 145 N VAL I 119
SHEET 1 R 5 ALA J 95 ASP J 101 0
SHEET 2 R 5 VAL J 29 LYS J 36 -1 N VAL J 31 O ILE J 99
SHEET 3 R 5 GLN J 15 GLU J 21 -1 N ASN J 19 O TRP J 32
SHEET 4 R 5 LYS J 3 LYS J 9 -1 N LEU J 8 O GLY J 16
SHEET 5 R 5 GLY J 150 ILE J 151 -1 O GLY J 150 N VAL J 5
SHEET 1 S 4 ASP J 83 ALA J 89 0
SHEET 2 S 4 GLY J 41 HIS J 48 -1 N GLY J 41 O ALA J 89
SHEET 3 S 4 THR J 116 HIS J 120 -1 O THR J 116 N HIS J 48
SHEET 4 S 4 ARG J 143 VAL J 148 -1 O GLY J 147 N LEU J 117
SSBOND 1 CYS A 57 CYS A 146 1555 1555 2.60
SSBOND 2 CYS B 57 CYS B 146 1555 1555 2.61
SSBOND 3 CYS C 57 CYS C 146 1555 1555 2.67
SSBOND 4 CYS D 57 CYS D 146 1555 1555 2.61
SSBOND 5 CYS E 57 CYS E 146 1555 1555 2.67
SSBOND 6 CYS F 57 CYS F 146 1555 1555 2.60
SSBOND 7 CYS G 57 CYS G 146 1555 1555 2.62
SSBOND 8 CYS H 57 CYS H 146 1555 1555 2.65
SSBOND 9 CYS I 57 CYS I 146 1555 1555 2.77
SSBOND 10 CYS J 57 CYS J 146 1555 1555 2.64
LINK C ACE A 0 N ALA A 1 1555 1555 1.33
LINK C ACE B 0 N ALA B 1 1555 1555 1.34
LINK C ACE C 0 N ALA C 1 1555 1555 1.34
LINK C ACE D 0 N ALA D 1 1555 1555 1.34
LINK C ACE E 0 N ALA E 1 1555 1555 1.34
LINK C ACE F 0 N ALA F 1 1555 1555 1.34
LINK C ACE G 0 N ALA G 1 1555 1555 1.36
LINK C ACE H 0 N ALA H 1 1555 1555 1.34
LINK C ACE I 0 N ALA I 1 1555 1555 1.35
LINK C ACE J 0 N ALA J 1 1555 1555 1.34
LINK ND1 HIS A 46 CU CU A 154 1555 1555 2.30
LINK NE2 HIS A 48 CU CU A 154 1555 1555 2.05
LINK ND1 HIS A 63 ZN ZN A 155 1555 1555 2.14
LINK ND1 HIS A 71 ZN ZN A 155 1555 1555 2.13
LINK ND1 HIS A 80 ZN ZN A 155 1555 1555 2.07
LINK OD1 ASP A 83 ZN ZN A 155 1555 1555 1.89
LINK NE2 HIS A 120 CU CU A 154 1555 1555 2.00
LINK ND1 HIS B 46 CU CU B 154 1555 1555 2.24
LINK NE2 HIS B 48 CU CU B 154 1555 1555 2.06
LINK ND1 HIS B 63 ZN ZN B 155 1555 1555 2.06
LINK ND1 HIS B 71 ZN ZN B 155 1555 1555 2.06
LINK ND1 HIS B 80 ZN ZN B 155 1555 1555 2.11
LINK OD1 ASP B 83 ZN ZN B 155 1555 1555 1.94
LINK NE2 HIS B 120 CU CU B 154 1555 1555 2.06
LINK ND1 HIS C 46 CU CU C 154 1555 1555 2.32
LINK NE2 HIS C 48 CU CU C 154 1555 1555 2.10
LINK ND1 HIS C 63 ZN ZN C 155 1555 1555 2.34
LINK ND1 HIS C 71 ZN ZN C 155 1555 1555 2.22
LINK ND1 HIS C 80 ZN ZN C 155 1555 1555 2.00
LINK OD1 ASP C 83 ZN ZN C 155 1555 1555 2.05
LINK NE2 HIS C 120 CU CU C 154 1555 1555 2.10
LINK ND1 HIS D 46 CU CU D 154 1555 1555 2.20
LINK NE2 HIS D 48 CU CU D 154 1555 1555 2.15
LINK ND1 HIS D 63 ZN ZN D 155 1555 1555 2.16
LINK ND1 HIS D 71 ZN ZN D 155 1555 1555 2.09
LINK ND1 HIS D 80 ZN ZN D 155 1555 1555 2.12
LINK OD1 ASP D 83 ZN ZN D 155 1555 1555 2.07
LINK NE2 HIS D 120 CU CU D 154 1555 1555 2.12
LINK ND1 HIS E 46 CU CU E 154 1555 1555 2.27
LINK NE2 HIS E 48 CU CU E 154 1555 1555 2.09
LINK ND1 HIS E 63 ZN ZN E 155 1555 1555 2.07
LINK ND1 HIS E 71 ZN ZN E 155 1555 1555 2.07
LINK ND1 HIS E 80 ZN ZN E 155 1555 1555 2.08
LINK OD1 ASP E 83 ZN ZN E 155 1555 1555 1.97
LINK NE2 HIS E 120 CU CU E 154 1555 1555 2.06
LINK ND1 HIS F 46 CU CU F 154 1555 1555 2.27
LINK NE2 HIS F 48 CU CU F 154 1555 1555 2.11
LINK ND1 HIS F 63 ZN ZN F 155 1555 1555 2.02
LINK ND1 HIS F 71 ZN ZN F 155 1555 1555 2.22
LINK ND1 HIS F 80 ZN ZN F 155 1555 1555 2.19
LINK OD1 ASP F 83 ZN ZN F 155 1555 1555 1.88
LINK NE2 HIS F 120 CU CU F 154 1555 1555 2.17
LINK ND1 HIS G 46 CU CU G 154 1555 1555 2.30
LINK NE2 HIS G 48 CU CU G 154 1555 1555 2.02
LINK ND1 HIS G 63 ZN ZN G 155 1555 1555 2.16
LINK ND1 HIS G 71 ZN ZN G 155 1555 1555 2.10
LINK ND1 HIS G 80 ZN ZN G 155 1555 1555 2.10
LINK OD1 ASP G 83 ZN ZN G 155 1555 1555 1.97
LINK NE2 HIS G 120 CU CU G 154 1555 1555 1.98
LINK ND1 HIS H 46 CU CU H 154 1555 1555 2.20
LINK NE2 HIS H 48 CU CU H 154 1555 1555 2.14
LINK ND1 HIS H 63 ZN ZN H 155 1555 1555 2.06
LINK ND1 HIS H 71 ZN ZN H 155 1555 1555 2.10
LINK ND1 HIS H 80 ZN ZN H 155 1555 1555 2.04
LINK OD1 ASP H 83 ZN ZN H 155 1555 1555 2.00
LINK NE2 HIS H 120 CU CU H 154 1555 1555 2.05
LINK ND1 HIS I 46 CU CU I 154 1555 1555 2.23
LINK NE2 HIS I 48 CU CU I 154 1555 1555 2.22
LINK ND1 HIS I 63 ZN ZN I 155 1555 1555 2.08
LINK ND1 HIS I 71 ZN ZN I 155 1555 1555 2.36
LINK ND1 HIS I 80 ZN ZN I 155 1555 1555 2.12
LINK OD1 ASP I 83 ZN ZN I 155 1555 1555 2.01
LINK NE2 HIS I 120 CU CU I 154 1555 1555 2.08
LINK ND1 HIS J 46 CU CU J 154 1555 1555 2.25
LINK NE2 HIS J 48 CU CU J 154 1555 1555 2.08
LINK ND1 HIS J 63 ZN ZN J 155 1555 1555 2.18
LINK ND1 HIS J 71 ZN ZN J 155 1555 1555 2.18
LINK ND1 HIS J 80 ZN ZN J 155 1555 1555 2.02
LINK OD1 ASP J 83 ZN ZN J 155 1555 1555 2.02
LINK NE2 HIS J 120 CU CU J 154 1555 1555 2.10
LINK NE2 HIS I 63 CU CU I 154 1555 1555 2.59
LINK NE2 HIS A 63 CU CU A 154 1555 1555 2.66
SITE 1 AC1 5 HIS A 46 HIS A 48 HIS A 63 HIS A 120
SITE 2 AC1 5 HOH A 679
SITE 1 AC2 4 HIS A 63 HIS A 71 HIS A 80 ASP A 83
SITE 1 AC3 4 HIS B 46 HIS B 48 HIS B 63 HIS B 120
SITE 1 AC4 4 HIS B 63 HIS B 71 HIS B 80 ASP B 83
SITE 1 AC5 4 HIS C 46 HIS C 48 HIS C 63 HIS C 120
SITE 1 AC6 4 HIS C 63 HIS C 71 HIS C 80 ASP C 83
SITE 1 AC7 4 HIS D 46 HIS D 48 HIS D 63 HIS D 120
SITE 1 AC8 4 HIS D 63 HIS D 71 HIS D 80 ASP D 83
SITE 1 AC9 4 HIS E 46 HIS E 48 HIS E 63 HIS E 120
SITE 1 BC1 5 HIS E 63 HIS E 71 HIS E 80 ASP E 83
SITE 2 BC1 5 LYS E 136
SITE 1 BC2 4 HIS F 46 HIS F 48 HIS F 63 HIS F 120
SITE 1 BC3 5 HIS F 63 HIS F 71 HIS F 80 ASP F 83
SITE 2 BC3 5 LYS F 136
SITE 1 BC4 4 HIS G 46 HIS G 48 HIS G 63 HIS G 120
SITE 1 BC5 4 HIS G 63 HIS G 71 HIS G 80 ASP G 83
SITE 1 BC6 4 HIS H 46 HIS H 48 HIS H 63 HIS H 120
SITE 1 BC7 4 HIS H 63 HIS H 71 HIS H 80 ASP H 83
SITE 1 BC8 5 HIS I 46 HIS I 48 HIS I 63 HIS I 120
SITE 2 BC8 5 HOH I 394
SITE 1 BC9 4 HIS I 63 HIS I 71 HIS I 80 ASP I 83
SITE 1 CC1 4 HIS J 46 HIS J 48 HIS J 63 HIS J 120
SITE 1 CC2 4 HIS J 63 HIS J 71 HIS J 80 ASP J 83
SITE 1 CC3 10 LEU G 67 ARG G 69 PHE H 64 PRO H 66
SITE 2 CC3 10 VAL H 103 ILE H 104 SER H 105 CYS H 111
SITE 3 CC3 10 ILE H 112 HOH H 160
SITE 1 CC4 7 HIS B 48 HIS B 63 HIS B 120 GLY B 141
SITE 2 CC4 7 ARG B 143 HOH B 381 HOH B 493
SITE 1 CC5 8 HIS J 48 HIS J 63 HIS J 120 THR J 137
SITE 2 CC5 8 GLY J 141 ARG J 143 HOH J 167 HOH J1325
CRYST1 166.148 203.263 143.319 90.00 90.00 90.00 C 2 2 21 80
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 0.006019 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004920 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006977 0.00000
HETATM 1 C ACE A 0 54.923 48.666 30.354 1.00 40.25 C
HETATM 2 O ACE A 0 55.189 47.816 31.211 1.00 45.21 O
HETATM 3 CH3 ACE A 0 55.477 50.062 30.363 1.00 35.59 C
(ATOM LINES ARE NOT SHOWN.)
END
