HEADER OXIDOREDUCTASE 07-APR-09 3GZQ
TITLE HUMAN SOD1 A4V METAL-FREE VARIANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];
COMPND 3 CHAIN: A, B;
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,
KEYWDS 2 ANTIOXIDANT, METAL-BINDING, COPPER, ZINC, AMYOTROPHIC
KEYWDS 3 LATERAL SCLEROSIS, DISEASE MUTATION, ACETYLATION,
KEYWDS 4 CYTOPLASM, APO, DISULFIDE BOND, PHOSPHOPROTEIN, UBL
KEYWDS 5 CONJUGATION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.GALALELDEEN,A.B.TAYLOR,L.J.WHITSON,P.J.HART
REVDAT 2 22-DEC-09 3GZQ 1 JRNL
REVDAT 1 13-OCT-09 3GZQ 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 1
REMARK 2
REMARK 2 RESOLUTION. 1.40 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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.06
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 49501
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 2518
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 30.0705 - 3.6690 0.97 2751 154 0.1745 0.2028
REMARK 3 2 3.6690 - 2.9130 0.99 2698 150 0.1608 0.1767
REMARK 3 3 2.9130 - 2.5450 1.00 2671 133 0.1680 0.1893
REMARK 3 4 2.5450 - 2.3124 1.00 2692 138 0.1564 0.1749
REMARK 3 5 2.3124 - 2.1467 0.99 2615 136 0.1556 0.1755
REMARK 3 6 2.1467 - 2.0202 1.00 2625 149 0.1315 0.1807
REMARK 3 7 2.0202 - 1.9190 0.99 2615 136 0.1404 0.1617
REMARK 3 8 1.9190 - 1.8355 0.99 2606 136 0.1333 0.1834
REMARK 3 9 1.8355 - 1.7648 1.00 2639 135 0.1236 0.1791
REMARK 3 10 1.7648 - 1.7039 1.00 2620 152 0.1233 0.1541
REMARK 3 11 1.7039 - 1.6507 1.00 2639 123 0.1191 0.1757
REMARK 3 12 1.6507 - 1.6035 1.00 2595 159 0.1227 0.1573
REMARK 3 13 1.6035 - 1.5613 1.00 2573 144 0.1237 0.1732
REMARK 3 14 1.5613 - 1.5232 1.00 2625 145 0.1338 0.1769
REMARK 3 15 1.5232 - 1.4886 1.00 2600 152 0.1439 0.1884
REMARK 3 16 1.4886 - 1.4569 0.99 2598 124 0.1625 0.2060
REMARK 3 17 1.4569 - 1.4277 0.97 2516 139 0.1832 0.1981
REMARK 3 18 1.4277 - 1.4010 0.89 2305 113 0.2138 0.2539
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 : 60.38
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.82190
REMARK 3 B22 (A**2) : 2.84700
REMARK 3 B33 (A**2) : 0.97490
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 : 0.006 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 3GZQ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-09.
REMARK 100 THE RCSB ID CODE IS RCSB052509.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49673
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
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 (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 33.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.58200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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 1OZU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M AMMONIUM SULFATE, 0.1 M MES,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 20.25650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.46900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.40550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.46900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.25650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.40550
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 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 ACE A 0
REMARK 465 ALA A 1
REMARK 465 LEU A 67
REMARK 465 SER A 68
REMARK 465 ARG A 69
REMARK 465 LYS A 70
REMARK 465 HIS A 71
REMARK 465 GLY A 72
REMARK 465 GLY A 73
REMARK 465 PRO A 74
REMARK 465 LYS A 75
REMARK 465 ASP A 76
REMARK 465 GLU A 77
REMARK 465 GLU A 78
REMARK 465 ARG A 79
REMARK 465 LEU A 126
REMARK 465 GLY A 127
REMARK 465 LYS A 128
REMARK 465 GLY A 129
REMARK 465 GLY A 130
REMARK 465 ASN A 131
REMARK 465 GLU A 132
REMARK 465 GLU A 133
REMARK 465 SER A 134
REMARK 465 THR A 135
REMARK 465 LYS A 136
REMARK 465 THR A 137
REMARK 465 GLY A 138
REMARK 465 ASN A 139
REMARK 465 ALA A 140
REMARK 465 GLY A 141
REMARK 465 SER B 68
REMARK 465 ARG B 69
REMARK 465 LYS B 70
REMARK 465 HIS B 71
REMARK 465 GLY B 72
REMARK 465 GLY B 73
REMARK 465 PRO B 74
REMARK 465 LYS B 75
REMARK 465 ASP B 76
REMARK 465 GLU B 77
REMARK 465 GLU B 78
REMARK 465 ARG B 79
REMARK 465 ASP B 125
REMARK 465 LEU B 126
REMARK 465 GLY B 127
REMARK 465 LYS B 128
REMARK 465 GLY B 129
REMARK 465 GLY B 130
REMARK 465 ASN B 131
REMARK 465 GLU B 132
REMARK 465 GLU B 133
REMARK 465 SER B 134
REMARK 465 THR B 135
REMARK 465 LYS B 136
REMARK 465 THR B 137
REMARK 465 GLY B 138
REMARK 465 ASN B 139
REMARK 465 ALA B 140
REMARK 465 GLY B 141
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 ASN A 65 80.49 -156.13
REMARK 500 ASN B 65 72.53 -159.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 154
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 154
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GZO RELATED DB: PDB
REMARK 900 RELATED ID: 3GZP RELATED DB: PDB
DBREF 3GZQ A 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 3GZQ B 1 153 UNP P00441 SODC_HUMAN 2 154
SEQADV 3GZQ ACE A 0 UNP P00441 INSERTION
SEQADV 3GZQ VAL A 4 UNP P00441 ALA 5 ENGINEERED
SEQADV 3GZQ ACE B 0 UNP P00441 INSERTION
SEQADV 3GZQ VAL B 4 UNP P00441 ALA 5 ENGINEERED
SEQRES 1 A 154 ACE ALA THR LYS VAL 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 GLY 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 VAL 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 GLY 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
HET ACE B 0 3
HET SO4 A 154 5
HET SO4 B 154 5
HETNAM ACE ACETYL GROUP
HETNAM SO4 SULFATE ION
FORMUL 2 ACE C2 H4 O
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *251(H2 O)
HELIX 1 1 CYS A 57 GLY A 61 5 5
HELIX 2 2 SER A 107 CYS A 111 5 5
HELIX 3 3 ALA B 55 ALA B 60 5 6
HELIX 4 4 SER B 107 CYS B 111 5 5
SHEET 1 A 5 ALA A 95 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 LEU A 8 O GLY A 16
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 GLY A 147 N LEU A 117
SHEET 1 C 5 ALA B 95 ASP B 101 0
SHEET 2 C 5 VAL B 29 LYS B 36 -1 N ILE B 35 O ALA B 95
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 LEU B 8 O GLY B 16
SHEET 5 C 5 GLY B 150 GLN B 153 -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
SSBOND 1 CYS A 57 CYS A 146 1555 1555 2.27
SSBOND 2 CYS B 57 CYS B 146 1555 1555 2.25
LINK C ACE B 0 N ALA B 1 1555 1555 1.33
SITE 1 AC1 7 HIS B 48 HIS B 63 HIS B 120 ARG B 143
SITE 2 AC1 7 HOH B 158 HOH B 218 HOH B 274
SITE 1 AC2 5 HIS A 48 HIS A 63 HIS A 120 ARG A 143
SITE 2 AC2 5 HOH A 194
CRYST1 40.513 58.811 104.938 90.00 90.00 90.00 P 21 21 21 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 0.024683 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017004 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009529 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
