HEADER OXIDOREDUCTASE 23-JUL-14 4U4I
TITLE MEGAVIRUS CHILENSIS SUPEROXIDE DISMUTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CU/ZN SUPEROXIDE DISMUTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.15.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: THE LOOPS INVOLVED IN COPPER AND ZINC BINDING ARE
COMPND 8 DISRDERED IN THE CRYSTAL STRUCTURE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MEGAVIRUS CHILIENSIS;
SOURCE 3 ORGANISM_TAXID: 1094892;
SOURCE 4 GENE: MG277;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: ROSETTA;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: MODIFIED PETDUET
KEYWDS CU-ZN SUPEROXIDE DISMUTASE, METAL-FREE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.LARTIGUE,J.-M.CLAVERIE,B.BURLAT,B.COUTARD,C.ABERGEL
REVDAT 3 24-DEC-14 4U4I 1 JRNL
REVDAT 2 12-NOV-14 4U4I 1 JRNL
REVDAT 1 05-NOV-14 4U4I 0
JRNL AUTH A.LARTIGUE,B.BURLAT,B.COUTARD,F.CHASPOUL,J.M.CLAVERIE,
JRNL AUTH 2 C.ABERGEL
JRNL TITL THE MEGAVIRUS CHILENSIS CU,ZN-SUPEROXIDE DISMUTASE: THE
JRNL TITL 2 FIRST VIRAL STRUCTURE OF A TYPICAL CELLULAR COPPER
JRNL TITL 3 CHAPERONE-INDEPENDENT HYPERSTABLE DIMERIC ENZYME.
JRNL REF J.VIROL. V. 89 824 2015
JRNL REFN ESSN 1098-5514
JRNL PMID 25355875
JRNL DOI 10.1128/JVI.02588-14
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.LARTIGUE,N.PHILIPPE,S.JEUDY,C.ABERGEL
REMARK 1 TITL PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF THE MEGAVIRUS
REMARK 1 TITL 2 SUPEROXIDE DISMUTASE.
REMARK 1 REF ACTA CRYSTALLOGR. SECT. F V. 68 1557 2012
REMARK 1 REF 2 STRUCT. BIOL. CRYST. COMMUN.
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 23192047
REMARK 1 DOI 10.1107/S174430911204657X
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.04
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 15726
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1573
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 38.0461 - 4.8897 1.00 1415 157 0.2028 0.2314
REMARK 3 2 4.8897 - 3.8823 1.00 1323 147 0.1642 0.1884
REMARK 3 3 3.8823 - 3.3919 1.00 1293 144 0.1763 0.1934
REMARK 3 4 3.3919 - 3.0820 1.00 1283 142 0.1775 0.2320
REMARK 3 5 3.0820 - 2.8611 1.00 1270 142 0.1882 0.2638
REMARK 3 6 2.8611 - 2.6925 1.00 1270 141 0.1948 0.2614
REMARK 3 7 2.6925 - 2.5577 1.00 1270 141 0.2069 0.2717
REMARK 3 8 2.5577 - 2.4464 1.00 1255 140 0.1948 0.2331
REMARK 3 9 2.4464 - 2.3522 1.00 1255 139 0.1862 0.2201
REMARK 3 10 2.3522 - 2.2710 1.00 1256 140 0.1886 0.2568
REMARK 3 11 2.2710 - 2.2000 1.00 1263 140 0.2090 0.2767
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.830
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.83
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 1980
REMARK 3 ANGLE : 1.139 2671
REMARK 3 CHIRALITY : 0.053 289
REMARK 3 PLANARITY : 0.005 354
REMARK 3 DIHEDRAL : 14.254 719
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 4U4I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000202784.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 105
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15785
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 39.140
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.90
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 15.00
REMARK 200 R MERGE FOR SHELL (I) : 0.80000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: RODS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE BUFFER, 20%(W/V)
REMARK 280 PEG 4000, 20%(V/V) MPD
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 58.71300
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 35.31300
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 35.31300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 88.06950
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 35.31300
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 35.31300
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 29.35650
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 35.31300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 35.31300
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 88.06950
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 35.31300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.31300
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 29.35650
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 58.71300
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: 11910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 GLY A 1
REMARK 465 PRO A 2
REMARK 465 GLY A 3
REMARK 465 SER A 4
REMARK 465 SER A 5
REMARK 465 ARG A 6
REMARK 465 TYR A 7
REMARK 465 ASP A 8
REMARK 465 GLY A 77
REMARK 465 VAL A 78
REMARK 465 HIS A 79
REMARK 465 LYS A 80
REMARK 465 ASP A 81
REMARK 465 ILE A 82
REMARK 465 ASN A 83
REMARK 465 ILE A 84
REMARK 465 GLN A 85
REMARK 465 HIS A 86
REMARK 465 ASN A 87
REMARK 465 HIS A 88
REMARK 465 LEU A 134
REMARK 465 GLY A 135
REMARK 465 MSE A 136
REMARK 465 THR A 137
REMARK 465 ASN A 138
REMARK 465 HIS A 139
REMARK 465 PRO A 140
REMARK 465 ASP A 141
REMARK 465 SER A 142
REMARK 465 LYS A 143
REMARK 465 THR A 144
REMARK 465 THR A 145
REMARK 465 GLY A 146
REMARK 465 ASN A 147
REMARK 465 SER A 148
REMARK 465 GLY B 1
REMARK 465 PRO B 2
REMARK 465 GLY B 3
REMARK 465 SER B 4
REMARK 465 SER B 5
REMARK 465 ARG B 6
REMARK 465 ASN B 76
REMARK 465 GLY B 77
REMARK 465 VAL B 78
REMARK 465 HIS B 79
REMARK 465 LYS B 80
REMARK 465 ASP B 81
REMARK 465 ILE B 82
REMARK 465 ASN B 83
REMARK 465 ILE B 84
REMARK 465 GLN B 85
REMARK 465 HIS B 86
REMARK 465 ASN B 87
REMARK 465 HIS B 88
REMARK 465 LEU B 89
REMARK 465 GLY B 90
REMARK 465 ASP B 91
REMARK 465 ASP B 133
REMARK 465 LEU B 134
REMARK 465 GLY B 135
REMARK 465 MSE B 136
REMARK 465 THR B 137
REMARK 465 ASN B 138
REMARK 465 HIS B 139
REMARK 465 PRO B 140
REMARK 465 ASP B 141
REMARK 465 SER B 142
REMARK 465 LYS B 143
REMARK 465 THR B 144
REMARK 465 THR B 145
REMARK 465 GLY B 146
REMARK 465 ASN B 147
REMARK 465 SER B 148
REMARK 465 GLY B 149
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 TYR B 7 O
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 252 O HOH A 253 1.84
REMARK 500 OD1 ASN A 11 O HOH A 201 1.98
REMARK 500 O HOH A 215 O HOH A 224 2.02
REMARK 500 O HOH A 219 O HOH A 234 2.10
REMARK 500 O HOH B 225 O HOH B 236 2.10
REMARK 500 O ASP A 133 O HOH A 202 2.16
REMARK 500 O HOH A 222 O HOH A 227 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 227 O HOH B 222 4555 1.72
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 CYS A 36 137.86 -172.68
REMARK 500 ARG A 123 -162.61 -111.01
REMARK 500 ASN B 63 41.38 -100.40
REMARK 500 PRO B 74 12.68 -69.90
REMARK 500 LEU B 112 80.58 -162.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 35 CYS A 36 -149.99
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4U4I A 5 161 UNP G5CS11 G5CS11_9VIRU 2 158
DBREF 4U4I B 5 161 UNP G5CS11 G5CS11_9VIRU 2 158
SEQADV 4U4I GLY A 1 UNP G5CS11 EXPRESSION TAG
SEQADV 4U4I PRO A 2 UNP G5CS11 EXPRESSION TAG
SEQADV 4U4I GLY A 3 UNP G5CS11 EXPRESSION TAG
SEQADV 4U4I SER A 4 UNP G5CS11 EXPRESSION TAG
SEQADV 4U4I GLY B 1 UNP G5CS11 EXPRESSION TAG
SEQADV 4U4I PRO B 2 UNP G5CS11 EXPRESSION TAG
SEQADV 4U4I GLY B 3 UNP G5CS11 EXPRESSION TAG
SEQADV 4U4I SER B 4 UNP G5CS11 EXPRESSION TAG
SEQRES 1 A 161 GLY PRO GLY SER SER ARG TYR ASP PHE PHE ASN VAL VAL
SEQRES 2 A 161 THR ALA ILE CYS GLN LEU ASP LYS PRO HIS ASP TYR GLY
SEQRES 3 A 161 TYR ALA ILE PHE THR GLN LEU PRO ASP CYS THR GLU ILE
SEQRES 4 A 161 GLN PHE HIS LEU LYS ASN LEU PRO PRO GLY LYS HIS GLY
SEQRES 5 A 161 CYS HIS ILE HIS LYS SER GLY ASP ARG ARG ASN GLY CYS
SEQRES 6 A 161 THR SER MSE GLY PRO HIS PHE ASN PRO PHE ASN GLY VAL
SEQRES 7 A 161 HIS LYS ASP ILE ASN ILE GLN HIS ASN HIS LEU GLY ASP
SEQRES 8 A 161 LEU GLY ASN ILE VAL VAL ASN ASN ASN GLY GLU CYS ASN
SEQRES 9 A 161 GLU ILE ILE CYS VAL LYS TYR LEU PRO LEU THR GLY SER
SEQRES 10 A 161 ASN GLN ILE ILE GLY ARG GLY LEU VAL ILE HIS GLU LYS
SEQRES 11 A 161 GLU ASP ASP LEU GLY MSE THR ASN HIS PRO ASP SER LYS
SEQRES 12 A 161 THR THR GLY ASN SER GLY ASP ARG ILE ALA CYS GLY ILE
SEQRES 13 A 161 ILE ALA TYR LEU ASN
SEQRES 1 B 161 GLY PRO GLY SER SER ARG TYR ASP PHE PHE ASN VAL VAL
SEQRES 2 B 161 THR ALA ILE CYS GLN LEU ASP LYS PRO HIS ASP TYR GLY
SEQRES 3 B 161 TYR ALA ILE PHE THR GLN LEU PRO ASP CYS THR GLU ILE
SEQRES 4 B 161 GLN PHE HIS LEU LYS ASN LEU PRO PRO GLY LYS HIS GLY
SEQRES 5 B 161 CYS HIS ILE HIS LYS SER GLY ASP ARG ARG ASN GLY CYS
SEQRES 6 B 161 THR SER MSE GLY PRO HIS PHE ASN PRO PHE ASN GLY VAL
SEQRES 7 B 161 HIS LYS ASP ILE ASN ILE GLN HIS ASN HIS LEU GLY ASP
SEQRES 8 B 161 LEU GLY ASN ILE VAL VAL ASN ASN ASN GLY GLU CYS ASN
SEQRES 9 B 161 GLU ILE ILE CYS VAL LYS TYR LEU PRO LEU THR GLY SER
SEQRES 10 B 161 ASN GLN ILE ILE GLY ARG GLY LEU VAL ILE HIS GLU LYS
SEQRES 11 B 161 GLU ASP ASP LEU GLY MSE THR ASN HIS PRO ASP SER LYS
SEQRES 12 B 161 THR THR GLY ASN SER GLY ASP ARG ILE ALA CYS GLY ILE
SEQRES 13 B 161 ILE ALA TYR LEU ASN
MODRES 4U4I MSE A 68 MET MODIFIED RESIDUE
MODRES 4U4I MSE B 68 MET MODIFIED RESIDUE
HET MSE A 68 8
HET MSE B 68 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 2(C5 H11 N O2 SE)
FORMUL 3 HOH *107(H2 O)
HELIX 1 AA1 ASN A 63 GLY A 69 5 7
HELIX 2 AA2 ASN B 63 GLY B 69 5 7
SHEET 1 AA1 8 ASP A 91 VAL A 97 0
SHEET 2 AA1 8 GLY A 49 HIS A 56 -1 N GLY A 49 O VAL A 97
SHEET 3 AA1 8 GLY A 124 HIS A 128 -1 O HIS A 128 N GLY A 52
SHEET 4 AA1 8 ARG A 151 TYR A 159 -1 O ALA A 153 N ILE A 127
SHEET 5 AA1 8 VAL A 13 GLN A 18 -1 N ILE A 16 O ALA A 158
SHEET 6 AA1 8 GLY A 26 LEU A 33 -1 O PHE A 30 N ALA A 15
SHEET 7 AA1 8 CYS A 36 LEU A 43 -1 O GLU A 38 N THR A 31
SHEET 8 AA1 8 ILE A 106 VAL A 109 -1 O ILE A 107 N ILE A 39
SHEET 1 AA2 8 ASN B 94 VAL B 97 0
SHEET 2 AA2 8 GLY B 49 HIS B 56 -1 N GLY B 49 O VAL B 97
SHEET 3 AA2 8 GLY B 124 HIS B 128 -1 O VAL B 126 N HIS B 54
SHEET 4 AA2 8 ARG B 151 TYR B 159 -1 O ALA B 153 N ILE B 127
SHEET 5 AA2 8 VAL B 13 GLN B 18 -1 N ILE B 16 O ALA B 158
SHEET 6 AA2 8 GLY B 26 LEU B 33 -1 O PHE B 30 N ALA B 15
SHEET 7 AA2 8 CYS B 36 LEU B 43 -1 O GLN B 40 N ILE B 29
SHEET 8 AA2 8 ILE B 106 VAL B 109 -1 O VAL B 109 N THR B 37
SSBOND 1 CYS A 36 CYS A 108 1555 1555 2.01
SSBOND 2 CYS A 65 CYS A 154 1555 1555 2.08
SSBOND 3 CYS B 36 CYS B 108 1555 1555 2.04
SSBOND 4 CYS B 65 CYS B 154 1555 1555 2.07
LINK C SER A 67 N MSE A 68 1555 1555 1.34
LINK C MSE A 68 N GLY A 69 1555 1555 1.33
LINK C SER B 67 N MSE B 68 1555 1555 1.33
LINK C MSE B 68 N GLY B 69 1555 1555 1.33
CISPEP 1 PHE A 10 ASN A 11 0 -8.34
CISPEP 2 LYS A 21 PRO A 22 0 -3.41
CISPEP 3 LYS B 21 PRO B 22 0 -1.18
CRYST1 70.626 70.626 117.426 90.00 90.00 90.00 P 43 21 2 16
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 0.014159 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014159 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008516 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
