HEADER VIRAL PROTEIN 28-AUG-12 4GSX
TITLE HIGH RESOLUTION STRUCTURE OF DENGUE VIRUS SEROTYPE 1 SE CONTAINING
TITLE 2 STEM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENVELOPE PROTEIN E;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 281-691;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DENGUE VIRUS 1;
SOURCE 3 ORGANISM_COMMON: DENV-1;
SOURCE 4 ORGANISM_TAXID: 11059;
SOURCE 5 STRAIN: WP74;
SOURCE 6 GENE: ENVELOPE PROTEIN;
SOURCE 7 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 8 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: HI5;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PFASTBAC
KEYWDS VIRAL FUSION PROTEIN, VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.E.KLEIN,J.L.CHOI,S.C.HARRISON
REVDAT 6 13-SEP-23 4GSX 1 HETSYN
REVDAT 5 29-JUL-20 4GSX 1 COMPND REMARK SEQADV HETNAM
REVDAT 5 2 1 LINK SITE
REVDAT 4 15-NOV-17 4GSX 1 REMARK
REVDAT 3 06-FEB-13 4GSX 1 JRNL
REVDAT 2 30-JAN-13 4GSX 1 LINK MODRES REMARK
REVDAT 1 19-DEC-12 4GSX 0
JRNL AUTH D.E.KLEIN,J.L.CHOI,S.C.HARRISON
JRNL TITL STRUCTURE OF A DENGUE VIRUS ENVELOPE PROTEIN LATE-STAGE
JRNL TITL 2 FUSION INTERMEDIATE.
JRNL REF J.VIROL. V. 87 2287 2013
JRNL REFN ISSN 0022-538X
JRNL PMID 23236058
JRNL DOI 10.1128/JVI.02957-12
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.400
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 76852
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) : 0.161
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 3879
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 26.1827 - 5.1529 0.91 3559 216 0.1748 0.1986
REMARK 3 2 5.1529 - 4.0951 0.94 3645 184 0.1213 0.1660
REMARK 3 3 4.0951 - 3.5789 0.94 3672 210 0.1313 0.1556
REMARK 3 4 3.5789 - 3.2523 0.95 3658 191 0.1453 0.1688
REMARK 3 5 3.2523 - 3.0196 0.95 3711 191 0.1532 0.1875
REMARK 3 6 3.0196 - 2.8418 0.95 3687 187 0.1660 0.1908
REMARK 3 7 2.8418 - 2.6996 0.95 3685 208 0.1702 0.2073
REMARK 3 8 2.6996 - 2.5822 0.95 3654 181 0.1823 0.1884
REMARK 3 9 2.5822 - 2.4829 0.94 3667 209 0.1763 0.2060
REMARK 3 10 2.4829 - 2.3973 0.95 3687 202 0.1827 0.2119
REMARK 3 11 2.3973 - 2.3224 0.95 3691 187 0.1867 0.1817
REMARK 3 12 2.3224 - 2.2560 0.95 3677 190 0.1850 0.1872
REMARK 3 13 2.2560 - 2.1966 0.94 3670 209 0.1820 0.2103
REMARK 3 14 2.1966 - 2.1431 0.95 3648 187 0.1889 0.2077
REMARK 3 15 2.1431 - 2.0944 0.94 3611 198 0.1881 0.2026
REMARK 3 16 2.0944 - 2.0498 0.94 3664 190 0.1986 0.2242
REMARK 3 17 2.0498 - 2.0088 0.94 3640 174 0.1964 0.2150
REMARK 3 18 2.0088 - 1.9709 0.94 3634 190 0.2122 0.2328
REMARK 3 19 1.9709 - 1.9358 0.94 3594 180 0.2232 0.2026
REMARK 3 20 1.9358 - 1.9030 0.91 3534 173 0.2462 0.2674
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.800
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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: 0.4000
REMARK 3 OPERATOR: H,-H-K,-L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.012 6133
REMARK 3 ANGLE : 1.295 8291
REMARK 3 CHIRALITY : 0.067 992
REMARK 3 PLANARITY : 0.005 1039
REMARK 3 DIHEDRAL : 17.085 2245
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 4GSX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-SEP-12.
REMARK 100 THE DEPOSITION ID IS D_1000074592.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : .979
REMARK 200 MONOCHROMATOR : CRYOGENICALLY-COOLED SINGLE
REMARK 200 CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76924
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.44500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.840
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MR PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3G7T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -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 146.25900
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 146.25900
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 146.25900
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 38.78550
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -67.17846
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 77.57100
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 48770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 BIOMT1 2 -0.500000 -0.866025 0.000000 -38.78550
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -67.17846
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 38.78550
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 -67.17846
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 691 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 933 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 813 LIES ON A SPECIAL POSITION.
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 -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 GLY A -6
REMARK 465 SER A -5
REMARK 465 SER A -4
REMARK 465 THR A -3
REMARK 465 SER A -2
REMARK 465 ASN A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 ASP A 147
REMARK 465 GLN A 148
REMARK 465 HIS A 149
REMARK 465 GLN A 150
REMARK 465 VAL A 151
REMARK 465 GLY A 152
REMARK 465 ASN A 153
REMARK 465 GLU A 154
REMARK 465 THR A 155
REMARK 465 THR A 156
REMARK 465 GLU A 157
REMARK 465 HIS A 158
REMARK 465 ALA A 404
REMARK 465 THR A 405
REMARK 465 ALA A 406
REMARK 465 ARG A 407
REMARK 465 GLY A 408
REMARK 465 ALA A 409
REMARK 465 ARG A 410
REMARK 465 ARG A 411
REMARK 465 GLY B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 GLY B -6
REMARK 465 SER B -5
REMARK 465 SER B -4
REMARK 465 THR B -3
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 HIS B 101
REMARK 465 GLY B 146
REMARK 465 ASP B 147
REMARK 465 GLN B 148
REMARK 465 HIS B 149
REMARK 465 GLN B 150
REMARK 465 VAL B 151
REMARK 465 GLY B 152
REMARK 465 ASN B 153
REMARK 465 GLU B 154
REMARK 465 THR B 155
REMARK 465 THR B 156
REMARK 465 GLU B 157
REMARK 465 THR B 405
REMARK 465 ALA B 406
REMARK 465 ARG B 407
REMARK 465 GLY B 408
REMARK 465 ALA B 409
REMARK 465 ARG B 410
REMARK 465 ARG B 411
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 GLU B 84 CG CD OE1 OE2
REMARK 470 HIS B 244 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 246 CG CD CE NZ
REMARK 470 LYS B 247 CG CD CE NZ
REMARK 470 LYS B 343 CG CD CE NZ
REMARK 470 GLU B 362 CG CD OE1 OE2
REMARK 470 LYS B 385 CG CD CE NZ
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 774 O HOH B 848 1.81
REMARK 500 O HOH B 849 O HOH B 857 1.81
REMARK 500 NZ LYS A 284 O HOH A 831 1.85
REMARK 500 O HOH A 858 O HOH A 903 1.85
REMARK 500 OE2 GLU B 49 O HOH B 798 1.86
REMARK 500 OE2 GLU A 309 O HOH A 948 1.87
REMARK 500 O GLY B 104 O HOH B 901 1.87
REMARK 500 O HOH B 700 O HOH B 835 1.88
REMARK 500 OD1 ASP A 71 O HOH A 793 1.90
REMARK 500 O HOH B 872 O HOH B 891 1.90
REMARK 500 O HOH B 632 O HOH B 854 1.95
REMARK 500 O HOH B 870 O HOH B 887 1.96
REMARK 500 O HOH B 821 O HOH B 845 1.97
REMARK 500 OG SER B 29 O HOH B 823 1.97
REMARK 500 O HOH B 744 O HOH B 871 1.98
REMARK 500 O HIS B 158 O HOH B 786 1.98
REMARK 500 O GLY B 328 NZ LYS B 361 1.98
REMARK 500 O HOH A 922 O HOH A 949 1.99
REMARK 500 O HOH B 787 O HOH B 861 2.00
REMARK 500 O SER B 227 O HOH B 834 2.03
REMARK 500 O LEU B 236 O HOH B 797 2.03
REMARK 500 O HOH A 799 O HOH A 901 2.04
REMARK 500 O HOH A 934 O HOH A 943 2.04
REMARK 500 O GLY B 254 NE2 GLN B 256 2.04
REMARK 500 OE2 GLU A 79 O HOH A 908 2.05
REMARK 500 O HOH B 794 O HOH B 895 2.05
REMARK 500 O HOH B 874 O HOH B 885 2.05
REMARK 500 OG1 THR A 69 O HOH A 935 2.05
REMARK 500 O THR A 329 O HOH A 912 2.06
REMARK 500 O HOH B 642 O HOH B 744 2.08
REMARK 500 OE1 GLU A 314 O HOH A 945 2.09
REMARK 500 O HOH A 855 O HOH A 881 2.10
REMARK 500 O HOH A 658 O HOH A 953 2.10
REMARK 500 O LYS B 246 O HOH B 814 2.10
REMARK 500 OG1 THR A 142 O HOH A 864 2.11
REMARK 500 OE2 GLU B 229 O HOH B 803 2.11
REMARK 500 O HOH B 790 O HOH B 816 2.11
REMARK 500 O HOH B 884 O HOH B 889 2.12
REMARK 500 O HOH B 858 O HOH B 863 2.12
REMARK 500 O HOH A 886 O HOH A 897 2.13
REMARK 500 O HOH A 816 O HOH A 936 2.14
REMARK 500 OD1 ASP B 87 O HOH B 880 2.16
REMARK 500 NZ LYS A 36 OG1 THR A 293 2.16
REMARK 500 OE1 GLU A 269 O HOH A 844 2.17
REMARK 500 O HOH A 866 O HOH A 882 2.17
REMARK 500 OE1 GLN A 347 O HOH A 938 2.17
REMARK 500 O HOH A 885 O HOH A 952 2.18
REMARK 500 OE1 GLU A 314 O HOH A 951 2.19
REMARK 500 O HOH A 756 O HOH A 862 2.19
REMARK 500 OE1 GLU A 79 O HOH A 934 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 A 919 O HOH A 928 3655 1.83
REMARK 500 O HOH A 942 O HOH B 901 3545 1.83
REMARK 500 O HOH B 662 O HOH B 662 2445 1.84
REMARK 500 O HOH B 678 O HOH B 678 2445 2.01
REMARK 500 O HOH A 811 O HOH B 754 3545 2.03
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 LYS A 36 99.46 -53.03
REMARK 500 ASP A 177 -36.79 73.77
REMARK 500 GLU A 202 -113.56 56.59
REMARK 500 LYS A 343 61.67 -111.72
REMARK 500 ASN A 355 72.28 -111.59
REMARK 500 HIS B 27 128.60 -36.97
REMARK 500 THR B 76 -12.42 104.62
REMARK 500 GLN B 77 30.02 -99.28
REMARK 500 THR B 95 -177.01 179.98
REMARK 500 ASN B 103 53.75 23.35
REMARK 500 ALA B 168 77.88 -118.24
REMARK 500 ASP B 177 -27.08 72.87
REMARK 500 GLU B 202 -113.61 53.47
REMARK 500 SER B 227 -79.67 -57.74
REMARK 500 LYS B 291 99.53 -48.84
REMARK 500 ASN B 355 73.02 -103.92
REMARK 500 ASP B 360 118.03 -160.67
REMARK 500 GLU B 362 -16.87 70.49
REMARK 500 GLU B 384 -7.29 -56.58
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 ALA B 18 THR B 19 149.87
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 CD A 503 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 10 OD1
REMARK 620 2 ASP A 10 OD2 50.8
REMARK 620 3 HOH A 623 O 106.8 157.6
REMARK 620 4 HOH A 932 O 88.7 93.6 85.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 502 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 98 OD2
REMARK 620 2 HOH A 710 O 106.6
REMARK 620 3 GLU B 311 OE1 149.3 100.7
REMARK 620 4 GLU B 311 OE2 96.6 153.2 53.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B 502 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 10 OD1
REMARK 620 2 ASP B 10 OD2 49.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B 503 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 27 NE2
REMARK 620 2 HIS B 282 NE2 96.8
REMARK 620 3 HOH B 789 O 107.5 108.5
REMARK 620 N 1 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3G7T RELATED DB: PDB
REMARK 900 RELATED ID: 1OK8 RELATED DB: PDB
REMARK 900 RELATED ID: 1URZ RELATED DB: PDB
REMARK 900 RELATED ID: 4GT0 RELATED DB: PDB
DBREF 4GSX A 1 411 UNP P17763 POLG_DEN1W 281 691
DBREF 4GSX B 1 411 UNP P17763 POLG_DEN1W 281 691
SEQADV 4GSX GLY A -15 UNP P17763 EXPRESSION TAG
SEQADV 4GSX HIS A -14 UNP P17763 EXPRESSION TAG
SEQADV 4GSX HIS A -13 UNP P17763 EXPRESSION TAG
SEQADV 4GSX HIS A -12 UNP P17763 EXPRESSION TAG
SEQADV 4GSX HIS A -11 UNP P17763 EXPRESSION TAG
SEQADV 4GSX HIS A -10 UNP P17763 EXPRESSION TAG
SEQADV 4GSX HIS A -9 UNP P17763 EXPRESSION TAG
SEQADV 4GSX HIS A -8 UNP P17763 EXPRESSION TAG
SEQADV 4GSX HIS A -7 UNP P17763 EXPRESSION TAG
SEQADV 4GSX GLY A -6 UNP P17763 EXPRESSION TAG
SEQADV 4GSX SER A -5 UNP P17763 EXPRESSION TAG
SEQADV 4GSX SER A -4 UNP P17763 EXPRESSION TAG
SEQADV 4GSX THR A -3 UNP P17763 EXPRESSION TAG
SEQADV 4GSX SER A -2 UNP P17763 EXPRESSION TAG
SEQADV 4GSX ASN A -1 UNP P17763 EXPRESSION TAG
SEQADV 4GSX GLY A 0 UNP P17763 EXPRESSION TAG
SEQADV 4GSX HIS A 101 UNP P17763 TRP 381 ENGINEERED MUTATION
SEQADV 4GSX ILE A 161 UNP P17763 THR 441 CONFLICT
SEQADV 4GSX GLY B -15 UNP P17763 EXPRESSION TAG
SEQADV 4GSX HIS B -14 UNP P17763 EXPRESSION TAG
SEQADV 4GSX HIS B -13 UNP P17763 EXPRESSION TAG
SEQADV 4GSX HIS B -12 UNP P17763 EXPRESSION TAG
SEQADV 4GSX HIS B -11 UNP P17763 EXPRESSION TAG
SEQADV 4GSX HIS B -10 UNP P17763 EXPRESSION TAG
SEQADV 4GSX HIS B -9 UNP P17763 EXPRESSION TAG
SEQADV 4GSX HIS B -8 UNP P17763 EXPRESSION TAG
SEQADV 4GSX HIS B -7 UNP P17763 EXPRESSION TAG
SEQADV 4GSX GLY B -6 UNP P17763 EXPRESSION TAG
SEQADV 4GSX SER B -5 UNP P17763 EXPRESSION TAG
SEQADV 4GSX SER B -4 UNP P17763 EXPRESSION TAG
SEQADV 4GSX THR B -3 UNP P17763 EXPRESSION TAG
SEQADV 4GSX SER B -2 UNP P17763 EXPRESSION TAG
SEQADV 4GSX ASN B -1 UNP P17763 EXPRESSION TAG
SEQADV 4GSX GLY B 0 UNP P17763 EXPRESSION TAG
SEQADV 4GSX HIS B 101 UNP P17763 TRP 381 ENGINEERED MUTATION
SEQADV 4GSX ILE B 161 UNP P17763 THR 441 CONFLICT
SEQRES 1 A 427 GLY HIS HIS HIS HIS HIS HIS HIS HIS GLY SER SER THR
SEQRES 2 A 427 SER ASN GLY MET ARG CYS VAL GLY ILE GLY ASN ARG ASP
SEQRES 3 A 427 PHE VAL GLU GLY LEU SER GLY ALA THR TRP VAL ASP VAL
SEQRES 4 A 427 VAL LEU GLU HIS GLY SER CYS VAL THR THR MET ALA LYS
SEQRES 5 A 427 ASP LYS PRO THR LEU ASP ILE GLU LEU LEU LYS THR GLU
SEQRES 6 A 427 VAL THR ASN PRO ALA VAL LEU ARG LYS LEU CYS ILE GLU
SEQRES 7 A 427 ALA LYS ILE SER ASN THR THR THR ASP SER ARG CYS PRO
SEQRES 8 A 427 THR GLN GLY GLU ALA THR LEU VAL GLU GLU GLN ASP THR
SEQRES 9 A 427 ASN PHE VAL CYS ARG ARG THR PHE VAL ASP ARG GLY HIS
SEQRES 10 A 427 GLY ASN GLY CYS GLY LEU PHE GLY LYS GLY SER LEU ILE
SEQRES 11 A 427 THR CYS ALA LYS PHE LYS CYS VAL THR LYS LEU GLU GLY
SEQRES 12 A 427 LYS ILE VAL GLN TYR GLU ASN LEU LYS TYR SER VAL ILE
SEQRES 13 A 427 VAL THR VAL HIS THR GLY ASP GLN HIS GLN VAL GLY ASN
SEQRES 14 A 427 GLU THR THR GLU HIS GLY THR ILE ALA THR ILE THR PRO
SEQRES 15 A 427 GLN ALA PRO THR SER GLU ILE GLN LEU THR ASP TYR GLY
SEQRES 16 A 427 ALA LEU THR LEU ASP CYS SER PRO ARG THR GLY LEU ASP
SEQRES 17 A 427 PHE ASN GLU MET VAL LEU LEU THR MET GLU LYS LYS SER
SEQRES 18 A 427 TRP LEU VAL HIS LYS GLN TRP PHE LEU ASP LEU PRO LEU
SEQRES 19 A 427 PRO TRP THR SER GLY ALA SER THR SER GLN GLU THR TRP
SEQRES 20 A 427 ASN ARG GLN ASP LEU LEU VAL THR PHE LYS THR ALA HIS
SEQRES 21 A 427 ALA LYS LYS GLN GLU VAL VAL VAL LEU GLY SER GLN GLU
SEQRES 22 A 427 GLY ALA MET HIS THR ALA LEU THR GLY ALA THR GLU ILE
SEQRES 23 A 427 GLN THR SER GLY THR THR THR ILE PHE ALA GLY HIS LEU
SEQRES 24 A 427 LYS CYS ARG LEU LYS MET ASP LYS LEU THR LEU LYS GLY
SEQRES 25 A 427 MET SER TYR VAL MET CYS THR GLY SER PHE LYS LEU GLU
SEQRES 26 A 427 LYS GLU VAL ALA GLU THR GLN HIS GLY THR VAL LEU VAL
SEQRES 27 A 427 GLN VAL LYS TYR GLU GLY THR ASP ALA PRO CYS LYS ILE
SEQRES 28 A 427 PRO PHE SER SER GLN ASP GLU LYS GLY VAL THR GLN ASN
SEQRES 29 A 427 GLY ARG LEU ILE THR ALA ASN PRO ILE VAL THR ASP LYS
SEQRES 30 A 427 GLU LYS PRO VAL ASN ILE GLU ALA GLU PRO PRO PHE GLY
SEQRES 31 A 427 GLU SER TYR ILE VAL VAL GLY ALA GLY GLU LYS ALA LEU
SEQRES 32 A 427 LYS LEU SER TRP PHE LYS LYS GLY SER SER ILE GLY LYS
SEQRES 33 A 427 MET PHE GLU ALA THR ALA ARG GLY ALA ARG ARG
SEQRES 1 B 427 GLY HIS HIS HIS HIS HIS HIS HIS HIS GLY SER SER THR
SEQRES 2 B 427 SER ASN GLY MET ARG CYS VAL GLY ILE GLY ASN ARG ASP
SEQRES 3 B 427 PHE VAL GLU GLY LEU SER GLY ALA THR TRP VAL ASP VAL
SEQRES 4 B 427 VAL LEU GLU HIS GLY SER CYS VAL THR THR MET ALA LYS
SEQRES 5 B 427 ASP LYS PRO THR LEU ASP ILE GLU LEU LEU LYS THR GLU
SEQRES 6 B 427 VAL THR ASN PRO ALA VAL LEU ARG LYS LEU CYS ILE GLU
SEQRES 7 B 427 ALA LYS ILE SER ASN THR THR THR ASP SER ARG CYS PRO
SEQRES 8 B 427 THR GLN GLY GLU ALA THR LEU VAL GLU GLU GLN ASP THR
SEQRES 9 B 427 ASN PHE VAL CYS ARG ARG THR PHE VAL ASP ARG GLY HIS
SEQRES 10 B 427 GLY ASN GLY CYS GLY LEU PHE GLY LYS GLY SER LEU ILE
SEQRES 11 B 427 THR CYS ALA LYS PHE LYS CYS VAL THR LYS LEU GLU GLY
SEQRES 12 B 427 LYS ILE VAL GLN TYR GLU ASN LEU LYS TYR SER VAL ILE
SEQRES 13 B 427 VAL THR VAL HIS THR GLY ASP GLN HIS GLN VAL GLY ASN
SEQRES 14 B 427 GLU THR THR GLU HIS GLY THR ILE ALA THR ILE THR PRO
SEQRES 15 B 427 GLN ALA PRO THR SER GLU ILE GLN LEU THR ASP TYR GLY
SEQRES 16 B 427 ALA LEU THR LEU ASP CYS SER PRO ARG THR GLY LEU ASP
SEQRES 17 B 427 PHE ASN GLU MET VAL LEU LEU THR MET GLU LYS LYS SER
SEQRES 18 B 427 TRP LEU VAL HIS LYS GLN TRP PHE LEU ASP LEU PRO LEU
SEQRES 19 B 427 PRO TRP THR SER GLY ALA SER THR SER GLN GLU THR TRP
SEQRES 20 B 427 ASN ARG GLN ASP LEU LEU VAL THR PHE LYS THR ALA HIS
SEQRES 21 B 427 ALA LYS LYS GLN GLU VAL VAL VAL LEU GLY SER GLN GLU
SEQRES 22 B 427 GLY ALA MET HIS THR ALA LEU THR GLY ALA THR GLU ILE
SEQRES 23 B 427 GLN THR SER GLY THR THR THR ILE PHE ALA GLY HIS LEU
SEQRES 24 B 427 LYS CYS ARG LEU LYS MET ASP LYS LEU THR LEU LYS GLY
SEQRES 25 B 427 MET SER TYR VAL MET CYS THR GLY SER PHE LYS LEU GLU
SEQRES 26 B 427 LYS GLU VAL ALA GLU THR GLN HIS GLY THR VAL LEU VAL
SEQRES 27 B 427 GLN VAL LYS TYR GLU GLY THR ASP ALA PRO CYS LYS ILE
SEQRES 28 B 427 PRO PHE SER SER GLN ASP GLU LYS GLY VAL THR GLN ASN
SEQRES 29 B 427 GLY ARG LEU ILE THR ALA ASN PRO ILE VAL THR ASP LYS
SEQRES 30 B 427 GLU LYS PRO VAL ASN ILE GLU ALA GLU PRO PRO PHE GLY
SEQRES 31 B 427 GLU SER TYR ILE VAL VAL GLY ALA GLY GLU LYS ALA LEU
SEQRES 32 B 427 LYS LEU SER TRP PHE LYS LYS GLY SER SER ILE GLY LYS
SEQRES 33 B 427 MET PHE GLU ALA THR ALA ARG GLY ALA ARG ARG
MODRES 4GSX ASN A 67 ASN GLYCOSYLATION SITE
MODRES 4GSX ASN B 67 ASN GLYCOSYLATION SITE
HET NAG A 501 14
HET CD A 502 1
HET CD A 503 1
HET CL A 504 1
HET NAG B 501 14
HET CD B 502 1
HET CD B 503 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM CD CADMIUM ION
HETNAM CL CHLORIDE ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 4 CD 4(CD 2+)
FORMUL 6 CL CL 1-
FORMUL 10 HOH *666(H2 O)
HELIX 1 1 GLY A 7 ARG A 9 5 3
HELIX 2 2 LEU A 82 ASP A 87 5 6
HELIX 3 3 GLY A 100 GLY A 104 5 5
HELIX 4 4 GLN A 131 GLU A 133 5 3
HELIX 5 5 LYS A 210 ASP A 215 1 6
HELIX 6 6 ARG A 233 LEU A 236 5 4
HELIX 7 7 GLN A 256 LEU A 264 1 9
HELIX 8 8 ALA A 382 ALA A 386 5 5
HELIX 9 9 GLY B 7 ARG B 9 5 3
HELIX 10 10 LEU B 82 GLN B 86 5 5
HELIX 11 11 GLN B 131 GLU B 133 5 3
HELIX 12 12 LYS B 210 ASP B 215 1 6
HELIX 13 13 ARG B 233 LEU B 236 5 4
HELIX 14 14 GLN B 256 THR B 265 1 10
SHEET 1 A10 VAL A 4 GLY A 5 0
SHEET 2 A10 VAL A 31 THR A 33 1 O THR A 32 N VAL A 4
SHEET 3 A10 LEU A 41 THR A 51 -1 O LEU A 41 N THR A 33
SHEET 4 A10 THR A 276 PHE A 279 -1 O THR A 277 N VAL A 50
SHEET 5 A10 THR A 268 SER A 273 -1 N GLN A 271 O ILE A 278
SHEET 6 A10 LYS A 204 HIS A 209 -1 N LEU A 207 O THR A 268
SHEET 7 A10 MET A 196 MET A 201 -1 N VAL A 197 O VAL A 208
SHEET 8 A10 GLY A 109 ILE A 129 -1 N LYS A 128 O LEU A 198
SHEET 9 A10 LEU A 135 VAL A 143 0
SHEET 10 A10 THR A 160 ILE A 164 -1 O ALA A 162 N VAL A 139
SHEET 1 B 9 PHE A 90 ARG A 99 0
SHEET 2 B 9 GLY A 109 ILE A 129 -1 O GLY A 111 N VAL A 97
SHEET 3 B 9 MET A 196 MET A 201 -1 O LEU A 198 N LYS A 128
SHEET 4 B 9 LYS A 204 HIS A 209 -1 O VAL A 208 N VAL A 197
SHEET 5 B 9 THR A 268 SER A 273 -1 O THR A 268 N LEU A 207
SHEET 6 B 9 THR A 276 PHE A 279 -1 O ILE A 278 N GLN A 271
SHEET 7 B 9 LEU A 41 THR A 51 -1 N VAL A 50 O THR A 277
SHEET 8 B 9 ALA A 54 SER A 72 0
SHEET 9 B 9 TRP A 220 SER A 222 -1 O THR A 221 N LYS A 58
SHEET 1 C 5 PHE A 11 GLU A 13 0
SHEET 2 C 5 ALA A 18 GLU A 26 -1 O TRP A 20 N VAL A 12
SHEET 3 C 5 HIS A 282 ASP A 290 -1 O CYS A 285 N VAL A 23
SHEET 4 C 5 GLY A 179 PRO A 187 -1 N ASP A 184 O ARG A 286
SHEET 5 C 5 THR A 170 LEU A 175 -1 N SER A 171 O LEU A 183
SHEET 1 D 2 VAL A 238 PHE A 240 0
SHEET 2 D 2 VAL A 250 VAL A 252 -1 O VAL A 251 N THR A 239
SHEET 1 E 3 PHE A 306 LEU A 308 0
SHEET 2 E 3 VAL A 320 TYR A 326 -1 O LYS A 325 N LYS A 307
SHEET 3 E 3 ALA A 313 GLU A 314 -1 N ALA A 313 O LEU A 321
SHEET 1 F 3 PHE A 306 LEU A 308 0
SHEET 2 F 3 VAL A 320 TYR A 326 -1 O LYS A 325 N LYS A 307
SHEET 3 F 3 VAL A 365 ALA A 369 -1 O ILE A 367 N VAL A 322
SHEET 1 G 2 CYS A 333 LYS A 334 0
SHEET 2 G 2 ILE A 357 VAL A 358 -1 O VAL A 358 N CYS A 333
SHEET 1 H 3 PHE A 337 ASP A 341 0
SHEET 2 H 3 GLY A 374 VAL A 380 -1 O TYR A 377 N GLN A 340
SHEET 3 H 3 LEU A 387 LYS A 393 -1 O LYS A 393 N GLY A 374
SHEET 1 I 5 CYS B 3 GLY B 5 0
SHEET 2 I 5 CYS B 30 MET B 34 1 O THR B 32 N VAL B 4
SHEET 3 I 5 THR B 40 THR B 51 -1 O LEU B 41 N THR B 33
SHEET 4 I 5 LEU B 135 VAL B 143 -1 O ILE B 140 N GLU B 44
SHEET 5 I 5 THR B 160 ILE B 164 -1 O ILE B 164 N TYR B 137
SHEET 1 J 5 CYS B 3 GLY B 5 0
SHEET 2 J 5 CYS B 30 MET B 34 1 O THR B 32 N VAL B 4
SHEET 3 J 5 THR B 40 THR B 51 -1 O LEU B 41 N THR B 33
SHEET 4 J 5 THR B 276 PHE B 279 -1 O THR B 277 N VAL B 50
SHEET 5 J 5 THR B 272 SER B 273 -1 N SER B 273 O THR B 276
SHEET 1 K 5 PHE B 11 GLU B 13 0
SHEET 2 K 5 ALA B 18 GLU B 26 -1 O TRP B 20 N VAL B 12
SHEET 3 K 5 HIS B 282 ASP B 290 -1 O CYS B 285 N VAL B 23
SHEET 4 K 5 GLY B 179 PRO B 187 -1 N ASP B 184 O ARG B 286
SHEET 5 K 5 THR B 170 LEU B 175 -1 N LEU B 175 O GLY B 179
SHEET 1 L 4 PHE B 90 ASP B 98 0
SHEET 2 L 4 LYS B 110 ILE B 129 -1 O GLY B 111 N VAL B 97
SHEET 3 L 4 ALA B 54 SER B 72 -1 N SER B 66 O LYS B 118
SHEET 4 L 4 TRP B 220 SER B 222 -1 O THR B 221 N LYS B 58
SHEET 1 M 5 PHE B 90 ASP B 98 0
SHEET 2 M 5 LYS B 110 ILE B 129 -1 O GLY B 111 N VAL B 97
SHEET 3 M 5 MET B 196 MET B 201 -1 O LEU B 198 N LYS B 128
SHEET 4 M 5 LYS B 204 HIS B 209 -1 O VAL B 208 N VAL B 197
SHEET 5 M 5 GLU B 269 ILE B 270 -1 O ILE B 270 N SER B 205
SHEET 1 N 2 VAL B 238 PHE B 240 0
SHEET 2 N 2 VAL B 250 VAL B 252 -1 O VAL B 251 N THR B 239
SHEET 1 O 3 PHE B 306 LEU B 308 0
SHEET 2 O 3 VAL B 320 TYR B 326 -1 O LYS B 325 N LYS B 307
SHEET 3 O 3 ALA B 313 GLU B 314 -1 N ALA B 313 O LEU B 321
SHEET 1 P 3 PHE B 306 LEU B 308 0
SHEET 2 P 3 VAL B 320 TYR B 326 -1 O LYS B 325 N LYS B 307
SHEET 3 P 3 VAL B 365 ALA B 369 -1 O ILE B 367 N VAL B 322
SHEET 1 Q 2 CYS B 333 LYS B 334 0
SHEET 2 Q 2 ILE B 357 VAL B 358 -1 O VAL B 358 N CYS B 333
SHEET 1 R 3 PHE B 337 ASP B 341 0
SHEET 2 R 3 GLY B 374 VAL B 380 -1 O TYR B 377 N GLN B 340
SHEET 3 R 3 LEU B 387 LYS B 393 -1 O LEU B 389 N ILE B 378
SSBOND 1 CYS A 3 CYS A 30 1555 1555 2.03
SSBOND 2 CYS A 60 CYS A 121 1555 1555 2.06
SSBOND 3 CYS A 74 CYS A 105 1555 1555 2.04
SSBOND 4 CYS A 92 CYS A 116 1555 1555 2.04
SSBOND 5 CYS A 185 CYS A 285 1555 1555 2.04
SSBOND 6 CYS A 302 CYS A 333 1555 1555 2.05
SSBOND 7 CYS B 3 CYS B 30 1555 1555 2.04
SSBOND 8 CYS B 60 CYS B 121 1555 1555 2.06
SSBOND 9 CYS B 74 CYS B 105 1555 1555 2.03
SSBOND 10 CYS B 92 CYS B 116 1555 1555 2.03
SSBOND 11 CYS B 185 CYS B 285 1555 1555 2.01
SSBOND 12 CYS B 302 CYS B 333 1555 1555 2.05
LINK ND2 ASN A 67 C1 NAG A 501 1555 1555 1.84
LINK ND2 ASN B 67 C1 NAG B 501 1555 1555 1.80
LINK OD1 ASP A 10 CD CD A 503 1555 1555 2.52
LINK OD2 ASP A 10 CD CD A 503 1555 1555 2.57
LINK OD2 ASP A 98 CD CD A 502 1555 1555 2.46
LINK CD CD A 502 O HOH A 710 1555 1555 2.67
LINK CD CD A 502 OE1 GLU B 311 1555 1555 2.43
LINK CD CD A 502 OE2 GLU B 311 1555 1555 2.45
LINK CD CD A 503 O HOH A 623 1555 1555 2.60
LINK CD CD A 503 O HOH A 932 1555 1555 2.62
LINK OD1 ASP B 10 CD CD B 502 1555 1555 2.52
LINK OD2 ASP B 10 CD CD B 502 1555 1555 2.65
LINK NE2 HIS B 27 CD CD B 503 1555 1555 2.48
LINK NE2 HIS B 282 CD CD B 503 1555 1555 2.42
LINK CD CD B 503 O HOH B 789 1555 1555 2.39
CISPEP 1 ALA A 331 PRO A 332 0 5.05
CISPEP 2 ALA B 331 PRO B 332 0 8.13
CRYST1 77.571 77.571 292.518 90.00 90.00 120.00 P 63 12
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 0.012891 0.007443 0.000000 0.00000
SCALE2 0.000000 0.014886 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003419 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
