HEADER GENE REGULATION/RNA 02-APR-15 4Z4D
TITLE HUMAN ARGONAUTE2 BOUND TO T1-G TARGET RNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN ARGONAUTE-2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HAGO2,ARGONAUTE RISC CATALYTIC COMPONENT 2,EUKARYOTIC
COMPND 5 TRANSLATION INITIATION FACTOR 2C 2,EIF2C 2,PAZ PIWI DOMAIN PROTEIN,
COMPND 6 PPD,PROTEIN SLICER;
COMPND 7 EC: 3.1.26.-;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: RNA (5'-
COMPND 12 R(P*UP*UP*CP*AP*CP*AP*UP*UP*GP*CP*CP*CP*AP*AP*GP*UP*CP*UP*UP*U)-3');
COMPND 13 CHAIN: B;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: RNA (5'-R(*CP*AP*AP*UP*GP*UP*GP*AP*G)-3');
COMPND 17 CHAIN: D;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: AGO2, EIF2C2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF-9;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 12 ORGANISM_TAXID: 32630;
SOURCE 13 MOL_ID: 3;
SOURCE 14 SYNTHETIC: YES;
SOURCE 15 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 16 ORGANISM_TAXID: 32630
KEYWDS ARGONAUTE2, MIRNA, GENE REGULATION-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.T.SCHIRLE,I.J.MACRAE
REVDAT 4 27-SEP-23 4Z4D 1 LINK
REVDAT 3 25-DEC-19 4Z4D 1 REMARK
REVDAT 2 20-SEP-17 4Z4D 1 REMARK
REVDAT 1 23-SEP-15 4Z4D 0
JRNL AUTH N.T.SCHIRLE,J.SHEU-GRUTTADAURIA,S.D.CHANDRADOSS,C.JOO,
JRNL AUTH 2 I.J.MACRAE
JRNL TITL WATER-MEDIATED RECOGNITION OF T1-ADENOSINE ANCHORS
JRNL TITL 2 ARGONAUTE2 TO MICRORNA TARGETS.
JRNL REF ELIFE V. 4 2015
JRNL REFN ESSN 2050-084X
JRNL PMID 26359634
JRNL DOI 10.7554/ELIFE.07646
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 113733
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 5721
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 35.4089 - 4.9660 0.97 3668 210 0.1503 0.1627
REMARK 3 2 4.9660 - 3.9434 0.96 3620 188 0.1349 0.1465
REMARK 3 3 3.9434 - 3.4454 0.98 3685 197 0.1458 0.1831
REMARK 3 4 3.4454 - 3.1306 0.99 3717 181 0.1576 0.1864
REMARK 3 5 3.1306 - 2.9063 0.99 3692 182 0.1665 0.1973
REMARK 3 6 2.9063 - 2.7350 0.95 3569 169 0.1648 0.1960
REMARK 3 7 2.7350 - 2.5981 0.98 3647 187 0.1644 0.1894
REMARK 3 8 2.5981 - 2.4850 0.98 3668 175 0.1631 0.1975
REMARK 3 9 2.4850 - 2.3894 0.98 3641 188 0.1682 0.1792
REMARK 3 10 2.3894 - 2.3069 0.98 3672 186 0.1646 0.1902
REMARK 3 11 2.3069 - 2.2348 0.98 3642 196 0.1589 0.1983
REMARK 3 12 2.2348 - 2.1709 0.95 3574 190 0.1631 0.1888
REMARK 3 13 2.1709 - 2.1138 0.95 3540 197 0.1690 0.2015
REMARK 3 14 2.1138 - 2.0622 0.97 3575 194 0.1653 0.1870
REMARK 3 15 2.0622 - 2.0154 0.97 3669 208 0.1678 0.2145
REMARK 3 16 2.0154 - 1.9725 0.97 3556 211 0.1736 0.2097
REMARK 3 17 1.9725 - 1.9330 0.98 3628 194 0.1746 0.1862
REMARK 3 18 1.9330 - 1.8965 0.97 3595 203 0.1776 0.2115
REMARK 3 19 1.8965 - 1.8627 0.98 3636 179 0.1760 0.2152
REMARK 3 20 1.8627 - 1.8311 0.97 3620 186 0.1779 0.1896
REMARK 3 21 1.8311 - 1.8016 0.92 3417 177 0.1855 0.2253
REMARK 3 22 1.8016 - 1.7739 0.95 3551 185 0.1905 0.2193
REMARK 3 23 1.7739 - 1.7478 0.97 3548 200 0.1876 0.2171
REMARK 3 24 1.7478 - 1.7231 0.96 3584 202 0.1944 0.2287
REMARK 3 25 1.7231 - 1.6999 0.97 3585 179 0.1974 0.2033
REMARK 3 26 1.6999 - 1.6778 0.96 3590 213 0.2133 0.2407
REMARK 3 27 1.6778 - 1.6568 0.96 3573 186 0.2156 0.2763
REMARK 3 28 1.6568 - 1.6369 0.97 3592 195 0.2264 0.2556
REMARK 3 29 1.6369 - 1.6178 0.96 3559 177 0.2415 0.2482
REMARK 3 30 1.6178 - 1.5996 0.92 3399 186 0.2761 0.2908
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.500
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: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.014 7330
REMARK 3 ANGLE : 1.460 10062
REMARK 3 CHIRALITY : 0.077 1129
REMARK 3 PLANARITY : 0.010 1195
REMARK 3 DIHEDRAL : 13.352 2842
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 22 THROUGH 419 )
REMARK 3 ORIGIN FOR THE GROUP (A): 65.0000 -0.1452 0.9362
REMARK 3 T TENSOR
REMARK 3 T11: 0.3840 T22: 0.4788
REMARK 3 T33: 0.2290 T12: 0.0274
REMARK 3 T13: -0.0093 T23: 0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 1.5210 L22: 0.4662
REMARK 3 L33: 2.1000 L12: -0.2462
REMARK 3 L13: 0.6014 L23: -0.1227
REMARK 3 S TENSOR
REMARK 3 S11: -0.1133 S12: 0.4857 S13: 0.1938
REMARK 3 S21: -0.2141 S22: -0.0107 S23: 0.0346
REMARK 3 S31: -0.4675 S32: -0.2791 S33: 0.1258
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 420 THROUGH 859 )
REMARK 3 ORIGIN FOR THE GROUP (A): 61.3136 -19.1014 33.4385
REMARK 3 T TENSOR
REMARK 3 T11: 0.1227 T22: 0.0965
REMARK 3 T33: 0.0822 T12: 0.0219
REMARK 3 T13: 0.0019 T23: 0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 1.7852 L22: 0.8880
REMARK 3 L33: 0.5835 L12: 0.6236
REMARK 3 L13: -0.0462 L23: 0.0322
REMARK 3 S TENSOR
REMARK 3 S11: 0.0070 S12: -0.1079 S13: -0.0541
REMARK 3 S21: 0.0550 S22: -0.0052 S23: 0.0369
REMARK 3 S31: 0.0500 S32: -0.0202 S33: -0.0008
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 9 )
REMARK 3 ORIGIN FOR THE GROUP (A): 61.9295 -22.3102 19.4893
REMARK 3 T TENSOR
REMARK 3 T11: 0.1378 T22: 0.1146
REMARK 3 T33: 0.1333 T12: 0.0084
REMARK 3 T13: -0.0071 T23: -0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 4.2829 L22: 0.5540
REMARK 3 L33: 1.9621 L12: 1.0237
REMARK 3 L13: -1.7187 L23: 0.2129
REMARK 3 S TENSOR
REMARK 3 S11: 0.0064 S12: 0.3038 S13: 0.1102
REMARK 3 S21: -0.0721 S22: 0.0631 S23: 0.0560
REMARK 3 S31: -0.1546 S32: -0.1097 S33: -0.0563
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 10 THROUGH 21 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.2628 3.6525 5.1850
REMARK 3 T TENSOR
REMARK 3 T11: 0.7360 T22: 0.7298
REMARK 3 T33: 0.6192 T12: 0.0351
REMARK 3 T13: -0.1866 T23: 0.2294
REMARK 3 L TENSOR
REMARK 3 L11: 3.1381 L22: 0.7435
REMARK 3 L33: 3.7386 L12: -0.1748
REMARK 3 L13: 3.2788 L23: 0.2740
REMARK 3 S TENSOR
REMARK 3 S11: -0.4996 S12: 1.0875 S13: 0.8715
REMARK 3 S21: -0.6209 S22: -0.0957 S23: 0.4546
REMARK 3 S31: -0.8084 S32: -0.0385 S33: 0.5960
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 9 )
REMARK 3 ORIGIN FOR THE GROUP (A): 61.5675 -26.9017 16.0180
REMARK 3 T TENSOR
REMARK 3 T11: 0.2120 T22: 0.2012
REMARK 3 T33: 0.2130 T12: -0.0502
REMARK 3 T13: -0.0093 T23: -0.0547
REMARK 3 L TENSOR
REMARK 3 L11: 4.7381 L22: 5.3524
REMARK 3 L33: 5.3690 L12: -1.4216
REMARK 3 L13: -1.4479 L23: -0.4417
REMARK 3 S TENSOR
REMARK 3 S11: 0.0060 S12: 0.2154 S13: -0.3193
REMARK 3 S21: -0.2122 S22: 0.0044 S23: 0.1414
REMARK 3 S31: 0.3158 S32: 0.1692 S33: -0.0110
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 4Z4D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000208614.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JAN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97950
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 113775
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 39.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : 0.03100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 4W5O
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, TRIS, ISOPROPANOL, PHENOL,
REMARK 280 MAGNESIUM, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 58.50800
REMARK 290 SMTRY3 2 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 TYR A 2
REMARK 465 SER A 3
REMARK 465 GLY A 4
REMARK 465 ALA A 5
REMARK 465 GLY A 6
REMARK 465 PRO A 7
REMARK 465 ALA A 8
REMARK 465 LEU A 9
REMARK 465 ALA A 10
REMARK 465 PRO A 11
REMARK 465 PRO A 12
REMARK 465 ALA A 13
REMARK 465 PRO A 14
REMARK 465 PRO A 15
REMARK 465 PRO A 16
REMARK 465 PRO A 17
REMARK 465 ILE A 18
REMARK 465 GLN A 19
REMARK 465 GLY A 20
REMARK 465 TYR A 21
REMARK 465 GLY A 121
REMARK 465 GLU A 122
REMARK 465 GLY A 123
REMARK 465 LYS A 124
REMARK 465 ASP A 125
REMARK 465 ARG A 126
REMARK 465 THR A 270
REMARK 465 HIS A 271
REMARK 465 CYS A 272
REMARK 465 GLY A 273
REMARK 465 GLN A 274
REMARK 465 MET A 275
REMARK 465 LEU A 296
REMARK 465 GLN A 297
REMARK 465 GLN A 298
REMARK 465 GLU A 299
REMARK 465 SER A 300
REMARK 465 GLY A 301
REMARK 465 GLN A 302
REMARK 465 THR A 303
REMARK 465 VAL A 304
REMARK 465 HIS A 822
REMARK 465 ASP A 823
REMARK 465 SER A 824
REMARK 465 ALA A 825
REMARK 465 GLU A 826
REMARK 465 GLY A 827
REMARK 465 SER A 828
REMARK 465 HIS A 829
REMARK 465 THR A 830
REMARK 465 SER A 831
REMARK 465 GLY A 832
REMARK 465 GLN A 833
REMARK 465 SER A 834
REMARK 465 ASN A 835
REMARK 465 C B 19
REMARK 465 A D 10
REMARK 465 A D 11
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 U B 18 N1 C2 O2 N3 C4 O4 C5
REMARK 470 U B 18 C6
REMARK 470 G D 9 C5' C4' O4' C3' O3' C2' O2'
REMARK 470 G D 9 C1' N9 C8 N7 C5 C6 O6
REMARK 470 G D 9 N1 C2 N2 N3 C4
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 155 CD PRO A 155 N 0.178
REMARK 500 GLN A 708 CA GLN A 708 C 0.200
REMARK 500 U B 1 P U B 1 OP3 -0.109
REMARK 500
REMARK 500 REMARK: NULL
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 C B 5 C6 - N1 - C2 ANGL. DEV. = 2.7 DEGREES
REMARK 500 U D 4 C5 - C6 - N1 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 PHE A 23 -70.69 -140.31
REMARK 500 ASP A 30 177.75 179.04
REMARK 500 ASN A 43 49.75 -80.15
REMARK 500 LYS A 51 53.66 -110.65
REMARK 500 ARG A 97 -90.18 -124.37
REMARK 500 PRO A 107 48.40 -77.00
REMARK 500 TRP A 211 -77.77 -101.58
REMARK 500 ASN A 623 -54.60 -130.99
REMARK 500 LYS A 739 -58.22 72.42
REMARK 500 ASP A 770 84.83 -154.12
REMARK 500 MET A 856 54.64 -100.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLN A 708 18.60
REMARK 500 GLN A 708 18.46
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 A1470 DISTANCE = 6.05 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 MG A 901 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 597 OD1
REMARK 620 2 VAL A 598 O 92.6
REMARK 620 3 HOH A1017 O 86.2 178.7
REMARK 620 4 HOH A1118 O 84.9 88.2 91.5
REMARK 620 5 HOH A1286 O 87.1 89.8 90.3 171.7
REMARK 620 6 HOH B 227 O 175.7 91.6 89.6 94.1 94.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 101 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A B 13 OP2
REMARK 620 2 HOH B 218 O 94.3
REMARK 620 3 HOH B 219 O 93.1 94.4
REMARK 620 4 HOH B 220 O 90.6 172.3 91.3
REMARK 620 5 HOH B 222 O 177.1 88.0 88.6 86.9
REMARK 620 6 HOH B 239 O 93.7 90.8 171.1 82.9 84.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 101 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U D 4 O4
REMARK 620 2 HOH D 209 O 87.7
REMARK 620 3 HOH D 219 O 93.0 176.5
REMARK 620 4 HOH D 227 O 88.5 89.4 87.2
REMARK 620 5 HOH D 229 O 93.8 91.8 91.6 177.5
REMARK 620 6 HOH D 235 O 175.9 90.1 89.0 88.0 89.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPH A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPH A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPH A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPH A 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA A 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA A 907
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA A 908
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA B 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPA B 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4Z4C RELATED DB: PDB
REMARK 900 RELATED ID: 4Z4E RELATED DB: PDB
REMARK 900 RELATED ID: 4Z4F RELATED DB: PDB
REMARK 900 RELATED ID: 4Z4G RELATED DB: PDB
REMARK 900 RELATED ID: 4Z4H RELATED DB: PDB
REMARK 900 RELATED ID: 4Z4I RELATED DB: PDB
DBREF 4Z4D A 1 859 UNP Q9UKV8 AGO2_HUMAN 1 859
DBREF 4Z4D B 1 21 PDB 4Z4D 4Z4D 1 21
DBREF 4Z4D D 1 11 PDB 4Z4D 4Z4D 1 11
SEQADV 4Z4D ASP A 387 UNP Q9UKV8 SER 387 ENGINEERED MUTATION
SEQRES 1 A 859 MET TYR SER GLY ALA GLY PRO ALA LEU ALA PRO PRO ALA
SEQRES 2 A 859 PRO PRO PRO PRO ILE GLN GLY TYR ALA PHE LYS PRO PRO
SEQRES 3 A 859 PRO ARG PRO ASP PHE GLY THR SER GLY ARG THR ILE LYS
SEQRES 4 A 859 LEU GLN ALA ASN PHE PHE GLU MET ASP ILE PRO LYS ILE
SEQRES 5 A 859 ASP ILE TYR HIS TYR GLU LEU ASP ILE LYS PRO GLU LYS
SEQRES 6 A 859 CYS PRO ARG ARG VAL ASN ARG GLU ILE VAL GLU HIS MET
SEQRES 7 A 859 VAL GLN HIS PHE LYS THR GLN ILE PHE GLY ASP ARG LYS
SEQRES 8 A 859 PRO VAL PHE ASP GLY ARG LYS ASN LEU TYR THR ALA MET
SEQRES 9 A 859 PRO LEU PRO ILE GLY ARG ASP LYS VAL GLU LEU GLU VAL
SEQRES 10 A 859 THR LEU PRO GLY GLU GLY LYS ASP ARG ILE PHE LYS VAL
SEQRES 11 A 859 SER ILE LYS TRP VAL SER CYS VAL SER LEU GLN ALA LEU
SEQRES 12 A 859 HIS ASP ALA LEU SER GLY ARG LEU PRO SER VAL PRO PHE
SEQRES 13 A 859 GLU THR ILE GLN ALA LEU ASP VAL VAL MET ARG HIS LEU
SEQRES 14 A 859 PRO SER MET ARG TYR THR PRO VAL GLY ARG SER PHE PHE
SEQRES 15 A 859 THR ALA SER GLU GLY CYS SER ASN PRO LEU GLY GLY GLY
SEQRES 16 A 859 ARG GLU VAL TRP PHE GLY PHE HIS GLN SER VAL ARG PRO
SEQRES 17 A 859 SER LEU TRP LYS MET MET LEU ASN ILE ASP VAL SER ALA
SEQRES 18 A 859 THR ALA PHE TYR LYS ALA GLN PRO VAL ILE GLU PHE VAL
SEQRES 19 A 859 CYS GLU VAL LEU ASP PHE LYS SER ILE GLU GLU GLN GLN
SEQRES 20 A 859 LYS PRO LEU THR ASP SER GLN ARG VAL LYS PHE THR LYS
SEQRES 21 A 859 GLU ILE LYS GLY LEU LYS VAL GLU ILE THR HIS CYS GLY
SEQRES 22 A 859 GLN MET LYS ARG LYS TYR ARG VAL CYS ASN VAL THR ARG
SEQRES 23 A 859 ARG PRO ALA SER HIS GLN THR PHE PRO LEU GLN GLN GLU
SEQRES 24 A 859 SER GLY GLN THR VAL GLU CYS THR VAL ALA GLN TYR PHE
SEQRES 25 A 859 LYS ASP ARG HIS LYS LEU VAL LEU ARG TYR PRO HIS LEU
SEQRES 26 A 859 PRO CYS LEU GLN VAL GLY GLN GLU GLN LYS HIS THR TYR
SEQRES 27 A 859 LEU PRO LEU GLU VAL CYS ASN ILE VAL ALA GLY GLN ARG
SEQRES 28 A 859 CYS ILE LYS LYS LEU THR ASP ASN GLN THR SER THR MET
SEQRES 29 A 859 ILE ARG ALA THR ALA ARG SER ALA PRO ASP ARG GLN GLU
SEQRES 30 A 859 GLU ILE SER LYS LEU MET ARG SER ALA ASP PHE ASN THR
SEQRES 31 A 859 ASP PRO TYR VAL ARG GLU PHE GLY ILE MET VAL LYS ASP
SEQRES 32 A 859 GLU MET THR ASP VAL THR GLY ARG VAL LEU GLN PRO PRO
SEQRES 33 A 859 SER ILE LEU TYR GLY GLY ARG ASN LYS ALA ILE ALA THR
SEQRES 34 A 859 PRO VAL GLN GLY VAL TRP ASP MET ARG ASN LYS GLN PHE
SEQRES 35 A 859 HIS THR GLY ILE GLU ILE LYS VAL TRP ALA ILE ALA CYS
SEQRES 36 A 859 PHE ALA PRO GLN ARG GLN CYS THR GLU VAL HIS LEU LYS
SEQRES 37 A 859 SER PHE THR GLU GLN LEU ARG LYS ILE SER ARG ASP ALA
SEQRES 38 A 859 GLY MET PRO ILE GLN GLY GLN PRO CYS PHE CYS LYS TYR
SEQRES 39 A 859 ALA GLN GLY ALA ASP SER VAL GLU PRO MET PHE ARG HIS
SEQRES 40 A 859 LEU LYS ASN THR TYR ALA GLY LEU GLN LEU VAL VAL VAL
SEQRES 41 A 859 ILE LEU PRO GLY LYS THR PRO VAL TYR ALA GLU VAL LYS
SEQRES 42 A 859 ARG VAL GLY ASP THR VAL LEU GLY MET ALA THR GLN CYS
SEQRES 43 A 859 VAL GLN MET LYS ASN VAL GLN ARG THR THR PRO GLN THR
SEQRES 44 A 859 LEU SER ASN LEU CYS LEU LYS ILE ASN VAL LYS LEU GLY
SEQRES 45 A 859 GLY VAL ASN ASN ILE LEU LEU PRO GLN GLY ARG PRO PRO
SEQRES 46 A 859 VAL PHE GLN GLN PRO VAL ILE PHE LEU GLY ALA ASP VAL
SEQRES 47 A 859 THR HIS PRO PRO ALA GLY ASP GLY LYS LYS PRO SER ILE
SEQRES 48 A 859 ALA ALA VAL VAL GLY SER MET ASP ALA HIS PRO ASN ARG
SEQRES 49 A 859 TYR CYS ALA THR VAL ARG VAL GLN GLN HIS ARG GLN GLU
SEQRES 50 A 859 ILE ILE GLN ASP LEU ALA ALA MET VAL ARG GLU LEU LEU
SEQRES 51 A 859 ILE GLN PHE TYR LYS SER THR ARG PHE LYS PRO THR ARG
SEQRES 52 A 859 ILE ILE PHE TYR ARG ASP GLY VAL SER GLU GLY GLN PHE
SEQRES 53 A 859 GLN GLN VAL LEU HIS HIS GLU LEU LEU ALA ILE ARG GLU
SEQRES 54 A 859 ALA CYS ILE LYS LEU GLU LYS ASP TYR GLN PRO GLY ILE
SEQRES 55 A 859 THR PHE ILE VAL VAL GLN LYS ARG HIS HIS THR ARG LEU
SEQRES 56 A 859 PHE CYS THR ASP LYS ASN GLU ARG VAL GLY LYS SER GLY
SEQRES 57 A 859 ASN ILE PRO ALA GLY THR THR VAL ASP THR LYS ILE THR
SEQRES 58 A 859 HIS PRO THR GLU PHE ASP PHE TYR LEU CYS SER HIS ALA
SEQRES 59 A 859 GLY ILE GLN GLY THR SER ARG PRO SER HIS TYR HIS VAL
SEQRES 60 A 859 LEU TRP ASP ASP ASN ARG PHE SER SER ASP GLU LEU GLN
SEQRES 61 A 859 ILE LEU THR TYR GLN LEU CYS HIS THR TYR VAL ARG CYS
SEQRES 62 A 859 THR ARG SER VAL SER ILE PRO ALA PRO ALA TYR TYR ALA
SEQRES 63 A 859 HIS LEU VAL ALA PHE ARG ALA ARG TYR HIS LEU VAL ASP
SEQRES 64 A 859 LYS GLU HIS ASP SER ALA GLU GLY SER HIS THR SER GLY
SEQRES 65 A 859 GLN SER ASN GLY ARG ASP HIS GLN ALA LEU ALA LYS ALA
SEQRES 66 A 859 VAL GLN VAL HIS GLN ASP THR LEU ARG THR MET TYR PHE
SEQRES 67 A 859 ALA
SEQRES 1 B 21 U U C A C A U U G C C C A
SEQRES 2 B 21 A G U C U C U U
SEQRES 1 D 11 C A A U G U G A G A A
HET MG A 901 1
HET IPH A 902 7
HET IPH A 903 7
HET IPH A 904 7
HET IPH A 905 7
HET IPA A 906 4
HET IPA A 907 4
HET IPA A 908 4
HET MG B 101 1
HET IPA B 102 4
HET IPA B 103 4
HET MG D 101 1
HETNAM MG MAGNESIUM ION
HETNAM IPH PHENOL
HETNAM IPA ISOPROPYL ALCOHOL
HETSYN IPA 2-PROPANOL
FORMUL 4 MG 3(MG 2+)
FORMUL 5 IPH 4(C6 H6 O)
FORMUL 9 IPA 5(C3 H8 O)
FORMUL 16 HOH *554(H2 O)
HELIX 1 AA1 PRO A 67 PHE A 82 1 16
HELIX 2 AA2 LEU A 140 SER A 148 1 9
HELIX 3 AA3 PRO A 155 HIS A 168 1 14
HELIX 4 AA4 LEU A 169 TYR A 174 1 6
HELIX 5 AA5 PRO A 229 ASP A 239 1 11
HELIX 6 AA6 SER A 242 GLN A 246 5 5
HELIX 7 AA7 THR A 251 LYS A 263 1 13
HELIX 8 AA8 VAL A 308 LYS A 317 1 10
HELIX 9 AA9 GLU A 342 CYS A 344 5 3
HELIX 10 AB1 THR A 357 ALA A 369 1 13
HELIX 11 AB2 SER A 371 ASP A 387 1 17
HELIX 12 AB3 PHE A 388 THR A 390 5 3
HELIX 13 AB4 ASP A 391 PHE A 397 1 7
HELIX 14 AB5 THR A 463 ALA A 481 1 19
HELIX 15 AB6 GLY A 497 ASP A 499 5 3
HELIX 16 AB7 SER A 500 TYR A 512 1 13
HELIX 17 AB8 PRO A 527 THR A 538 1 12
HELIX 18 AB9 MET A 549 ARG A 554 1 6
HELIX 19 AC1 THR A 556 LEU A 571 1 16
HELIX 20 AC2 PRO A 580 ARG A 583 5 4
HELIX 21 AC3 PRO A 584 GLN A 589 5 6
HELIX 22 AC4 ASP A 641 ARG A 658 1 18
HELIX 23 AC5 SER A 672 GLY A 674 5 3
HELIX 24 AC6 GLN A 675 GLU A 695 1 21
HELIX 25 AC7 ASP A 719 ARG A 723 5 5
HELIX 26 AC8 SER A 775 CYS A 787 1 13
HELIX 27 AC9 PRO A 800 LEU A 817 1 18
HELIX 28 AD1 ARG A 837 GLN A 847 1 11
SHEET 1 AA111 TYR A 625 GLN A 632 0
SHEET 2 AA111 SER A 610 SER A 617 -1 N SER A 610 O GLN A 632
SHEET 3 AA111 VAL A 591 THR A 599 -1 N ASP A 597 O ALA A 613
SHEET 4 AA111 ARG A 663 ASP A 669 1 O ILE A 665 N LEU A 594
SHEET 5 AA111 GLY A 701 GLN A 708 1 O ILE A 705 N ARG A 668
SHEET 6 AA111 SER A 763 ASP A 770 -1 O HIS A 766 N VAL A 706
SHEET 7 AA111 ASP A 747 CYS A 751 -1 N LEU A 750 O SER A 763
SHEET 8 AA111 THR A 734 VAL A 736 -1 N THR A 734 O CYS A 751
SHEET 9 AA111 THR A 406 VAL A 412 -1 N ARG A 411 O THR A 735
SHEET 10 AA111 ARG A 36 ALA A 42 -1 N ILE A 38 O GLY A 410
SHEET 11 AA111 LEU A 715 CYS A 717 -1 O PHE A 716 N GLN A 41
SHEET 1 AA2 4 THR A 175 VAL A 177 0
SHEET 2 AA2 4 SER A 180 THR A 183 -1 O PHE A 182 N THR A 175
SHEET 3 AA2 4 ARG A 196 ARG A 207 -1 O PHE A 202 N PHE A 181
SHEET 4 AA2 4 PRO A 191 GLY A 193 -1 N LEU A 192 O ARG A 196
SHEET 1 AA3 6 THR A 175 VAL A 177 0
SHEET 2 AA3 6 SER A 180 THR A 183 -1 O PHE A 182 N THR A 175
SHEET 3 AA3 6 ARG A 196 ARG A 207 -1 O PHE A 202 N PHE A 181
SHEET 4 AA3 6 MET A 213 TYR A 225 -1 O ASN A 216 N SER A 205
SHEET 5 AA3 6 PHE A 44 ASP A 48 -1 N PHE A 45 O LEU A 215
SHEET 6 AA3 6 MET A 400 VAL A 401 -1 O MET A 400 N ASP A 48
SHEET 1 AA4 5 VAL A 93 PHE A 94 0
SHEET 2 AA4 5 ASN A 99 THR A 102 -1 O TYR A 101 N VAL A 93
SHEET 3 AA4 5 ASP A 53 LYS A 62 -1 N TYR A 57 O LEU A 100
SHEET 4 AA4 5 PHE A 128 SER A 139 -1 O LYS A 133 N GLU A 58
SHEET 5 AA4 5 VAL A 113 VAL A 117 -1 N LEU A 115 O VAL A 130
SHEET 1 AA5 5 THR A 337 PRO A 340 0
SHEET 2 AA5 5 PRO A 326 VAL A 330 -1 N LEU A 328 O LEU A 339
SHEET 3 AA5 5 LYS A 278 PRO A 288 -1 N ASN A 283 O GLN A 329
SHEET 4 AA5 5 LYS A 266 GLU A 268 -1 N VAL A 267 O TYR A 279
SHEET 5 AA5 5 ASN A 345 ILE A 346 -1 O ASN A 345 N GLU A 268
SHEET 1 AA6 2 THR A 293 PHE A 294 0
SHEET 2 AA6 2 CYS A 306 THR A 307 -1 O CYS A 306 N PHE A 294
SHEET 1 AA7 3 ILE A 427 ALA A 428 0
SHEET 2 AA7 3 ILE A 418 LEU A 419 -1 N ILE A 418 O ALA A 428
SHEET 3 AA7 3 ILE A 577 LEU A 578 -1 O ILE A 577 N LEU A 419
SHEET 1 AA8 4 PHE A 491 TYR A 494 0
SHEET 2 AA8 4 TRP A 451 CYS A 455 1 N CYS A 455 O LYS A 493
SHEET 3 AA8 4 LEU A 517 LEU A 522 1 O VAL A 519 N ALA A 452
SHEET 4 AA8 4 THR A 544 GLN A 548 1 O VAL A 547 N LEU A 522
LINK OD1 ASP A 597 MG MG A 901 1555 1555 2.12
LINK O VAL A 598 MG MG A 901 1555 1555 2.06
LINK MG MG A 901 O HOH A1017 1555 1555 2.10
LINK MG MG A 901 O HOH A1118 1555 1555 2.16
LINK MG MG A 901 O HOH A1286 1555 1555 2.10
LINK MG MG A 901 O HOH B 227 1555 1555 1.94
LINK OP2 A B 13 MG MG B 101 1555 1555 2.06
LINK MG MG B 101 O HOH B 218 1555 1555 2.05
LINK MG MG B 101 O HOH B 219 1555 1555 2.04
LINK MG MG B 101 O HOH B 220 1555 1555 2.06
LINK MG MG B 101 O HOH B 222 1555 1555 2.07
LINK MG MG B 101 O HOH B 239 1555 1555 2.12
LINK O4 U D 4 MG MG D 101 1555 1555 2.12
LINK MG MG D 101 O HOH D 209 1555 1555 2.06
LINK MG MG D 101 O HOH D 219 1555 1555 2.09
LINK MG MG D 101 O HOH D 227 1555 1555 2.11
LINK MG MG D 101 O HOH D 229 1555 1555 2.07
LINK MG MG D 101 O HOH D 235 1555 1555 2.06
CISPEP 1 LYS A 62 PRO A 63 0 1.53
CISPEP 2 HIS A 621 PRO A 622 0 -9.04
SITE 1 AC1 6 ASP A 597 VAL A 598 HOH A1017 HOH A1118
SITE 2 AC1 6 HOH A1286 HOH B 227
SITE 1 AC2 8 ARG A 688 CYS A 691 ILE A 692 TYR A 698
SITE 2 AC2 8 GLN A 699 PRO A 700 ASP A 771 HOH A1110
SITE 1 AC3 5 LEU A 650 TYR A 654 LYS A 660 TYR A 698
SITE 2 AC3 5 HOH A1157
SITE 1 AC4 5 PHE A 587 GLN A 589 PRO A 590 VAL A 591
SITE 2 AC4 5 ALA A 620
SITE 1 AC5 9 GLY A 541 MET A 542 ALA A 543 LYS A 570
SITE 2 AC5 9 THR A 852 THR A 855 TYR A 857 HOH A1229
SITE 3 AC5 9 HOH A1293
SITE 1 AC6 6 ALA A 184 GLU A 197 ALA A 227 TYR A 654
SITE 2 AC6 6 ARG A 658 HOH A1457
SITE 1 AC7 2 THR A 183 PHE A 200
SITE 1 AC8 7 THR A 37 ALA A 530 ARG A 534 VAL A 818
SITE 2 AC8 7 LYS A 820 HOH A1211 HOH A1410
SITE 1 AC9 6 A B 13 HOH B 218 HOH B 219 HOH B 220
SITE 2 AC9 6 HOH B 222 HOH B 239
SITE 1 AD1 4 LYS A 525 U B 1 A D 2 A D 3
SITE 1 AD2 6 THR A 599 HIS A 600 PRO A 601 PRO A 602
SITE 2 AD2 6 G B 9 C B 10
SITE 1 AD3 6 U D 4 HOH D 209 HOH D 219 HOH D 227
SITE 2 AD3 6 HOH D 229 HOH D 235
CRYST1 55.738 117.016 69.874 90.00 92.43 90.00 P 1 21 1 2
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 0.017941 0.000000 0.000761 0.00000
SCALE2 0.000000 0.008546 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014324 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
