HEADER GENE REGULATION/RNA 02-APR-15 4Z4F
TITLE HUMAN ARGONAUTE2 BOUND TO T1-DAP 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*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*(N6G)P*A)-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, GENE REGULATION-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.T.SCHIRLE,I.J.MACRAE
REVDAT 2 27-SEP-23 4Z4F 1 REMARK LINK
REVDAT 1 23-SEP-15 4Z4F 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. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.46
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 21036
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 1049
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 35.4628 - 5.3513 0.93 2865 156 0.1682 0.1886
REMARK 3 2 5.3513 - 4.2498 0.95 2853 161 0.1565 0.2203
REMARK 3 3 4.2498 - 3.7133 0.98 2926 158 0.1650 0.2053
REMARK 3 4 3.7133 - 3.3740 0.92 2750 145 0.1934 0.2677
REMARK 3 5 3.3740 - 3.1324 0.97 2955 140 0.2015 0.2796
REMARK 3 6 3.1324 - 2.9478 0.96 2882 150 0.2388 0.2851
REMARK 3 7 2.9478 - 2.8002 0.92 2756 139 0.2820 0.3551
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) : 0.420
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.910
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 : 0.006 7227
REMARK 3 ANGLE : 0.903 9900
REMARK 3 CHIRALITY : 0.043 1117
REMARK 3 PLANARITY : 0.004 1180
REMARK 3 DIHEDRAL : 13.645 2797
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 22 THROUGH 138 )
REMARK 3 ORIGIN FOR THE GROUP (A): 75.0289 12.3128 5.4318
REMARK 3 T TENSOR
REMARK 3 T11: 0.7415 T22: 0.4859
REMARK 3 T33: 0.5499 T12: 0.0220
REMARK 3 T13: 0.0174 T23: 0.1453
REMARK 3 L TENSOR
REMARK 3 L11: 2.0494 L22: 1.8584
REMARK 3 L33: 2.4247 L12: -0.7423
REMARK 3 L13: 0.5072 L23: -0.5753
REMARK 3 S TENSOR
REMARK 3 S11: -0.0045 S12: 0.4912 S13: 0.7922
REMARK 3 S21: -0.4611 S22: -0.1156 S23: -0.2572
REMARK 3 S31: -0.9202 S32: -0.0647 S33: 0.1087
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 139 THROUGH 238 )
REMARK 3 ORIGIN FOR THE GROUP (A): 71.4458 -3.3024 4.6612
REMARK 3 T TENSOR
REMARK 3 T11: 0.4648 T22: 0.4041
REMARK 3 T33: 0.2768 T12: -0.0131
REMARK 3 T13: 0.0322 T23: 0.0760
REMARK 3 L TENSOR
REMARK 3 L11: 4.1541 L22: 1.1098
REMARK 3 L33: 3.1037 L12: 0.1409
REMARK 3 L13: 1.4035 L23: -0.0243
REMARK 3 S TENSOR
REMARK 3 S11: -0.2634 S12: 0.4313 S13: 0.3282
REMARK 3 S21: -0.1550 S22: 0.0935 S23: 0.0920
REMARK 3 S31: -0.6050 S32: 0.0638 S33: 0.1893
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 239 THROUGH 419 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.5220 -8.7683 -4.4463
REMARK 3 T TENSOR
REMARK 3 T11: 0.5164 T22: 0.7636
REMARK 3 T33: 0.4686 T12: 0.0125
REMARK 3 T13: 0.0172 T23: -0.0392
REMARK 3 L TENSOR
REMARK 3 L11: 1.5315 L22: 0.5463
REMARK 3 L33: 2.1169 L12: -0.1955
REMARK 3 L13: 0.7251 L23: -0.3223
REMARK 3 S TENSOR
REMARK 3 S11: 0.0017 S12: 0.7042 S13: 0.0711
REMARK 3 S21: -0.3024 S22: 0.0268 S23: 0.1662
REMARK 3 S31: -0.0982 S32: -0.3904 S33: -0.0217
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 420 THROUGH 859 )
REMARK 3 ORIGIN FOR THE GROUP (A): 61.3874 -20.1063 33.5092
REMARK 3 T TENSOR
REMARK 3 T11: 0.2096 T22: 0.1958
REMARK 3 T33: 0.2060 T12: 0.0386
REMARK 3 T13: -0.0096 T23: 0.0296
REMARK 3 L TENSOR
REMARK 3 L11: 2.5203 L22: 1.3328
REMARK 3 L33: 1.3375 L12: 0.3743
REMARK 3 L13: -0.2055 L23: 0.1113
REMARK 3 S TENSOR
REMARK 3 S11: 0.0058 S12: -0.1298 S13: -0.1518
REMARK 3 S21: 0.0809 S22: -0.0071 S23: 0.1672
REMARK 3 S31: 0.1016 S32: -0.0741 S33: 0.0034
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 15 )
REMARK 3 ORIGIN FOR THE GROUP (A): 61.7666 -14.1208 17.1690
REMARK 3 T TENSOR
REMARK 3 T11: 0.6091 T22: 0.3802
REMARK 3 T33: 0.5877 T12: 0.0795
REMARK 3 T13: 0.0195 T23: 0.1408
REMARK 3 L TENSOR
REMARK 3 L11: 0.8698 L22: 0.6035
REMARK 3 L33: 1.3949 L12: 0.1934
REMARK 3 L13: 0.2743 L23: 0.9059
REMARK 3 S TENSOR
REMARK 3 S11: 0.0652 S12: 0.3562 S13: 0.6451
REMARK 3 S21: 0.0872 S22: 0.1011 S23: 0.2557
REMARK 3 S31: -0.8466 S32: -0.1842 S33: -0.1180
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 16 THROUGH 21 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.7625 7.0921 -8.4304
REMARK 3 T TENSOR
REMARK 3 T11: 1.7124 T22: 2.0369
REMARK 3 T33: 2.0386 T12: 0.1164
REMARK 3 T13: -0.4249 T23: 0.1613
REMARK 3 L TENSOR
REMARK 3 L11: 1.9999 L22: 1.0642
REMARK 3 L33: 3.2698 L12: -0.5891
REMARK 3 L13: 2.1553 L23: 0.2655
REMARK 3 S TENSOR
REMARK 3 S11: 0.1105 S12: 1.3641 S13: 0.6095
REMARK 3 S21: -0.9481 S22: -0.2505 S23: 1.7407
REMARK 3 S31: -0.4487 S32: -0.6595 S33: 0.1373
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 10 )
REMARK 3 ORIGIN FOR THE GROUP (A): 62.5838 -29.4411 17.2138
REMARK 3 T TENSOR
REMARK 3 T11: 0.5389 T22: 0.2971
REMARK 3 T33: 0.3932 T12: -0.0046
REMARK 3 T13: -0.0313 T23: 0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 3.8132 L22: 3.3257
REMARK 3 L33: 4.5640 L12: -1.3614
REMARK 3 L13: 1.8653 L23: -2.5341
REMARK 3 S TENSOR
REMARK 3 S11: 0.2985 S12: -0.0145 S13: -0.5361
REMARK 3 S21: -0.2954 S22: 0.0236 S23: 0.2135
REMARK 3 S31: 0.9187 S32: -0.0063 S33: -0.3768
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 4Z4F 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_1000208616.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAY-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 : 21078
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 38.860
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : 0.09700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
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 : NULL
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 (%): 42.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
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 58.29550
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: 8460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 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 GLU A 64
REMARK 465 LYS A 65
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 17
REMARK 465 U B 18
REMARK 465 C B 19
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 A D 10 C5' C4' O4' C3' O3' C2' O2'
REMARK 470 A D 10 C1' N9 C8 N7 C5 C6 N6
REMARK 470 A D 10 N1 C2 N3 C4
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 NE2 GLN A 459 OE2 GLU A 464 2.09
REMARK 500 NH2 ARG A 90 O PRO A 105 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 0.193
REMARK 500 PRO A 326 CD PRO A 326 N 0.137
REMARK 500 U B 1 P U B 1 OP3 -0.128
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 PRO A 323 C - N - CD ANGL. DEV. = 12.9 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 -157.88 -124.87
REMARK 500 ASP A 30 -179.04 -178.36
REMARK 500 ASN A 43 44.40 -75.17
REMARK 500 LYS A 51 59.49 -101.20
REMARK 500 ILE A 86 -67.96 -121.58
REMARK 500 ARG A 97 -78.94 -132.21
REMARK 500 LYS A 98 49.69 -150.38
REMARK 500 PRO A 107 65.36 -67.49
REMARK 500 ILE A 108 -20.44 -140.24
REMARK 500 TRP A 134 84.43 95.22
REMARK 500 LEU A 140 -58.25 71.04
REMARK 500 TRP A 211 -71.78 -95.49
REMARK 500 ASP A 239 47.09 75.29
REMARK 500 PRO A 326 -169.96 -75.51
REMARK 500 MET A 483 70.08 -113.85
REMARK 500 CYS A 492 109.23 -160.49
REMARK 500 ASN A 623 -49.83 -140.68
REMARK 500 LYS A 739 -61.28 67.94
REMARK 500 TRP A 769 140.37 -172.14
REMARK 500 THR A 794 54.54 -90.70
REMARK 500 MET A 856 56.93 -105.15
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 MG A 901 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 597 OD1
REMARK 620 2 VAL A 598 O 88.3
REMARK 620 3 HOH A1003 O 87.8 175.9
REMARK 620 4 HOH A1006 O 75.1 86.6 91.1
REMARK 620 5 HOH A1007 O 78.4 91.6 88.9 153.4
REMARK 620 6 HOH B 204 O 156.3 100.4 82.8 83.4 122.9
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 201 O 58.6
REMARK 620 3 HOH B 202 O 58.3 116.9
REMARK 620 N 1 2
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 201 O 99.8
REMARK 620 3 HOH D 202 O 81.7 171.9
REMARK 620 4 HOH D 203 O 85.1 67.1 105.3
REMARK 620 5 HOH D 204 O 76.4 121.5 66.6 160.5
REMARK 620 6 HOH D 205 O 163.1 89.1 87.5 85.2 111.2
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 MG B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
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: 4Z4D RELATED DB: PDB
REMARK 900 RELATED ID: 4Z4E 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 4Z4F A 1 859 UNP Q9UKV8 AGO2_HUMAN 1 859
DBREF 4Z4F B 1 21 PDB 4Z4F 4Z4F 1 21
DBREF 4Z4F D 1 11 PDB 4Z4F 4Z4F 1 11
SEQADV 4Z4F 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 N6G A A
HET N6G D 9 23
HET MG A 901 1
HET IPH A 902 7
HET IPH A 903 7
HET IPH A 904 7
HET MG B 101 1
HET MG D 101 1
HETNAM N6G ((2R,3S,4R,5S)-5-(2,6-DIAMINO-9H-PURIN-9-YL)-3,4-
HETNAM 2 N6G DIHYDROXY-TETRAHYDROFURAN-2-YL)METHYL DIHYDROGEN
HETNAM 3 N6G PHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM IPH PHENOL
FORMUL 3 N6G C10 H15 N6 O7 P
FORMUL 4 MG 3(MG 2+)
FORMUL 5 IPH 3(C6 H6 O)
FORMUL 10 HOH *16(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 ARG A 315 1 8
HELIX 9 AA9 THR A 357 ALA A 369 1 13
HELIX 10 AB1 SER A 371 ASP A 387 1 17
HELIX 11 AB2 ASP A 391 PHE A 397 1 7
HELIX 12 AB3 THR A 463 ALA A 481 1 19
HELIX 13 AB4 GLY A 497 ASP A 499 5 3
HELIX 14 AB5 SER A 500 TYR A 512 1 13
HELIX 15 AB6 THR A 526 THR A 538 1 13
HELIX 16 AB7 MET A 549 ARG A 554 1 6
HELIX 17 AB8 THR A 556 LEU A 571 1 16
HELIX 18 AB9 PRO A 580 ARG A 583 5 4
HELIX 19 AC1 PRO A 584 GLN A 589 5 6
HELIX 20 AC2 ASP A 641 ARG A 658 1 18
HELIX 21 AC3 SER A 672 GLY A 674 5 3
HELIX 22 AC4 GLN A 675 GLU A 695 1 21
HELIX 23 AC5 ASP A 719 ARG A 723 5 5
HELIX 24 AC6 SER A 775 LEU A 786 1 12
HELIX 25 AC7 PRO A 800 LEU A 817 1 18
HELIX 26 AC8 ARG A 837 VAL A 846 1 10
SHEET 1 AA111 TYR A 625 GLN A 632 0
SHEET 2 AA111 SER A 610 SER A 617 -1 N ALA A 612 O ARG A 630
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 VAL A 736 O TYR A 749
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 LEU A 40 O VAL A 408
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 ASP A 218 N HIS A 203
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 4 VAL A 93 PHE A 94 0
SHEET 2 AA4 4 LEU A 100 THR A 102 -1 O TYR A 101 N VAL A 93
SHEET 3 AA4 4 ILE A 54 TYR A 57 -1 N TYR A 57 O LEU A 100
SHEET 4 AA4 4 SER A 136 VAL A 138 -1 O VAL A 138 N ILE A 54
SHEET 1 AA5 3 LEU A 59 LYS A 62 0
SHEET 2 AA5 3 PHE A 128 ILE A 132 -1 O LYS A 129 N LYS A 62
SHEET 3 AA5 3 VAL A 113 VAL A 117 -1 N LEU A 115 O VAL A 130
SHEET 1 AA6 5 TYR A 338 PRO A 340 0
SHEET 2 AA6 5 PRO A 326 VAL A 330 -1 N LEU A 328 O LEU A 339
SHEET 3 AA6 5 LYS A 278 PRO A 288 -1 N ASN A 283 O GLN A 329
SHEET 4 AA6 5 LYS A 266 GLU A 268 -1 N VAL A 267 O TYR A 279
SHEET 5 AA6 5 ASN A 345 ILE A 346 -1 O ASN A 345 N GLU A 268
SHEET 1 AA7 2 THR A 293 PHE A 294 0
SHEET 2 AA7 2 CYS A 306 THR A 307 -1 O CYS A 306 N PHE A 294
SHEET 1 AA8 3 ILE A 427 ALA A 428 0
SHEET 2 AA8 3 ILE A 418 LEU A 419 -1 N ILE A 418 O ALA A 428
SHEET 3 AA8 3 ILE A 577 LEU A 578 -1 O ILE A 577 N LEU A 419
SHEET 1 AA9 4 PHE A 491 TYR A 494 0
SHEET 2 AA9 4 TRP A 451 CYS A 455 1 N ILE A 453 O PHE A 491
SHEET 3 AA9 4 LEU A 517 LEU A 522 1 O VAL A 519 N ALA A 452
SHEET 4 AA9 4 THR A 544 GLN A 548 1 O GLN A 545 N VAL A 520
LINK O3' A D 8 P N6G D 9 1555 1555 1.61
LINK O3' N6G D 9 P A D 10 1555 1555 1.61
LINK OD1 ASP A 597 MG MG A 901 1555 1555 2.43
LINK O VAL A 598 MG MG A 901 1555 1555 2.08
LINK MG MG A 901 O HOH A1003 1555 1555 2.29
LINK MG MG A 901 O HOH A1006 1555 1555 2.15
LINK MG MG A 901 O HOH A1007 1555 1555 2.14
LINK MG MG A 901 O HOH B 204 1555 1555 2.16
LINK OP2 A B 13 MG MG B 101 1555 1555 2.77
LINK MG MG B 101 O HOH B 201 1555 1555 2.11
LINK MG MG B 101 O HOH B 202 1555 1555 2.26
LINK O4 U D 4 MG MG D 101 1555 1555 2.14
LINK MG MG D 101 O HOH D 201 1555 1555 2.41
LINK MG MG D 101 O HOH D 202 1555 1555 1.99
LINK MG MG D 101 O HOH D 203 1555 1555 2.39
LINK MG MG D 101 O HOH D 204 1555 1555 2.98
LINK MG MG D 101 O HOH D 205 1555 1555 2.69
CISPEP 1 LYS A 62 PRO A 63 0 10.67
CISPEP 2 HIS A 621 PRO A 622 0 -7.38
SITE 1 AC1 7 ASP A 597 VAL A 598 HOH A1003 HOH A1006
SITE 2 AC1 7 HOH A1007 C B 10 HOH B 204
SITE 1 AC2 4 LYS A 660 PRO A 661 GLU A 695 TYR A 698
SITE 1 AC3 6 PHE A 587 GLN A 589 PRO A 590 VAL A 591
SITE 2 AC3 6 ALA A 620 PHE A 653
SITE 1 AC4 6 ASP A 537 MET A 542 ALA A 543 THR A 852
SITE 2 AC4 6 THR A 855 TYR A 857
SITE 1 AC5 3 A B 13 HOH B 201 HOH B 202
SITE 1 AC6 6 U D 4 HOH D 201 HOH D 202 HOH D 203
SITE 2 AC6 6 HOH D 204 HOH D 205
CRYST1 55.859 116.591 70.375 90.00 92.52 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 0.017902 0.000000 0.000787 0.00000
SCALE2 0.000000 0.008577 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014223 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
