HEADER GENE REGULATION 07-MAR-05 1Z25
TITLE STRUCTURE OF P.FURIOSUS ARGONAUTE WITH BOUND MN2+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ARGONAUTE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE 3 ORGANISM_TAXID: 2261;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21RIPL;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PSMT3
KEYWDS ARGONAUTE, PIWI, ACTIVE SITE, RNASEH, MG2+, RNAI, GENE REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR F.V.RIVAS,N.H.TOLIA,J.J.SONG,J.P.ARAGON,J.LIU,G.J.HANNON,L.JOSHUA-TOR
REVDAT 5 14-FEB-24 1Z25 1 REMARK
REVDAT 4 20-OCT-21 1Z25 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1Z25 1 VERSN
REVDAT 2 24-MAY-05 1Z25 1 JRNL
REVDAT 1 05-APR-05 1Z25 0
JRNL AUTH F.V.RIVAS,N.H.TOLIA,J.J.SONG,J.P.ARAGON,J.LIU,G.J.HANNON,
JRNL AUTH 2 L.JOSHUA-TOR
JRNL TITL PURIFIED ARGONAUTE2 AND AN SIRNA FORM RECOMBINANT HUMAN
JRNL TITL 2 RISC.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 12 340 2005
JRNL REFN ISSN 1545-9993
JRNL PMID 15800637
JRNL DOI 10.1038/NSMB918
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 216852.600
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 27656
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1285
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3611
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE : 0.3410
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 202
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.024
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5920
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 165
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 53.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.23000
REMARK 3 B22 (A**2) : -0.53000
REMARK 3 B33 (A**2) : 5.77000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.56000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.33
REMARK 3 ESD FROM SIGMAA (A) : 0.32
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.43
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.40
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.830
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 7.170 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 11.130; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 10.140; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 14.780; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.31
REMARK 3 BSOL : 42.51
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Z25 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032202.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-AUG-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X26C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27689
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.52000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ALCOHOL, PH 8.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 290K
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 52.55400
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 300 REMARK: BIOLOGICAL MONOMER
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: MONOMERIC
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 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 PHE A 27
REMARK 465 ASN A 28
REMARK 465 ASP A 29
REMARK 465 PRO A 30
REMARK 465 GLU A 31
REMARK 465 GLU A 32
REMARK 465 GLU A 33
REMARK 465 LEU A 34
REMARK 465 GLN A 35
REMARK 465 LYS A 36
REMARK 465 GLU A 37
REMARK 465 GLY A 38
REMARK 465 ILE A 253
REMARK 465 LYS A 254
REMARK 465 LYS A 255
REMARK 465 ASN A 256
REMARK 465 LYS A 257
REMARK 465 GLU A 278
REMARK 465 SER A 279
REMARK 465 ASP A 280
REMARK 465 VAL A 281
REMARK 465 LEU A 347
REMARK 465 ASN A 348
REMARK 465 VAL A 349
REMARK 465 GLN A 350
REMARK 465 LYS A 351
REMARK 465 SER A 352
REMARK 465 GLN A 353
REMARK 465 LEU A 354
REMARK 465 SER A 414
REMARK 465 LEU A 415
REMARK 465 ALA A 416
REMARK 465 LYS A 417
REMARK 465 LYS A 418
REMARK 465 TYR A 419
REMARK 465 ASN A 420
REMARK 465 SER A 421
REMARK 465 LEU A 422
REMARK 465 ALA A 423
REMARK 465 LYS A 424
REMARK 465 LYS A 425
REMARK 465 ALA A 426
REMARK 465 ARG A 427
REMARK 465 SER A 428
REMARK 465 THR A 429
REMARK 465 ASN A 430
REMARK 465 GLU A 431
REMARK 465 ILE A 432
REMARK 465 GLY A 433
REMARK 465 LEU A 434
REMARK 465 PRO A 435
REMARK 465 PHE A 436
REMARK 465 LEU A 437
REMARK 465 ASP A 438
REMARK 465 PHE A 439
REMARK 465 ARG A 440
REMARK 465 GLY A 441
REMARK 465 LYS A 442
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 8 37.08 -80.83
REMARK 500 LYS A 15 -8.50 -59.22
REMARK 500 SER A 40 -179.37 -176.85
REMARK 500 ASN A 57 21.71 -69.34
REMARK 500 LEU A 58 61.03 32.12
REMARK 500 LEU A 66 108.42 -55.32
REMARK 500 TYR A 68 107.99 -161.64
REMARK 500 GLU A 69 23.02 -74.09
REMARK 500 PHE A 72 153.47 162.97
REMARK 500 HIS A 135 -79.27 -87.04
REMARK 500 ASP A 136 -96.12 -103.27
REMARK 500 LYS A 161 18.54 53.96
REMARK 500 LYS A 187 32.23 38.91
REMARK 500 GLU A 195 92.78 -60.57
REMARK 500 GLU A 196 136.09 -25.55
REMARK 500 ASN A 206 96.94 -47.68
REMARK 500 ASN A 223 44.72 -80.78
REMARK 500 SER A 251 -146.04 -60.97
REMARK 500 TYR A 259 -78.30 -136.05
REMARK 500 LYS A 260 119.37 84.62
REMARK 500 LYS A 283 -49.34 -134.63
REMARK 500 LYS A 338 -131.88 -81.69
REMARK 500 SER A 341 78.94 -117.03
REMARK 500 ILE A 344 89.86 -64.98
REMARK 500 SER A 345 89.04 -175.24
REMARK 500 TRP A 357 -38.54 -36.44
REMARK 500 ILE A 379 132.54 -30.33
REMARK 500 ARG A 380 -105.83 -78.77
REMARK 500 LEU A 393 151.06 -47.01
REMARK 500 LEU A 450 -3.28 -58.71
REMARK 500 ARG A 519 4.43 -64.94
REMARK 500 ALA A 560 77.75 -156.58
REMARK 500 SER A 565 103.86 -33.41
REMARK 500 GLU A 566 73.39 46.38
REMARK 500 TYR A 568 90.75 65.59
REMARK 500 ARG A 594 -79.12 -72.45
REMARK 500 GLU A 596 68.25 -68.71
REMARK 500 SER A 597 133.88 174.34
REMARK 500 ASN A 615 42.12 83.40
REMARK 500 ASN A 666 74.56 -105.46
REMARK 500 TYR A 670 147.30 -170.04
REMARK 500 LEU A 726 58.99 -92.30
REMARK 500 SER A 732 77.59 66.48
REMARK 500 GLU A 754 35.19 72.96
REMARK 500 ILE A 757 74.20 -100.83
REMARK 500 LYS A 758 95.97 -65.84
REMARK 500 LEU A 767 57.97 -95.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 413 0.07 SIDE CHAIN
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 MN A 771 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 628 OD2
REMARK 620 2 HIS A 745 ND1 88.5
REMARK 620 3 HOH A 774 O 166.1 80.0
REMARK 620 4 HOH A 781 O 87.9 162.2 100.6
REMARK 620 5 HOH A 788 O 88.3 83.6 82.7 78.9
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 771
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1U04 RELATED DB: PDB
REMARK 900 APO P.FURIOSUS ARGONAUTE
REMARK 900 RELATED ID: 1Z26 RELATED DB: PDB
REMARK 900 STRUCTURE OF PYROCOCCUS FURIOSUS ARGONAUTE WITH BOUND TUNGSTATE
DBREF 1Z25 A 1 770 UNP Q8U3D2 Q8U3D2_PYRFU 1 770
SEQADV 1Z25 SER A 0 UNP Q8U3D2 CLONING ARTIFACT
SEQADV 1Z25 ILE A 4 UNP Q8U3D2 LYS 4 ENGINEERED MUTATION
SEQRES 1 A 771 SER MET LYS ALA ILE VAL VAL ILE ASN LEU VAL LYS ILE
SEQRES 2 A 771 ASN LYS LYS ILE ILE PRO ASP LYS ILE TYR VAL TYR ARG
SEQRES 3 A 771 LEU PHE ASN ASP PRO GLU GLU GLU LEU GLN LYS GLU GLY
SEQRES 4 A 771 TYR SER ILE TYR ARG LEU ALA TYR GLU ASN VAL GLY ILE
SEQRES 5 A 771 VAL ILE ASP PRO GLU ASN LEU ILE ILE ALA THR THR LYS
SEQRES 6 A 771 GLU LEU GLU TYR GLU GLY GLU PHE ILE PRO GLU GLY GLU
SEQRES 7 A 771 ILE SER PHE SER GLU LEU ARG ASN ASP TYR GLN SER LYS
SEQRES 8 A 771 LEU VAL LEU ARG LEU LEU LYS GLU ASN GLY ILE GLY GLU
SEQRES 9 A 771 TYR GLU LEU SER LYS LEU LEU ARG LYS PHE ARG LYS PRO
SEQRES 10 A 771 LYS THR PHE GLY ASP TYR LYS VAL ILE PRO SER VAL GLU
SEQRES 11 A 771 MET SER VAL ILE LYS HIS ASP GLU ASP PHE TYR LEU VAL
SEQRES 12 A 771 ILE HIS ILE ILE HIS GLN ILE GLN SER MET LYS THR LEU
SEQRES 13 A 771 TRP GLU LEU VAL ASN LYS ASP PRO LYS GLU LEU GLU GLU
SEQRES 14 A 771 PHE LEU MET THR HIS LYS GLU ASN LEU MET LEU LYS ASP
SEQRES 15 A 771 ILE ALA SER PRO LEU LYS THR VAL TYR LYS PRO CYS PHE
SEQRES 16 A 771 GLU GLU TYR THR LYS LYS PRO LYS LEU ASP HIS ASN GLN
SEQRES 17 A 771 GLU ILE VAL LYS TYR TRP TYR ASN TYR HIS ILE GLU ARG
SEQRES 18 A 771 TYR TRP ASN THR PRO GLU ALA LYS LEU GLU PHE TYR ARG
SEQRES 19 A 771 LYS PHE GLY GLN VAL ASP LEU LYS GLN PRO ALA ILE LEU
SEQRES 20 A 771 ALA LYS PHE ALA SER LYS ILE LYS LYS ASN LYS ASN TYR
SEQRES 21 A 771 LYS ILE TYR LEU LEU PRO GLN LEU VAL VAL PRO THR TYR
SEQRES 22 A 771 ASN ALA GLU GLN LEU GLU SER ASP VAL ALA LYS GLU ILE
SEQRES 23 A 771 LEU GLU TYR THR LYS LEU MET PRO GLU GLU ARG LYS GLU
SEQRES 24 A 771 LEU LEU GLU ASN ILE LEU ALA GLU VAL ASP SER ASP ILE
SEQRES 25 A 771 ILE ASP LYS SER LEU SER GLU ILE GLU VAL GLU LYS ILE
SEQRES 26 A 771 ALA GLN GLU LEU GLU ASN LYS ILE ARG VAL ARG ASP ASP
SEQRES 27 A 771 LYS GLY ASN SER VAL PRO ILE SER GLN LEU ASN VAL GLN
SEQRES 28 A 771 LYS SER GLN LEU LEU LEU TRP THR ASN TYR SER ARG LYS
SEQRES 29 A 771 TYR PRO VAL ILE LEU PRO TYR GLU VAL PRO GLU LYS PHE
SEQRES 30 A 771 ARG LYS ILE ARG GLU ILE PRO MET PHE ILE ILE LEU ASP
SEQRES 31 A 771 SER GLY LEU LEU ALA ASP ILE GLN ASN PHE ALA THR ASN
SEQRES 32 A 771 GLU PHE ARG GLU LEU VAL LYS SER MET TYR TYR SER LEU
SEQRES 33 A 771 ALA LYS LYS TYR ASN SER LEU ALA LYS LYS ALA ARG SER
SEQRES 34 A 771 THR ASN GLU ILE GLY LEU PRO PHE LEU ASP PHE ARG GLY
SEQRES 35 A 771 LYS GLU LYS VAL ILE THR GLU ASP LEU ASN SER ASP LYS
SEQRES 36 A 771 GLY ILE ILE GLU VAL VAL GLU GLN VAL SER SER PHE MET
SEQRES 37 A 771 LYS GLY LYS GLU LEU GLY LEU ALA PHE ILE ALA ALA ARG
SEQRES 38 A 771 ASN LYS LEU SER SER GLU LYS PHE GLU GLU ILE LYS ARG
SEQRES 39 A 771 ARG LEU PHE ASN LEU ASN VAL ILE SER GLN VAL VAL ASN
SEQRES 40 A 771 GLU ASP THR LEU LYS ASN LYS ARG ASP LYS TYR ASP ARG
SEQRES 41 A 771 ASN ARG LEU ASP LEU PHE VAL ARG HIS ASN LEU LEU PHE
SEQRES 42 A 771 GLN VAL LEU SER LYS LEU GLY VAL LYS TYR TYR VAL LEU
SEQRES 43 A 771 ASP TYR ARG PHE ASN TYR ASP TYR ILE ILE GLY ILE ASP
SEQRES 44 A 771 VAL ALA PRO MET LYS ARG SER GLU GLY TYR ILE GLY GLY
SEQRES 45 A 771 SER ALA VAL MET PHE ASP SER GLN GLY TYR ILE ARG LYS
SEQRES 46 A 771 ILE VAL PRO ILE LYS ILE GLY GLU GLN ARG GLY GLU SER
SEQRES 47 A 771 VAL ASP MET ASN GLU PHE PHE LYS GLU MET VAL ASP LYS
SEQRES 48 A 771 PHE LYS GLU PHE ASN ILE LYS LEU ASP ASN LYS LYS ILE
SEQRES 49 A 771 LEU LEU LEU ARG ASP GLY ARG ILE THR ASN ASN GLU GLU
SEQRES 50 A 771 GLU GLY LEU LYS TYR ILE SER GLU MET PHE ASP ILE GLU
SEQRES 51 A 771 VAL VAL THR MET ASP VAL ILE LYS ASN HIS PRO VAL ARG
SEQRES 52 A 771 ALA PHE ALA ASN MET LYS MET TYR PHE ASN LEU GLY GLY
SEQRES 53 A 771 ALA ILE TYR LEU ILE PRO HIS LYS LEU LYS GLN ALA LYS
SEQRES 54 A 771 GLY THR PRO ILE PRO ILE LYS LEU ALA LYS LYS ARG ILE
SEQRES 55 A 771 ILE LYS ASN GLY LYS VAL GLU LYS GLN SER ILE THR ARG
SEQRES 56 A 771 GLN ASP VAL LEU ASP ILE PHE ILE LEU THR ARG LEU ASN
SEQRES 57 A 771 TYR GLY SER ILE SER ALA ASP MET ARG LEU PRO ALA PRO
SEQRES 58 A 771 VAL HIS TYR ALA HIS LYS PHE ALA ASN ALA ILE ARG ASN
SEQRES 59 A 771 GLU TRP LYS ILE LYS GLU GLU PHE LEU ALA GLU GLY PHE
SEQRES 60 A 771 LEU TYR PHE VAL
HET MN A 771 1
HETNAM MN MANGANESE (II) ION
FORMUL 2 MN MN 2+
FORMUL 3 HOH *165(H2 O)
HELIX 1 1 ASN A 13 ILE A 17 5 5
HELIX 2 2 SER A 40 ASN A 48 1 9
HELIX 3 3 SER A 79 LEU A 83 5 5
HELIX 4 4 ARG A 84 ASN A 99 1 16
HELIX 5 5 GLY A 102 ARG A 114 1 13
HELIX 6 6 THR A 154 VAL A 159 1 6
HELIX 7 7 ASP A 162 HIS A 173 1 12
HELIX 8 8 ASN A 206 TRP A 222 1 17
HELIX 9 9 THR A 224 PHE A 235 1 12
HELIX 10 10 ILE A 285 LYS A 290 1 6
HELIX 11 11 MET A 292 VAL A 307 1 16
HELIX 12 12 ALA A 325 ASN A 330 5 6
HELIX 13 13 LEU A 356 SER A 361 5 6
HELIX 14 14 PRO A 373 LYS A 378 5 6
HELIX 15 15 LEU A 393 TYR A 412 1 20
HELIX 16 16 SER A 452 LYS A 468 1 17
HELIX 17 17 SER A 484 ASN A 497 1 14
HELIX 18 18 GLU A 507 LYS A 513 1 7
HELIX 19 19 ASP A 523 LEU A 538 1 16
HELIX 20 20 ASP A 599 PHE A 614 1 16
HELIX 21 21 THR A 632 ASP A 647 1 16
HELIX 22 22 THR A 713 ARG A 725 1 13
HELIX 23 23 PRO A 738 ASN A 753 1 16
HELIX 24 24 LYS A 758 ALA A 763 1 6
SHEET 1 A10 LYS A 2 VAL A 6 0
SHEET 2 A10 GLU A 318 LYS A 323 -1 O ILE A 319 N VAL A 5
SHEET 3 A10 MET A 669 LEU A 673 -1 O TYR A 670 N GLU A 322
SHEET 4 A10 ALA A 676 ILE A 680 -1 O TYR A 678 N PHE A 671
SHEET 5 A10 ILE A 694 LYS A 703 -1 O LEU A 696 N ILE A 677
SHEET 6 A10 GLU A 649 ILE A 656 -1 N ILE A 656 O LYS A 695
SHEET 7 A10 LYS A 622 ARG A 627 1 N ILE A 623 O VAL A 651
SHEET 8 A10 TYR A 553 MET A 562 1 N ILE A 555 O LEU A 626
SHEET 9 A10 ILE A 569 ASP A 577 -1 O PHE A 576 N ILE A 554
SHEET 10 A10 ILE A 582 LYS A 589 -1 O LYS A 584 N MET A 575
SHEET 1 B 6 LYS A 2 VAL A 6 0
SHEET 2 B 6 GLU A 318 LYS A 323 -1 O ILE A 319 N VAL A 5
SHEET 3 B 6 MET A 669 LEU A 673 -1 O TYR A 670 N GLU A 322
SHEET 4 B 6 ALA A 676 ILE A 680 -1 O TYR A 678 N PHE A 671
SHEET 5 B 6 ILE A 694 LYS A 703 -1 O LEU A 696 N ILE A 677
SHEET 6 B 6 LYS A 706 LYS A 709 -1 O GLU A 708 N ILE A 701
SHEET 1 C 7 LEU A 9 LYS A 11 0
SHEET 2 C 7 PHE A 139 SER A 151 -1 O LEU A 141 N VAL A 10
SHEET 3 C 7 VAL A 269 ASN A 273 -1 O TYR A 272 N ILE A 149
SHEET 4 C 7 MET A 178 LYS A 180 -1 N LYS A 180 O VAL A 269
SHEET 5 C 7 VAL A 189 PRO A 192 -1 O TYR A 190 N LEU A 179
SHEET 6 C 7 ALA A 244 PHE A 249 -1 O LYS A 248 N LYS A 191
SHEET 7 C 7 LEU A 203 ASP A 204 -1 N ASP A 204 O ALA A 244
SHEET 1 D 8 LYS A 117 PHE A 119 0
SHEET 2 D 8 TYR A 122 LYS A 134 -1 O TYR A 122 N PHE A 119
SHEET 3 D 8 PHE A 139 SER A 151 -1 O GLN A 150 N LYS A 123
SHEET 4 D 8 VAL A 269 ASN A 273 -1 O TYR A 272 N ILE A 149
SHEET 5 D 8 MET A 178 LYS A 180 -1 N LYS A 180 O VAL A 269
SHEET 6 D 8 VAL A 189 PRO A 192 -1 O TYR A 190 N LEU A 179
SHEET 7 D 8 ALA A 244 PHE A 249 -1 O LYS A 248 N LYS A 191
SHEET 8 D 8 ILE A 261 LEU A 263 -1 O ILE A 261 N ALA A 247
SHEET 1 E 4 GLY A 50 ASP A 54 0
SHEET 2 E 4 ILE A 59 THR A 62 -1 O ALA A 61 N ILE A 51
SHEET 3 E 4 ILE A 21 ARG A 25 -1 N TYR A 22 O THR A 62
SHEET 4 E 4 ILE A 73 ILE A 78 -1 O ILE A 73 N ARG A 25
SHEET 1 F 2 ILE A 332 ARG A 333 0
SHEET 2 F 2 VAL A 544 LEU A 545 -1 O VAL A 544 N ARG A 333
SHEET 1 G 4 LYS A 444 GLU A 448 0
SHEET 2 G 4 MET A 384 ASP A 389 1 N LEU A 388 O ILE A 446
SHEET 3 G 4 GLY A 473 ALA A 479 1 O PHE A 476 N PHE A 385
SHEET 4 G 4 VAL A 500 ASN A 506 1 O ILE A 501 N GLY A 473
SHEET 1 H 2 ARG A 514 ASP A 515 0
SHEET 2 H 2 ASP A 518 LEU A 522 -1 O ARG A 521 N ASP A 515
LINK OD2 ASP A 628 MN MN A 771 1555 1555 2.51
LINK ND1 HIS A 745 MN MN A 771 1555 1555 2.14
LINK MN MN A 771 O HOH A 774 1555 1555 2.51
LINK MN MN A 771 O HOH A 781 1555 1555 2.44
LINK MN MN A 771 O HOH A 788 1555 1555 2.38
SITE 1 AC1 6 ASP A 558 ASP A 628 HIS A 745 HOH A 774
SITE 2 AC1 6 HOH A 781 HOH A 788
CRYST1 68.662 105.108 73.662 90.00 102.70 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 0.014564 0.000000 0.003281 0.00000
SCALE2 0.000000 0.009514 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013916 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
