HEADER LIGASE 14-MAY-10 3AII
TITLE ARCHAEAL NON-DISCRIMINATING GLUTAMYL-TRNA SYNTHETASE FROM
TITLE 2 METHANOTHERMOBACTER THERMAUTOTROPHICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMYL-TRNA SYNTHETASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GLUTAMATE--TRNA LIGASE, GLURS;
COMPND 5 EC: 6.1.1.17;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOTHERMOBACTER THERMAUTOTROPHICUS;
SOURCE 3 ORGANISM_TAXID: 187420;
SOURCE 4 STRAIN: STR. DELTA H;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS AMINO-ACYL TRNA SYNTHETASE, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR O.NUREKI,R.ISHITANI
REVDAT 2 13-MAR-24 3AII 1 REMARK LINK
REVDAT 1 04-AUG-10 3AII 0
JRNL AUTH O.NUREKI,P.O'DONOGHUE,N.WATANABE,A.OHMORI,H.OSHIKANE,
JRNL AUTH 2 Y.ARAISO,K.SHEPPARD,D.SOLL,R.ISHITANI
JRNL TITL STRUCTURE OF AN ARCHAEAL NON-DISCRIMINATING GLUTAMYL-TRNA
JRNL TITL 2 SYNTHETASE: A MISSING LINK IN THE EVOLUTION OF GLN-TRNAGLN
JRNL TITL 3 FORMATION
JRNL REF NUCLEIC ACIDS RES. 2010
JRNL REFN ESSN 1362-4962
JRNL PMID 20601684
JRNL DOI 10.1093/NAR/GKQ605
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6_289)
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.070
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 67747
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 3397
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 36.6988 - 4.7562 0.97 2862 150 0.2318 0.2354
REMARK 3 2 4.7562 - 3.7764 1.00 2827 151 0.1702 0.1759
REMARK 3 3 3.7764 - 3.2994 1.00 2799 147 0.1819 0.2097
REMARK 3 4 3.2994 - 2.9979 1.00 2780 151 0.1950 0.2068
REMARK 3 5 2.9979 - 2.7831 1.00 2784 142 0.1949 0.2259
REMARK 3 6 2.7831 - 2.6190 1.00 2755 144 0.1932 0.2094
REMARK 3 7 2.6190 - 2.4879 1.00 2764 142 0.1900 0.2308
REMARK 3 8 2.4879 - 2.3796 1.00 2723 151 0.1857 0.2267
REMARK 3 9 2.3796 - 2.2880 1.00 2729 152 0.1911 0.2332
REMARK 3 10 2.2880 - 2.2091 1.00 2760 134 0.1884 0.2572
REMARK 3 11 2.2091 - 2.1400 1.00 2723 146 0.1742 0.2052
REMARK 3 12 2.1400 - 2.0789 1.00 2712 137 0.1814 0.2134
REMARK 3 13 2.0789 - 2.0241 1.00 2741 159 0.1822 0.2257
REMARK 3 14 2.0241 - 1.9748 1.00 2726 144 0.1801 0.2053
REMARK 3 15 1.9748 - 1.9299 1.00 2691 132 0.1745 0.2186
REMARK 3 16 1.9299 - 1.8888 1.00 2726 147 0.1755 0.1804
REMARK 3 17 1.8888 - 1.8510 1.00 2705 146 0.1773 0.2208
REMARK 3 18 1.8510 - 1.8161 1.00 2699 140 0.1887 0.2097
REMARK 3 19 1.8161 - 1.7837 0.99 2710 152 0.1861 0.2452
REMARK 3 20 1.7837 - 1.7534 0.99 2672 137 0.2014 0.2173
REMARK 3 21 1.7534 - 1.7251 0.97 2633 132 0.2122 0.2529
REMARK 3 22 1.7251 - 1.6986 0.94 2555 137 0.2293 0.2482
REMARK 3 23 1.6986 - 1.6736 0.86 2326 121 0.2383 0.2885
REMARK 3 24 1.6736 - 1.6500 0.72 1948 103 0.2425 0.2627
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 : 0.40
REMARK 3 B_SOL : 60.07
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.300
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) : 5.22400
REMARK 3 B22 (A**2) : -7.11050
REMARK 3 B33 (A**2) : 1.88640
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 3851
REMARK 3 ANGLE : 1.041 5218
REMARK 3 CHIRALITY : 0.072 544
REMARK 3 PLANARITY : 0.005 693
REMARK 3 DIHEDRAL : 14.836 1482
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 3AII COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000029294.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
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 : 67808
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 10.50
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 42.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.31200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM SODIUM CACODYLATE, 50MM CALCIUM
REMARK 280 CHLORIDE, 8% PEG6000, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 27.03500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.70100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.94900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.70100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.03500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.94900
REMARK 290 SMTRY3 4 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 MET A 1
REMARK 465 VAL A 2
REMARK 465 PRO A 3
REMARK 465 VAL A 4
REMARK 465 GLU A 5
REMARK 465 ASP A 6
REMARK 465 LEU A 7
REMARK 465 VAL A 8
REMARK 465 TYR A 9
REMARK 465 ARG A 10
REMARK 465 TYR A 11
REMARK 465 ALA A 12
REMARK 465 LEU A 13
REMARK 465 LEU A 14
REMARK 465 ASN A 15
REMARK 465 ALA A 16
REMARK 465 VAL A 17
REMARK 465 LYS A 18
REMARK 465 HIS A 19
REMARK 465 ARG A 20
REMARK 465 GLY A 21
REMARK 465 ARG A 22
REMARK 465 ALA A 23
REMARK 465 ASN A 24
REMARK 465 PRO A 25
REMARK 465 GLY A 26
REMARK 465 ALA A 27
REMARK 465 VAL A 28
REMARK 465 MET A 29
REMARK 465 GLY A 30
REMARK 465 ALA A 31
REMARK 465 VAL A 32
REMARK 465 MET A 33
REMARK 465 SER A 34
REMARK 465 ASN A 35
REMARK 465 GLU A 36
REMARK 465 PRO A 37
REMARK 465 GLU A 38
REMARK 465 LEU A 39
REMARK 465 ARG A 40
REMARK 465 LYS A 41
REMARK 465 MET A 42
REMARK 465 ALA A 43
REMARK 465 PRO A 44
REMARK 465 GLN A 45
REMARK 465 VAL A 46
REMARK 465 LYS A 47
REMARK 465 GLU A 48
REMARK 465 ALA A 49
REMARK 465 VAL A 50
REMARK 465 GLU A 51
REMARK 465 ALA A 52
REMARK 465 ALA A 53
REMARK 465 VAL A 54
REMARK 465 GLU A 55
REMARK 465 ARG A 56
REMARK 465 VAL A 57
REMARK 465 ASN A 58
REMARK 465 SER A 59
REMARK 465 LEU A 60
REMARK 465 SER A 61
REMARK 465 PRO A 62
REMARK 465 GLU A 63
REMARK 465 GLU A 64
REMARK 465 GLN A 65
REMARK 465 GLN A 66
REMARK 465 GLN A 67
REMARK 465 GLU A 68
REMARK 465 MET A 69
REMARK 465 GLU A 70
REMARK 465 ARG A 71
REMARK 465 LEU A 72
REMARK 465 GLY A 73
REMARK 465 LEU A 74
REMARK 465 GLU A 75
REMARK 465 ILE A 76
REMARK 465 THR A 77
REMARK 465 GLU A 78
REMARK 465 ARG A 79
REMARK 465 LYS A 80
REMARK 465 GLN A 81
REMARK 465 LYS A 82
REMARK 465 LYS A 83
REMARK 465 ARG A 84
REMARK 465 LYS A 85
REMARK 465 GLY A 86
REMARK 465 GLY A 293
REMARK 465 LYS A 294
REMARK 465 ASP A 295
REMARK 465 HIS A 296
REMARK 465 LEU A 297
REMARK 465 MET A 325
REMARK 465 ASP A 326
REMARK 465 ASP A 327
REMARK 465 VAL A 328
REMARK 465 ALA A 329
REMARK 465 LEU A 330
REMARK 465 SER A 331
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 PRO A 105 49.13 -87.64
REMARK 500 THR A 239 -117.72 -119.15
REMARK 500 ASP A 250 61.58 36.85
REMARK 500 VAL A 377 37.58 -92.51
REMARK 500 GLU A 400 -19.08 -143.86
REMARK 500 ALA A 463 -85.39 -120.95
REMARK 500 SER A 477 -173.21 -170.94
REMARK 500 ASP A 526 -15.78 92.17
REMARK 500 PHE A 534 -61.61 -129.16
REMARK 500 ALA A 551 -69.32 -92.30
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 CA A1002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 129 O
REMARK 620 2 HOH A 554 O 85.8
REMARK 620 3 HOH A 555 O 95.1 74.5
REMARK 620 4 HOH A 556 O 87.8 151.8 78.8
REMARK 620 5 ACY A 601 OXT 90.9 78.6 151.8 129.0
REMARK 620 6 ACY A 601 O 96.9 126.1 156.9 81.9 47.7
REMARK 620 7 HOH A 933 O 167.3 90.2 95.5 101.2 76.5 75.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 191 SG
REMARK 620 2 CYS A 193 SG 103.4
REMARK 620 3 CYS A 208 SG 115.9 109.8
REMARK 620 4 CYS A 210 SG 112.7 110.6 104.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1002
DBREF 3AII A 1 553 UNP O26157 SYE_METTH 1 553
SEQRES 1 A 553 MET VAL PRO VAL GLU ASP LEU VAL TYR ARG TYR ALA LEU
SEQRES 2 A 553 LEU ASN ALA VAL LYS HIS ARG GLY ARG ALA ASN PRO GLY
SEQRES 3 A 553 ALA VAL MET GLY ALA VAL MET SER ASN GLU PRO GLU LEU
SEQRES 4 A 553 ARG LYS MET ALA PRO GLN VAL LYS GLU ALA VAL GLU ALA
SEQRES 5 A 553 ALA VAL GLU ARG VAL ASN SER LEU SER PRO GLU GLU GLN
SEQRES 6 A 553 GLN GLN GLU MET GLU ARG LEU GLY LEU GLU ILE THR GLU
SEQRES 7 A 553 ARG LYS GLN LYS LYS ARG LYS GLY LEU ARG GLU LEU ALA
SEQRES 8 A 553 GLY VAL LYS GLY GLU VAL VAL LEU ARG PHE ALA PRO ASN
SEQRES 9 A 553 PRO SER GLY PRO LEU HIS ILE GLY HIS ALA ARG ALA ALA
SEQRES 10 A 553 ILE LEU ASN HIS GLU TYR ALA ARG LYS TYR ASP GLY ARG
SEQRES 11 A 553 LEU ILE LEU ARG ILE GLU ASP THR ASP PRO ARG ARG VAL
SEQRES 12 A 553 ASP PRO GLU ALA TYR ASP MET ILE PRO ALA ASP LEU GLU
SEQRES 13 A 553 TRP LEU GLY VAL GLU TRP ASP GLU THR VAL ILE GLN SER
SEQRES 14 A 553 ASP ARG MET GLU THR TYR TYR GLU TYR THR GLU LYS LEU
SEQRES 15 A 553 ILE GLU ARG GLY GLY ALA TYR VAL CYS THR CYS ARG PRO
SEQRES 16 A 553 GLU GLU PHE ARG GLU LEU LYS ASN ARG GLY GLU ALA CYS
SEQRES 17 A 553 HIS CYS ARG SER LEU GLY PHE ARG GLU ASN LEU GLN ARG
SEQRES 18 A 553 TRP ARG GLU MET PHE GLU MET LYS GLU GLY SER ALA VAL
SEQRES 19 A 553 VAL ARG VAL LYS THR ASP LEU ASN HIS PRO ASN PRO ALA
SEQRES 20 A 553 ILE ARG ASP TRP VAL SER MET ARG ILE VAL GLU ALA GLU
SEQRES 21 A 553 HIS PRO ARG THR GLY THR ARG TYR ARG VAL TYR PRO MET
SEQRES 22 A 553 MET ASN PHE SER VAL ALA VAL ASP ASP HIS LEU LEU GLY
SEQRES 23 A 553 VAL THR HIS VAL LEU ARG GLY LYS ASP HIS LEU ALA ASN
SEQRES 24 A 553 ARG GLU LYS GLN GLU TYR LEU TYR ARG HIS LEU GLY TRP
SEQRES 25 A 553 GLU PRO PRO GLU PHE ILE HIS TYR GLY ARG LEU LYS MET
SEQRES 26 A 553 ASP ASP VAL ALA LEU SER THR SER GLY ALA ARG GLU GLY
SEQRES 27 A 553 ILE LEU ARG GLY GLU TYR SER GLY TRP ASP ASP PRO ARG
SEQRES 28 A 553 LEU GLY THR LEU ARG ALA ILE ALA ARG ARG GLY ILE ARG
SEQRES 29 A 553 PRO GLU ALA ILE ARG LYS LEU MET VAL GLU ILE GLY VAL
SEQRES 30 A 553 LYS ILE ALA ASP SER THR MET SER TRP LYS LYS ILE TYR
SEQRES 31 A 553 GLY LEU ASN ARG SER ILE LEU GLU GLU GLU ALA ARG ARG
SEQRES 32 A 553 TYR PHE PHE ALA ALA ASP PRO VAL LYS LEU GLU VAL VAL
SEQRES 33 A 553 GLY LEU PRO GLY PRO VAL ARG VAL GLU ARG PRO LEU HIS
SEQRES 34 A 553 PRO ASP HIS PRO GLU ILE GLY ASN ARG VAL LEU GLU LEU
SEQRES 35 A 553 ARG GLY GLU VAL TYR LEU PRO GLY ASP ASP LEU GLY GLU
SEQRES 36 A 553 GLY PRO LEU ARG LEU ILE ASP ALA VAL ASN VAL ILE TYR
SEQRES 37 A 553 SER GLY GLY GLU LEU ARG TYR HIS SER GLU GLY ILE GLU
SEQRES 38 A 553 GLU ALA ARG GLU LEU GLY ALA SER MET ILE HIS TRP VAL
SEQRES 39 A 553 PRO ALA GLU SER ALA LEU GLU ALA GLU VAL ILE MET PRO
SEQRES 40 A 553 ASP ALA SER ARG VAL ARG GLY VAL ILE GLU ALA ASP ALA
SEQRES 41 A 553 SER GLU LEU GLU VAL ASP ASP VAL VAL GLN LEU GLU ARG
SEQRES 42 A 553 PHE GLY PHE ALA ARG LEU ASP SER ALA GLY PRO GLY MET
SEQRES 43 A 553 VAL PHE TYR TYR ALA HIS LYS
HET ACY A 601 4
HET EDO A 602 4
HET ZN A1001 1
HET CA A1002 1
HETNAM ACY ACETIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 ACY C2 H4 O2
FORMUL 3 EDO C2 H6 O2
FORMUL 4 ZN ZN 2+
FORMUL 5 CA CA 2+
FORMUL 6 HOH *420(H2 O)
HELIX 1 1 HIS A 110 TYR A 127 1 18
HELIX 2 2 ASP A 139 VAL A 143 5 5
HELIX 3 3 ASP A 144 PRO A 145 5 2
HELIX 4 4 GLU A 146 GLY A 159 1 14
HELIX 5 5 ARG A 171 ARG A 185 1 15
HELIX 6 6 ARG A 194 ARG A 204 1 11
HELIX 7 7 CYS A 208 LEU A 213 5 6
HELIX 8 8 GLY A 214 MET A 225 1 12
HELIX 9 9 PHE A 226 MET A 228 5 3
HELIX 10 10 ASN A 245 ARG A 249 5 5
HELIX 11 11 MET A 273 LEU A 285 1 13
HELIX 12 12 ALA A 298 GLY A 311 1 14
HELIX 13 13 THR A 332 GLY A 342 1 11
HELIX 14 14 THR A 354 ARG A 361 1 8
HELIX 15 15 ARG A 364 GLY A 376 1 13
HELIX 16 16 SER A 385 GLU A 398 1 14
HELIX 17 17 HIS A 432 ILE A 435 5 4
HELIX 18 18 GLY A 479 GLY A 487 1 9
HELIX 19 19 GLU A 497 ALA A 499 5 3
HELIX 20 20 ALA A 518 LEU A 523 5 6
SHEET 1 A 3 VAL A 98 PHE A 101 0
SHEET 2 A 3 ARG A 130 ILE A 135 1 O ILE A 132 N PHE A 101
SHEET 3 A 3 GLU A 164 ILE A 167 1 O GLU A 164 N LEU A 133
SHEET 1 B 4 ALA A 188 CYS A 191 0
SHEET 2 B 4 VAL A 234 VAL A 237 -1 O ARG A 236 N TYR A 189
SHEET 3 B 4 VAL A 252 ILE A 256 -1 O SER A 253 N VAL A 235
SHEET 4 B 4 VAL A 270 PRO A 272 -1 O TYR A 271 N ARG A 255
SHEET 1 C 2 HIS A 289 ARG A 292 0
SHEET 2 C 2 GLU A 316 HIS A 319 1 O GLU A 316 N VAL A 290
SHEET 1 D 7 ARG A 402 TYR A 404 0
SHEET 2 D 7 VAL A 528 LEU A 531 1 O GLN A 530 N ARG A 402
SHEET 3 D 7 GLY A 535 SER A 541 -1 O GLY A 535 N LEU A 531
SHEET 4 D 7 MET A 546 HIS A 552 -1 O HIS A 552 N PHE A 536
SHEET 5 D 7 LEU A 500 ILE A 505 1 N ILE A 505 O PHE A 548
SHEET 6 D 7 ARG A 511 ILE A 516 -1 O VAL A 512 N VAL A 504
SHEET 7 D 7 PHE A 406 ALA A 408 -1 N ALA A 407 O VAL A 515
SHEET 1 E 7 SER A 489 ILE A 491 0
SHEET 2 E 7 GLY A 456 LEU A 460 1 N ARG A 459 O SER A 489
SHEET 3 E 7 VAL A 464 SER A 469 -1 O VAL A 466 N LEU A 458
SHEET 4 E 7 GLU A 472 SER A 477 -1 O SER A 477 N ASN A 465
SHEET 5 E 7 PRO A 410 VAL A 416 1 N VAL A 416 O TYR A 475
SHEET 6 E 7 GLU A 445 PRO A 449 -1 O VAL A 446 N LEU A 413
SHEET 7 E 7 VAL A 494 PRO A 495 -1 O VAL A 494 N TYR A 447
SHEET 1 F 2 VAL A 422 PRO A 427 0
SHEET 2 F 2 ASN A 437 LEU A 442 -1 O LEU A 440 N VAL A 424
LINK O GLY A 129 CA CA A1002 1555 1555 2.44
LINK SG CYS A 191 ZN ZN A1001 1555 1555 2.35
LINK SG CYS A 193 ZN ZN A1001 1555 1555 2.37
LINK SG CYS A 208 ZN ZN A1001 1555 1555 2.43
LINK SG CYS A 210 ZN ZN A1001 1555 1555 2.37
LINK O HOH A 554 CA CA A1002 1555 1555 2.57
LINK O HOH A 555 CA CA A1002 1555 1555 2.47
LINK O HOH A 556 CA CA A1002 1555 1555 2.41
LINK OXT ACY A 601 CA CA A1002 1555 1555 2.50
LINK O ACY A 601 CA CA A1002 1555 1555 2.93
LINK O HOH A 933 CA CA A1002 1555 1555 2.22
CISPEP 1 GLY A 543 PRO A 544 0 0.03
SITE 1 AC1 6 GLY A 129 LEU A 131 GLU A 161 ASP A 163
SITE 2 AC1 6 HOH A 933 CA A1002
SITE 1 AC2 5 ASP A 154 TRP A 157 ALA A 359 HOH A 574
SITE 2 AC2 5 HOH A 917
SITE 1 AC3 4 CYS A 191 CYS A 193 CYS A 208 CYS A 210
SITE 1 AC4 6 GLY A 129 HOH A 554 HOH A 555 HOH A 556
SITE 2 AC4 6 ACY A 601 HOH A 933
CRYST1 54.070 99.898 105.402 90.00 90.00 90.00 P 21 21 21 4
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 0.018495 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010010 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009487 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
