HEADER LIGASE 19-DEC-15 5FG0
TITLE STRUCTURE OF THE CONSERVED YEAST LISTERIN (LTN1) N-TERMINAL DOMAIN,
TITLE 2 MONOCLINIC FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE LISTERIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: RING DOMAIN MUTANT KILLED BY RTF1 DELETION PROTEIN 1;
COMPND 5 EC: 6.3.2.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 STRAIN: ATCC 204508 / S288C;
SOURCE 7 GENE: RKR1, LTN1, YMR247C, YM9408.09C, YM9920.01C;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_VARIANT: CODON PLUS RIL;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PSMT3
KEYWDS UBIQUITIN LIGASE, PROTEIN QUALITY CONTROL, RIBOSOME, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.K.DOAMEKPOR,C.D.LIMA
REVDAT 6 06-MAR-24 5FG0 1 LINK
REVDAT 5 20-NOV-19 5FG0 1 REMARK
REVDAT 4 20-SEP-17 5FG0 1 JRNL REMARK
REVDAT 3 03-AUG-16 5FG0 1 JRNL
REVDAT 2 20-JUL-16 5FG0 1 JRNL
REVDAT 1 06-JUL-16 5FG0 0
JRNL AUTH S.K.DOAMEKPOR,J.W.LEE,N.L.HEPOWIT,C.WU,C.CHARENTON,
JRNL AUTH 2 M.LEONARD,M.H.BENGTSON,K.R.RAJASHANKAR,M.S.SACHS,C.D.LIMA,
JRNL AUTH 3 C.A.JOAZEIRO
JRNL TITL STRUCTURE AND FUNCTION OF THE YEAST LISTERIN (LTN1)
JRNL TITL 2 CONSERVED N-TERMINAL DOMAIN IN BINDING TO STALLED 60S
JRNL TITL 3 RIBOSOMAL SUBUNITS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 113 E4151 2016
JRNL REFN ESSN 1091-6490
JRNL PMID 27385828
JRNL DOI 10.1073/PNAS.1605951113
REMARK 2
REMARK 2 RESOLUTION. 2.41 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1951
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) : 2.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.35
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.090
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 46411
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.050
REMARK 3 FREE R VALUE TEST SET COUNT : 1880
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 48.3571 - 5.6599 0.98 3520 152 0.1510 0.1897
REMARK 3 2 5.6599 - 4.4935 0.99 3497 154 0.1473 0.1654
REMARK 3 3 4.4935 - 3.9258 0.98 3462 141 0.1456 0.1718
REMARK 3 4 3.9258 - 3.5670 0.99 3475 147 0.1661 0.2111
REMARK 3 5 3.5670 - 3.3114 0.99 3447 148 0.1908 0.2365
REMARK 3 6 3.3114 - 3.1162 0.99 3461 146 0.2101 0.2290
REMARK 3 7 3.1162 - 2.9601 0.98 3402 147 0.2103 0.2584
REMARK 3 8 2.9601 - 2.8313 0.99 3486 144 0.2100 0.2604
REMARK 3 9 2.8313 - 2.7223 0.99 3421 145 0.2189 0.2747
REMARK 3 10 2.7223 - 2.6284 0.99 3451 147 0.2170 0.2647
REMARK 3 11 2.6284 - 2.5462 0.98 3414 138 0.2142 0.2656
REMARK 3 12 2.5462 - 2.4734 0.98 3413 142 0.2316 0.2637
REMARK 3 13 2.4734 - 2.4083 0.88 3082 129 0.2466 0.3003
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.30
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 : 0.003 6740
REMARK 3 ANGLE : 0.608 9099
REMARK 3 CHIRALITY : 0.030 1050
REMARK 3 PLANARITY : 0.003 1130
REMARK 3 DIHEDRAL : 10.111 2494
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 14 THROUGH 225 )
REMARK 3 ORIGIN FOR THE GROUP (A): 204.3919 43.1657 18.2949
REMARK 3 T TENSOR
REMARK 3 T11: 0.5511 T22: 0.2665
REMARK 3 T33: 0.2849 T12: 0.0282
REMARK 3 T13: -0.0299 T23: -0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 1.8179 L22: 2.5064
REMARK 3 L33: 1.6631 L12: 0.9755
REMARK 3 L13: -0.8187 L23: -0.2334
REMARK 3 S TENSOR
REMARK 3 S11: 0.0822 S12: -0.0952 S13: 0.0381
REMARK 3 S21: -0.7195 S22: -0.1965 S23: -0.0364
REMARK 3 S31: -0.2558 S32: 0.1052 S33: -0.0379
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 226 THROUGH 420 )
REMARK 3 ORIGIN FOR THE GROUP (A): 176.4869 35.8819 42.4506
REMARK 3 T TENSOR
REMARK 3 T11: 0.2866 T22: 0.3523
REMARK 3 T33: 0.3617 T12: 0.0147
REMARK 3 T13: -0.0179 T23: 0.0259
REMARK 3 L TENSOR
REMARK 3 L11: 2.5867 L22: 0.9060
REMARK 3 L33: 1.0130 L12: -0.2035
REMARK 3 L13: -0.9034 L23: -0.0386
REMARK 3 S TENSOR
REMARK 3 S11: 0.0379 S12: -0.0312 S13: 0.0445
REMARK 3 S21: 0.0102 S22: 0.0645 S23: 0.1806
REMARK 3 S31: -0.0740 S32: -0.2036 S33: 0.0002
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 14 THROUGH 224 )
REMARK 3 ORIGIN FOR THE GROUP (A): 204.7905 6.2064 12.8360
REMARK 3 T TENSOR
REMARK 3 T11: 0.3792 T22: 0.3069
REMARK 3 T33: 0.2848 T12: 0.0146
REMARK 3 T13: 0.0485 T23: 0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 1.9197 L22: 2.1028
REMARK 3 L33: 2.4595 L12: -0.2997
REMARK 3 L13: -0.3624 L23: -0.2691
REMARK 3 S TENSOR
REMARK 3 S11: -0.0034 S12: 0.1474 S13: 0.0608
REMARK 3 S21: -0.3269 S22: -0.0988 S23: -0.2408
REMARK 3 S31: -0.0753 S32: 0.1335 S33: 0.0001
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 225 THROUGH 420 )
REMARK 3 ORIGIN FOR THE GROUP (A): 178.8208 -4.3485 36.9301
REMARK 3 T TENSOR
REMARK 3 T11: 0.2796 T22: 0.2985
REMARK 3 T33: 0.3288 T12: 0.0044
REMARK 3 T13: -0.0250 T23: -0.0318
REMARK 3 L TENSOR
REMARK 3 L11: 2.8433 L22: 0.8815
REMARK 3 L33: 0.9074 L12: 0.4399
REMARK 3 L13: -0.9614 L23: -0.3487
REMARK 3 S TENSOR
REMARK 3 S11: 0.0450 S12: 0.0059 S13: -0.0385
REMARK 3 S21: 0.0090 S22: 0.0229 S23: 0.0759
REMARK 3 S31: 0.1228 S32: -0.1707 S33: 0.0018
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 5FG0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216534.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6-7
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46438
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.410
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 (%) : 98.0
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.41
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.41600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7% (W/V) PEG8000, 0.1 M POTASSIUM
REMARK 280 CHLORIDE, AND 2.5% (V/V) GLYCEROL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
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 40.17600
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 350
REMARK 350 BIOMOLECULE: 2
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: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 SER A 11
REMARK 465 LEU A 12
REMARK 465 ASN A 13
REMARK 465 VAL A 421
REMARK 465 LYS A 422
REMARK 465 LYS A 423
REMARK 465 MET A 424
REMARK 465 SER B 11
REMARK 465 LEU B 12
REMARK 465 ASN B 13
REMARK 465 VAL B 421
REMARK 465 LYS B 422
REMARK 465 LYS B 423
REMARK 465 MET B 424
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 ASN A 254 CG OD1 ND2
REMARK 470 LYS A 391 CG CD CE NZ
REMARK 470 PHE A 393 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 396 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 420 CG CD NE CZ NH1 NH2
REMARK 470 TYR B 43 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYR B 81 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN B 256 CG CD OE1 NE2
REMARK 470 LYS B 391 CG CD CE NZ
REMARK 470 PHE B 393 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 396 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 420 CG CD NE CZ NH1 NH2
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 OD1 ASP B 15 O HOH B 601 2.03
REMARK 500 O SER A 234 O HOH A 601 2.15
REMARK 500 ND2 ASN A 257 OD1 ASN A 259 2.19
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 ASN A 21 40.32 -150.26
REMARK 500 ASP A 58 107.26 -54.27
REMARK 500 GLU A 80 -43.57 -149.22
REMARK 500 LYS A 123 -52.16 70.33
REMARK 500 PHE A 159 60.36 -117.70
REMARK 500 LYS A 253 -72.95 -62.66
REMARK 500 ASN A 254 163.33 174.67
REMARK 500 ASN A 257 -169.96 -74.22
REMARK 500 GLU A 376 -47.68 -132.67
REMARK 500 LYS A 391 -63.22 -90.53
REMARK 500 SER A 417 -70.92 -54.71
REMARK 500 ASN B 28 -175.02 -66.71
REMARK 500 LEU B 121 58.71 -92.05
REMARK 500 LYS B 123 -25.51 69.93
REMARK 500 PHE B 159 56.40 -115.05
REMARK 500 ASP B 228 44.17 -106.29
REMARK 500 ASN B 257 -166.56 -112.21
REMARK 500 SER B 349 68.90 -151.94
REMARK 500 GLU B 376 -48.83 -133.67
REMARK 500 PHE B 393 37.78 -90.74
REMARK 500 ASN B 397 56.30 -97.46
REMARK 500 GLU B 419 -169.36 -69.75
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 K A 501 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 185 O
REMARK 620 2 GLU A 188 O 96.9
REMARK 620 3 TYR A 208 OH 83.0 74.0
REMARK 620 4 SER A 245 OG 72.5 166.0 95.3
REMARK 620 5 HOH A 648 O 72.2 104.0 154.8 81.8
REMARK 620 6 HOH A 675 O 150.8 106.1 86.3 81.6 117.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 501 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 185 O
REMARK 620 2 GLU B 188 O 90.6
REMARK 620 3 TYR B 208 OH 77.1 73.9
REMARK 620 4 SER B 245 OG 77.0 160.7 88.7
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 K A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FG1 RELATED DB: PDB
DBREF 5FG0 A 13 424 UNP Q04781 LTN1_YEAST 13 424
DBREF 5FG0 B 13 424 UNP Q04781 LTN1_YEAST 13 424
SEQADV 5FG0 SER A 11 UNP Q04781 EXPRESSION TAG
SEQADV 5FG0 LEU A 12 UNP Q04781 EXPRESSION TAG
SEQADV 5FG0 SER B 11 UNP Q04781 EXPRESSION TAG
SEQADV 5FG0 LEU B 12 UNP Q04781 EXPRESSION TAG
SEQRES 1 A 414 SER LEU ASN THR ASP LEU GLY LEU GLY HIS ASN GLY VAL
SEQRES 2 A 414 ARG ILE SER LEU ASN TYR PHE ASP GLY LEU PRO ASP PRO
SEQRES 3 A 414 SER LEU LEU ASN SER LEU TYR SER ASN GLU LEU LYS LEU
SEQRES 4 A 414 ILE PHE LYS SER LEU LEU LYS ARG ASP GLU THR THR LYS
SEQRES 5 A 414 GLU LYS ALA LEU MET ASP LEU SER ASN LEU ILE SER ASP
SEQRES 6 A 414 PHE ASN GLN ASN GLU TYR PHE PHE ASN ASP ILE PHE LEU
SEQRES 7 A 414 LEU CYS TRP SER GLN ILE TYR ALA LYS LEU ILE ILE SER
SEQRES 8 A 414 ASP TYR LYS VAL ILE ARG LEU GLN SER HIS GLN ILE THR
SEQRES 9 A 414 ILE MET LEU VAL LYS SER LEU ARG LYS LYS ILE SER LYS
SEQRES 10 A 414 PHE LEU LYS ASP PHE ILE PRO LEU ILE LEU LEU GLY THR
SEQRES 11 A 414 CYS GLU LEU ASP TYR SER VAL SER LYS PRO SER LEU ASN
SEQRES 12 A 414 GLU LEU THR GLU CYS PHE ASN LYS ASP PRO ALA LYS ILE
SEQRES 13 A 414 ASN ALA LEU TRP ALA VAL PHE GLN GLU GLN LEU LEU ASN
SEQRES 14 A 414 LEU VAL LYS GLU ILE VAL VAL ASN GLU ASN GLU ASP THR
SEQRES 15 A 414 ILE SER ASP GLU ARG TYR SER SER LYS GLU GLU SER GLU
SEQRES 16 A 414 PHE ARG TYR HIS ARG VAL ILE ALA SER ALA VAL LEU LEU
SEQRES 17 A 414 LEU ILE LYS LEU PHE VAL HIS ASN LYS ASP VAL SER GLU
SEQRES 18 A 414 ARG ASN SER SER SER LEU LYS VAL ILE LEU SER ASP GLU
SEQRES 19 A 414 SER ILE TRP LYS LEU LEU ASN LEU LYS ASN GLY GLN ASN
SEQRES 20 A 414 THR ASN ALA TYR GLU THR VAL LEU ARG LEU ILE ASP VAL
SEQRES 21 A 414 LEU TYR THR ARG GLY TYR MET PRO SER HIS LYS ASN ILE
SEQRES 22 A 414 MET LYS LEU ALA VAL LYS LYS LEU LEU LYS SER LEU THR
SEQRES 23 A 414 HIS ILE THR SER LYS ASN ILE LEU LYS VAL CYS PRO VAL
SEQRES 24 A 414 LEU PRO SER ILE LEU ASN LEU LEU ALA THR LEU ASP ASP
SEQRES 25 A 414 TYR GLU ASP GLY THR ILE TRP SER TYR ASP LYS SER SER
SEQRES 26 A 414 LYS GLU LYS VAL LEU LYS PHE LEU SER VAL SER ARG THR
SEQRES 27 A 414 SER PRO SER PRO GLY PHE PHE ASN ALA VAL PHE ALA LEU
SEQRES 28 A 414 TYR SER SER THR LYS ARG HIS SER PHE LEU ASP TYR TYR
SEQRES 29 A 414 LEU GLU TRP LEU PRO PHE TRP GLN LYS SER VAL GLN ARG
SEQRES 30 A 414 LEU ASN GLU LYS GLY PHE SER ALA ARG ASN SER ALA GLU
SEQRES 31 A 414 VAL LEU ASN GLU PHE TRP THR ASN PHE LEU LYS PHE ALA
SEQRES 32 A 414 GLU ASP SER SER GLU GLU ARG VAL LYS LYS MET
SEQRES 1 B 414 SER LEU ASN THR ASP LEU GLY LEU GLY HIS ASN GLY VAL
SEQRES 2 B 414 ARG ILE SER LEU ASN TYR PHE ASP GLY LEU PRO ASP PRO
SEQRES 3 B 414 SER LEU LEU ASN SER LEU TYR SER ASN GLU LEU LYS LEU
SEQRES 4 B 414 ILE PHE LYS SER LEU LEU LYS ARG ASP GLU THR THR LYS
SEQRES 5 B 414 GLU LYS ALA LEU MET ASP LEU SER ASN LEU ILE SER ASP
SEQRES 6 B 414 PHE ASN GLN ASN GLU TYR PHE PHE ASN ASP ILE PHE LEU
SEQRES 7 B 414 LEU CYS TRP SER GLN ILE TYR ALA LYS LEU ILE ILE SER
SEQRES 8 B 414 ASP TYR LYS VAL ILE ARG LEU GLN SER HIS GLN ILE THR
SEQRES 9 B 414 ILE MET LEU VAL LYS SER LEU ARG LYS LYS ILE SER LYS
SEQRES 10 B 414 PHE LEU LYS ASP PHE ILE PRO LEU ILE LEU LEU GLY THR
SEQRES 11 B 414 CYS GLU LEU ASP TYR SER VAL SER LYS PRO SER LEU ASN
SEQRES 12 B 414 GLU LEU THR GLU CYS PHE ASN LYS ASP PRO ALA LYS ILE
SEQRES 13 B 414 ASN ALA LEU TRP ALA VAL PHE GLN GLU GLN LEU LEU ASN
SEQRES 14 B 414 LEU VAL LYS GLU ILE VAL VAL ASN GLU ASN GLU ASP THR
SEQRES 15 B 414 ILE SER ASP GLU ARG TYR SER SER LYS GLU GLU SER GLU
SEQRES 16 B 414 PHE ARG TYR HIS ARG VAL ILE ALA SER ALA VAL LEU LEU
SEQRES 17 B 414 LEU ILE LYS LEU PHE VAL HIS ASN LYS ASP VAL SER GLU
SEQRES 18 B 414 ARG ASN SER SER SER LEU LYS VAL ILE LEU SER ASP GLU
SEQRES 19 B 414 SER ILE TRP LYS LEU LEU ASN LEU LYS ASN GLY GLN ASN
SEQRES 20 B 414 THR ASN ALA TYR GLU THR VAL LEU ARG LEU ILE ASP VAL
SEQRES 21 B 414 LEU TYR THR ARG GLY TYR MET PRO SER HIS LYS ASN ILE
SEQRES 22 B 414 MET LYS LEU ALA VAL LYS LYS LEU LEU LYS SER LEU THR
SEQRES 23 B 414 HIS ILE THR SER LYS ASN ILE LEU LYS VAL CYS PRO VAL
SEQRES 24 B 414 LEU PRO SER ILE LEU ASN LEU LEU ALA THR LEU ASP ASP
SEQRES 25 B 414 TYR GLU ASP GLY THR ILE TRP SER TYR ASP LYS SER SER
SEQRES 26 B 414 LYS GLU LYS VAL LEU LYS PHE LEU SER VAL SER ARG THR
SEQRES 27 B 414 SER PRO SER PRO GLY PHE PHE ASN ALA VAL PHE ALA LEU
SEQRES 28 B 414 TYR SER SER THR LYS ARG HIS SER PHE LEU ASP TYR TYR
SEQRES 29 B 414 LEU GLU TRP LEU PRO PHE TRP GLN LYS SER VAL GLN ARG
SEQRES 30 B 414 LEU ASN GLU LYS GLY PHE SER ALA ARG ASN SER ALA GLU
SEQRES 31 B 414 VAL LEU ASN GLU PHE TRP THR ASN PHE LEU LYS PHE ALA
SEQRES 32 B 414 GLU ASP SER SER GLU GLU ARG VAL LYS LYS MET
HET K A 501 1
HET EDO A 502 4
HET K B 501 1
HET EDO B 502 4
HET EDO B 503 4
HETNAM K POTASSIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 K 2(K 1+)
FORMUL 4 EDO 3(C2 H6 O2)
FORMUL 8 HOH *169(H2 O)
HELIX 1 AA1 ASP A 35 SER A 41 1 7
HELIX 2 AA2 SER A 44 LEU A 55 1 12
HELIX 3 AA3 ASP A 58 ASP A 75 1 18
HELIX 4 AA4 ASN A 84 ILE A 99 1 16
HELIX 5 AA5 TYR A 103 LEU A 121 1 19
HELIX 6 AA6 ILE A 125 LYS A 127 5 3
HELIX 7 AA7 PHE A 128 CYS A 141 1 14
HELIX 8 AA8 ASP A 144 PHE A 159 1 16
HELIX 9 AA9 ASP A 162 PHE A 173 1 12
HELIX 10 AB1 PHE A 173 VAL A 186 1 14
HELIX 11 AB2 ASN A 189 SER A 194 1 6
HELIX 12 AB3 SER A 200 ASN A 226 1 27
HELIX 13 AB4 ASP A 228 ASN A 233 1 6
HELIX 14 AB5 ASN A 233 ASP A 243 1 11
HELIX 15 AB6 ILE A 246 LEU A 250 5 5
HELIX 16 AB7 THR A 258 ARG A 274 1 17
HELIX 17 AB8 GLY A 275 HIS A 280 1 6
HELIX 18 AB9 HIS A 280 LEU A 295 1 16
HELIX 19 AC1 THR A 296 ILE A 298 5 3
HELIX 20 AC2 ASN A 302 CYS A 307 1 6
HELIX 21 AC3 VAL A 309 ASP A 321 1 13
HELIX 22 AC4 GLY A 326 ASP A 332 5 7
HELIX 23 AC5 SER A 334 ARG A 347 1 14
HELIX 24 AC6 GLY A 353 LYS A 366 1 14
HELIX 25 AC7 ARG A 367 SER A 369 5 3
HELIX 26 AC8 GLU A 376 GLY A 392 1 17
HELIX 27 AC9 ASN A 397 GLU A 414 1 18
HELIX 28 AD1 ASP B 35 ASN B 40 1 6
HELIX 29 AD2 SER B 44 LEU B 55 1 12
HELIX 30 AD3 THR B 61 ASP B 75 1 15
HELIX 31 AD4 ASN B 84 ILE B 99 1 16
HELIX 32 AD5 TYR B 103 LEU B 121 1 19
HELIX 33 AD6 ILE B 125 LYS B 127 5 3
HELIX 34 AD7 PHE B 128 CYS B 141 1 14
HELIX 35 AD8 ASP B 144 PHE B 159 1 16
HELIX 36 AD9 ASP B 162 PHE B 173 1 12
HELIX 37 AE1 PHE B 173 VAL B 186 1 14
HELIX 38 AE2 ASN B 189 SER B 194 1 6
HELIX 39 AE3 SER B 200 HIS B 225 1 26
HELIX 40 AE4 ASP B 228 ASN B 233 1 6
HELIX 41 AE5 ASN B 233 ASP B 243 1 11
HELIX 42 AE6 ILE B 246 LEU B 250 5 5
HELIX 43 AE7 THR B 258 ARG B 274 1 17
HELIX 44 AE8 HIS B 280 LEU B 295 1 16
HELIX 45 AE9 THR B 296 ILE B 298 5 3
HELIX 46 AF1 ASN B 302 CYS B 307 1 6
HELIX 47 AF2 VAL B 309 ASP B 321 1 13
HELIX 48 AF3 GLY B 326 ASP B 332 5 7
HELIX 49 AF4 SER B 334 ARG B 347 1 14
HELIX 50 AF5 GLY B 353 LYS B 366 1 14
HELIX 51 AF6 ARG B 367 SER B 369 5 3
HELIX 52 AF7 GLU B 376 LYS B 391 1 16
HELIX 53 AF8 ASN B 397 GLU B 414 1 18
HELIX 54 AF9 ASP B 415 SER B 417 5 3
LINK O VAL A 185 K K A 501 1555 1555 2.74
LINK O GLU A 188 K K A 501 1555 1555 2.77
LINK OH TYR A 208 K K A 501 1555 1555 2.76
LINK OG SER A 245 K K A 501 1555 1555 2.76
LINK K K A 501 O HOH A 648 1555 1555 2.76
LINK K K A 501 O HOH A 675 1555 1555 2.82
LINK O VAL B 185 K K B 501 1555 1555 2.73
LINK O GLU B 188 K K B 501 1555 1555 2.79
LINK OH TYR B 208 K K B 501 1555 1555 2.81
LINK OG SER B 245 K K B 501 1555 1555 2.74
CISPEP 1 ASN A 254 GLY A 255 0 -2.95
CISPEP 2 GLY A 392 PHE A 393 0 0.86
CISPEP 3 GLY B 392 PHE B 393 0 0.57
CISPEP 4 ARG B 396 ASN B 397 0 1.48
SITE 1 AC1 6 VAL A 185 GLU A 188 TYR A 208 SER A 245
SITE 2 AC1 6 HOH A 648 HOH A 675
SITE 1 AC2 5 ILE A 99 HIS A 111 LEU A 138 GLU A 142
SITE 2 AC2 5 SER A 214
SITE 1 AC3 4 VAL B 185 GLU B 188 TYR B 208 SER B 245
SITE 1 AC4 4 ILE B 99 HIS B 111 GLU B 142 SER B 214
SITE 1 AC5 5 SER B 53 THR B 61 LYS B 64 ALA B 65
SITE 2 AC5 5 ASP B 68
CRYST1 88.514 80.352 97.325 90.00 116.58 90.00 P 1 21 1 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 0.011298 0.000000 0.005653 0.00000
SCALE2 0.000000 0.012445 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011489 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
