HEADER TRANSPORT PROTEIN, MEMBRANE PROTEIN 28-MAY-13 4KY0
TITLE CRYSTAL STRUCTURE OF A SUBSTRATE-FREE GLUTAMATE TRANSPORTER HOMOLOGUE
TITLE 2 FROM THERMOCOCCUS KODAKARENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTON/GLUTAMATE SYMPORTER, SDF FAMILY;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOCOCCUS KODAKARENSIS;
SOURCE 3 ORGANISM_TAXID: 69014;
SOURCE 4 STRAIN: ATCC BAA-918 / JCM 12380 / KOD1;
SOURCE 5 GENE: TK0986;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS AMINO ACID TRANSPORTER, ASPARTATE TRANSPORT, GLUTAMATE TRANSPORT
KEYWDS 2 HOMOLOGUE, TRANSPORT PROTEIN, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.GUSKOV,S.JENSEN,S.REMPEL,I.HANELT,D.J.SLOTBOOM
REVDAT 3 20-SEP-23 4KY0 1 REMARK SEQADV
REVDAT 2 23-OCT-13 4KY0 1 JRNL
REVDAT 1 11-SEP-13 4KY0 0
JRNL AUTH S.JENSEN,A.GUSKOV,S.REMPEL,I.HANELT,D.J.SLOTBOOM
JRNL TITL CRYSTAL STRUCTURE OF A SUBSTRATE-FREE ASPARTATE TRANSPORTER.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 20 1224 2013
JRNL REFN ISSN 1545-9993
JRNL PMID 24013209
JRNL DOI 10.1038/NSMB.2663
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 50511
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2526
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 48.3660 - 7.8518 0.99 2851 151 0.2317 0.2824
REMARK 3 2 7.8518 - 6.2364 1.00 2748 145 0.2206 0.2318
REMARK 3 3 6.2364 - 5.4493 1.00 2715 142 0.1956 0.2615
REMARK 3 4 5.4493 - 4.9516 1.00 2687 141 0.1583 0.2297
REMARK 3 5 4.9516 - 4.5970 1.00 2691 142 0.1421 0.1989
REMARK 3 6 4.5970 - 4.3262 0.99 2645 139 0.1458 0.2054
REMARK 3 7 4.3262 - 4.1096 1.00 2677 141 0.1748 0.2354
REMARK 3 8 4.1096 - 3.9308 1.00 2623 139 0.1903 0.2488
REMARK 3 9 3.9308 - 3.7796 1.00 2654 139 0.2044 0.2258
REMARK 3 10 3.7796 - 3.6492 1.00 2658 140 0.2131 0.3021
REMARK 3 11 3.6492 - 3.5351 1.00 2640 139 0.2550 0.3329
REMARK 3 12 3.5351 - 3.4341 0.99 2625 138 0.2940 0.3489
REMARK 3 13 3.4341 - 3.3437 1.00 2605 138 0.3021 0.4107
REMARK 3 14 3.3437 - 3.2621 1.00 2651 139 0.3168 0.3698
REMARK 3 15 3.2621 - 3.1880 1.00 2630 139 0.3459 0.3826
REMARK 3 16 3.1880 - 3.1202 1.00 2646 139 0.3563 0.4056
REMARK 3 17 3.1202 - 3.0578 1.00 2640 138 0.3543 0.4153
REMARK 3 18 3.0578 - 3.0001 1.00 2599 137 0.3516 0.3802
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) : 0.570
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.970
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 99.35
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 : 0.010 9528
REMARK 3 ANGLE : 1.510 12948
REMARK 3 CHIRALITY : 0.061 1614
REMARK 3 PLANARITY : 0.008 1580
REMARK 3 DIHEDRAL : 16.723 3377
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0777 48.1853 -32.1031
REMARK 3 T TENSOR
REMARK 3 T11: 0.6527 T22: 0.7786
REMARK 3 T33: 0.5076 T12: 0.2874
REMARK 3 T13: -0.0554 T23: -0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 2.5942 L22: 1.6193
REMARK 3 L33: 2.5523 L12: -0.2579
REMARK 3 L13: -1.2225 L23: -0.5050
REMARK 3 S TENSOR
REMARK 3 S11: 0.0093 S12: -0.0792 S13: 0.1302
REMARK 3 S21: 0.2176 S22: 0.1892 S23: 0.2712
REMARK 3 S31: -0.5206 S32: -0.8078 S33: -0.2193
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 47.8720 62.8492 -26.9447
REMARK 3 T TENSOR
REMARK 3 T11: 0.7075 T22: 0.5658
REMARK 3 T33: 0.6942 T12: 0.0346
REMARK 3 T13: 0.1611 T23: 0.1465
REMARK 3 L TENSOR
REMARK 3 L11: 1.9733 L22: 2.2772
REMARK 3 L33: 3.1407 L12: 0.0051
REMARK 3 L13: 0.8111 L23: 1.1642
REMARK 3 S TENSOR
REMARK 3 S11: -0.1016 S12: -0.0083 S13: 0.3728
REMARK 3 S21: -0.4908 S22: 0.0965 S23: -0.1216
REMARK 3 S31: -0.4380 S32: 0.5122 S33: -0.0046
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): 38.7034 19.2234 -24.2750
REMARK 3 T TENSOR
REMARK 3 T11: 0.7425 T22: 0.4361
REMARK 3 T33: 0.6059 T12: 0.1600
REMARK 3 T13: 0.1129 T23: -0.0298
REMARK 3 L TENSOR
REMARK 3 L11: 2.5825 L22: 1.9910
REMARK 3 L33: 2.8725 L12: 0.3240
REMARK 3 L13: 0.6238 L23: -0.0508
REMARK 3 S TENSOR
REMARK 3 S11: -0.0108 S12: 0.0195 S13: -0.0364
REMARK 3 S21: 0.0335 S22: -0.1454 S23: -0.0171
REMARK 3 S31: 0.6162 S32: -0.0648 S33: 0.1391
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4KY0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1000079936.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50511
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 48.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: PHASER
REMARK 200 STARTING MODEL: 2NWX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG4000, 100 MM TRIS/BICINE, 60 MM
REMARK 280 CACL2/MGCL2, 5% OG, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 206.34000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 103.17000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 103.17000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 206.34000
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: 7210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 GLY A 2
REMARK 465 LYS A 3
REMARK 465 SER A 4
REMARK 465 LEU A 5
REMARK 465 LEU A 6
REMARK 465 ARG A 7
REMARK 465 ARG A 8
REMARK 465 GLU A 126
REMARK 465 ALA A 127
REMARK 465 GLN A 128
REMARK 465 PRO A 129
REMARK 465 PRO A 130
REMARK 465 SER A 131
REMARK 465 HIS A 431
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 LYS B 3
REMARK 465 SER B 4
REMARK 465 LEU B 5
REMARK 465 LEU B 6
REMARK 465 ARG B 7
REMARK 465 ARG B 8
REMARK 465 TYR B 9
REMARK 465 GLY B 122
REMARK 465 LYS B 123
REMARK 465 ALA B 124
REMARK 465 ILE B 125
REMARK 465 GLU B 126
REMARK 465 ALA B 127
REMARK 465 GLN B 128
REMARK 465 SER B 430
REMARK 465 HIS B 431
REMARK 465 MET C 1
REMARK 465 GLY C 2
REMARK 465 LYS C 3
REMARK 465 SER C 4
REMARK 465 LEU C 5
REMARK 465 LEU C 6
REMARK 465 ARG C 7
REMARK 465 ARG C 8
REMARK 465 TYR C 9
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 NH1 ARG C 107 OE1 GLN C 341 2.13
REMARK 500 OD1 ASP A 424 OG SER A 426 2.13
REMARK 500 O VAL A 140 NH1 ARG B 54 2.19
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 LEU B 336 CA - CB - CG ANGL. DEV. = 15.2 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 PRO A 13 88.32 -56.79
REMARK 500 ILE A 75 -141.16 43.89
REMARK 500 VAL A 115 -47.39 -134.83
REMARK 500 SER A 119 -61.08 -121.60
REMARK 500 LYS A 123 -116.20 52.93
REMARK 500 ILE A 247 -66.07 -102.40
REMARK 500 GLU A 292 -66.02 -90.71
REMARK 500 GLU A 294 -59.99 -122.12
REMARK 500 ILE A 301 -63.84 -98.80
REMARK 500 PHE A 304 -60.72 -106.78
REMARK 500 GLU A 420 -88.19 -124.24
REMARK 500 ILE B 75 -137.60 43.57
REMARK 500 ALA B 113 -58.33 -128.29
REMARK 500 SER B 131 -78.49 -125.29
REMARK 500 LEU B 132 8.78 56.91
REMARK 500 GLU B 152 71.02 34.43
REMARK 500 ILE B 247 -64.09 -100.64
REMARK 500 GLU B 292 -63.33 -92.47
REMARK 500 GLU B 294 -61.61 -123.04
REMARK 500 ILE B 301 -62.53 -100.03
REMARK 500 PHE B 304 -60.69 -106.97
REMARK 500 GLU B 420 -87.99 -122.33
REMARK 500 ILE C 75 -134.70 42.03
REMARK 500 ASN C 116 166.22 175.61
REMARK 500 THR C 121 -167.52 -163.85
REMARK 500 ALA C 127 37.15 38.28
REMARK 500 SER C 131 -70.39 -47.79
REMARK 500 VAL C 133 -60.10 -97.09
REMARK 500 GLU C 152 107.31 -48.46
REMARK 500 ILE C 247 -63.37 -103.43
REMARK 500 GLU C 292 -66.20 -90.56
REMARK 500 GLU C 294 -60.63 -122.04
REMARK 500 ILE C 301 -63.05 -102.66
REMARK 500 PHE C 304 -61.14 -105.59
REMARK 500 GLU C 420 -87.57 -124.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 123 ALA A 124 -132.23
REMARK 500 GLU A 422 LEU A 423 -30.50
REMARK 500 GLU C 126 ALA C 127 145.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 C 502
DBREF 4KY0 A 1 430 UNP Q5JID0 Q5JID0_PYRKO 1 430
DBREF 4KY0 B 1 430 UNP Q5JID0 Q5JID0_PYRKO 1 430
DBREF 4KY0 C 1 430 UNP Q5JID0 Q5JID0_PYRKO 1 430
SEQADV 4KY0 HIS A 431 UNP Q5JID0 EXPRESSION TAG
SEQADV 4KY0 HIS B 431 UNP Q5JID0 EXPRESSION TAG
SEQADV 4KY0 HIS C 431 UNP Q5JID0 EXPRESSION TAG
SEQRES 1 A 431 MET GLY LYS SER LEU LEU ARG ARG TYR LEU ASP TYR PRO
SEQRES 2 A 431 VAL LEU TRP LYS ILE LEU TRP GLY LEU VAL LEU GLY ALA
SEQRES 3 A 431 VAL PHE GLY LEU ILE ALA GLY HIS PHE GLY TYR ALA GLY
SEQRES 4 A 431 ALA VAL LYS THR TYR ILE LYS PRO PHE GLY ASP LEU PHE
SEQRES 5 A 431 VAL ARG LEU LEU LYS MET LEU VAL MET PRO ILE VAL LEU
SEQRES 6 A 431 ALA SER LEU VAL VAL GLY ALA ALA SER ILE SER PRO ALA
SEQRES 7 A 431 ARG LEU GLY ARG VAL GLY VAL LYS ILE VAL VAL TYR TYR
SEQRES 8 A 431 LEU ALA THR SER ALA MET ALA VAL PHE PHE GLY LEU ILE
SEQRES 9 A 431 VAL GLY ARG LEU PHE ASN VAL GLY ALA ASN VAL ASN LEU
SEQRES 10 A 431 GLY SER GLY THR GLY LYS ALA ILE GLU ALA GLN PRO PRO
SEQRES 11 A 431 SER LEU VAL GLN THR LEU LEU ASN ILE VAL PRO THR ASN
SEQRES 12 A 431 PRO PHE ALA SER LEU ALA LYS GLY GLU VAL LEU PRO VAL
SEQRES 13 A 431 ILE PHE PHE ALA ILE ILE LEU GLY ILE ALA ILE THR TYR
SEQRES 14 A 431 LEU MET ASN ARG ASN GLU GLU ARG VAL ARG LYS SER ALA
SEQRES 15 A 431 GLU THR LEU LEU ARG VAL PHE ASP GLY LEU ALA GLU ALA
SEQRES 16 A 431 MET TYR LEU ILE VAL GLY GLY VAL MET GLN TYR ALA PRO
SEQRES 17 A 431 ILE GLY VAL PHE ALA LEU ILE ALA TYR VAL MET ALA GLU
SEQRES 18 A 431 GLN GLY VAL ARG VAL VAL GLY PRO LEU ALA LYS VAL VAL
SEQRES 19 A 431 GLY ALA VAL TYR THR GLY LEU PHE LEU GLN ILE VAL ILE
SEQRES 20 A 431 THR TYR PHE ILE LEU LEU LYS VAL PHE GLY ILE ASP PRO
SEQRES 21 A 431 ILE LYS PHE ILE ARG LYS ALA LYS ASP ALA MET ILE THR
SEQRES 22 A 431 ALA PHE VAL THR ARG SER SER SER GLY THR LEU PRO VAL
SEQRES 23 A 431 THR MET ARG VAL ALA GLU GLU GLU MET GLY VAL ASP LYS
SEQRES 24 A 431 GLY ILE PHE SER PHE THR LEU PRO LEU GLY ALA THR ILE
SEQRES 25 A 431 ASN MET ASP GLY THR ALA LEU TYR GLN GLY VAL THR VAL
SEQRES 26 A 431 LEU PHE VAL ALA ASN ALA ILE GLY HIS PRO LEU THR LEU
SEQRES 27 A 431 GLY GLN GLN LEU VAL VAL VAL LEU THR ALA VAL LEU ALA
SEQRES 28 A 431 SER ILE GLY THR ALA GLY VAL PRO GLY ALA GLY ALA ILE
SEQRES 29 A 431 MET LEU ALA MET VAL LEU GLN SER VAL GLY LEU ASP LEU
SEQRES 30 A 431 THR PRO GLY SER PRO VAL ALA LEU ALA TYR ALA MET ILE
SEQRES 31 A 431 LEU GLY ILE ASP ALA ILE LEU ASP MET GLY ARG THR MET
SEQRES 32 A 431 VAL ASN VAL THR GLY ASP LEU ALA GLY THR VAL ILE VAL
SEQRES 33 A 431 ALA LYS THR GLU LYS GLU LEU ASP GLU SER LYS TRP ILE
SEQRES 34 A 431 SER HIS
SEQRES 1 B 431 MET GLY LYS SER LEU LEU ARG ARG TYR LEU ASP TYR PRO
SEQRES 2 B 431 VAL LEU TRP LYS ILE LEU TRP GLY LEU VAL LEU GLY ALA
SEQRES 3 B 431 VAL PHE GLY LEU ILE ALA GLY HIS PHE GLY TYR ALA GLY
SEQRES 4 B 431 ALA VAL LYS THR TYR ILE LYS PRO PHE GLY ASP LEU PHE
SEQRES 5 B 431 VAL ARG LEU LEU LYS MET LEU VAL MET PRO ILE VAL LEU
SEQRES 6 B 431 ALA SER LEU VAL VAL GLY ALA ALA SER ILE SER PRO ALA
SEQRES 7 B 431 ARG LEU GLY ARG VAL GLY VAL LYS ILE VAL VAL TYR TYR
SEQRES 8 B 431 LEU ALA THR SER ALA MET ALA VAL PHE PHE GLY LEU ILE
SEQRES 9 B 431 VAL GLY ARG LEU PHE ASN VAL GLY ALA ASN VAL ASN LEU
SEQRES 10 B 431 GLY SER GLY THR GLY LYS ALA ILE GLU ALA GLN PRO PRO
SEQRES 11 B 431 SER LEU VAL GLN THR LEU LEU ASN ILE VAL PRO THR ASN
SEQRES 12 B 431 PRO PHE ALA SER LEU ALA LYS GLY GLU VAL LEU PRO VAL
SEQRES 13 B 431 ILE PHE PHE ALA ILE ILE LEU GLY ILE ALA ILE THR TYR
SEQRES 14 B 431 LEU MET ASN ARG ASN GLU GLU ARG VAL ARG LYS SER ALA
SEQRES 15 B 431 GLU THR LEU LEU ARG VAL PHE ASP GLY LEU ALA GLU ALA
SEQRES 16 B 431 MET TYR LEU ILE VAL GLY GLY VAL MET GLN TYR ALA PRO
SEQRES 17 B 431 ILE GLY VAL PHE ALA LEU ILE ALA TYR VAL MET ALA GLU
SEQRES 18 B 431 GLN GLY VAL ARG VAL VAL GLY PRO LEU ALA LYS VAL VAL
SEQRES 19 B 431 GLY ALA VAL TYR THR GLY LEU PHE LEU GLN ILE VAL ILE
SEQRES 20 B 431 THR TYR PHE ILE LEU LEU LYS VAL PHE GLY ILE ASP PRO
SEQRES 21 B 431 ILE LYS PHE ILE ARG LYS ALA LYS ASP ALA MET ILE THR
SEQRES 22 B 431 ALA PHE VAL THR ARG SER SER SER GLY THR LEU PRO VAL
SEQRES 23 B 431 THR MET ARG VAL ALA GLU GLU GLU MET GLY VAL ASP LYS
SEQRES 24 B 431 GLY ILE PHE SER PHE THR LEU PRO LEU GLY ALA THR ILE
SEQRES 25 B 431 ASN MET ASP GLY THR ALA LEU TYR GLN GLY VAL THR VAL
SEQRES 26 B 431 LEU PHE VAL ALA ASN ALA ILE GLY HIS PRO LEU THR LEU
SEQRES 27 B 431 GLY GLN GLN LEU VAL VAL VAL LEU THR ALA VAL LEU ALA
SEQRES 28 B 431 SER ILE GLY THR ALA GLY VAL PRO GLY ALA GLY ALA ILE
SEQRES 29 B 431 MET LEU ALA MET VAL LEU GLN SER VAL GLY LEU ASP LEU
SEQRES 30 B 431 THR PRO GLY SER PRO VAL ALA LEU ALA TYR ALA MET ILE
SEQRES 31 B 431 LEU GLY ILE ASP ALA ILE LEU ASP MET GLY ARG THR MET
SEQRES 32 B 431 VAL ASN VAL THR GLY ASP LEU ALA GLY THR VAL ILE VAL
SEQRES 33 B 431 ALA LYS THR GLU LYS GLU LEU ASP GLU SER LYS TRP ILE
SEQRES 34 B 431 SER HIS
SEQRES 1 C 431 MET GLY LYS SER LEU LEU ARG ARG TYR LEU ASP TYR PRO
SEQRES 2 C 431 VAL LEU TRP LYS ILE LEU TRP GLY LEU VAL LEU GLY ALA
SEQRES 3 C 431 VAL PHE GLY LEU ILE ALA GLY HIS PHE GLY TYR ALA GLY
SEQRES 4 C 431 ALA VAL LYS THR TYR ILE LYS PRO PHE GLY ASP LEU PHE
SEQRES 5 C 431 VAL ARG LEU LEU LYS MET LEU VAL MET PRO ILE VAL LEU
SEQRES 6 C 431 ALA SER LEU VAL VAL GLY ALA ALA SER ILE SER PRO ALA
SEQRES 7 C 431 ARG LEU GLY ARG VAL GLY VAL LYS ILE VAL VAL TYR TYR
SEQRES 8 C 431 LEU ALA THR SER ALA MET ALA VAL PHE PHE GLY LEU ILE
SEQRES 9 C 431 VAL GLY ARG LEU PHE ASN VAL GLY ALA ASN VAL ASN LEU
SEQRES 10 C 431 GLY SER GLY THR GLY LYS ALA ILE GLU ALA GLN PRO PRO
SEQRES 11 C 431 SER LEU VAL GLN THR LEU LEU ASN ILE VAL PRO THR ASN
SEQRES 12 C 431 PRO PHE ALA SER LEU ALA LYS GLY GLU VAL LEU PRO VAL
SEQRES 13 C 431 ILE PHE PHE ALA ILE ILE LEU GLY ILE ALA ILE THR TYR
SEQRES 14 C 431 LEU MET ASN ARG ASN GLU GLU ARG VAL ARG LYS SER ALA
SEQRES 15 C 431 GLU THR LEU LEU ARG VAL PHE ASP GLY LEU ALA GLU ALA
SEQRES 16 C 431 MET TYR LEU ILE VAL GLY GLY VAL MET GLN TYR ALA PRO
SEQRES 17 C 431 ILE GLY VAL PHE ALA LEU ILE ALA TYR VAL MET ALA GLU
SEQRES 18 C 431 GLN GLY VAL ARG VAL VAL GLY PRO LEU ALA LYS VAL VAL
SEQRES 19 C 431 GLY ALA VAL TYR THR GLY LEU PHE LEU GLN ILE VAL ILE
SEQRES 20 C 431 THR TYR PHE ILE LEU LEU LYS VAL PHE GLY ILE ASP PRO
SEQRES 21 C 431 ILE LYS PHE ILE ARG LYS ALA LYS ASP ALA MET ILE THR
SEQRES 22 C 431 ALA PHE VAL THR ARG SER SER SER GLY THR LEU PRO VAL
SEQRES 23 C 431 THR MET ARG VAL ALA GLU GLU GLU MET GLY VAL ASP LYS
SEQRES 24 C 431 GLY ILE PHE SER PHE THR LEU PRO LEU GLY ALA THR ILE
SEQRES 25 C 431 ASN MET ASP GLY THR ALA LEU TYR GLN GLY VAL THR VAL
SEQRES 26 C 431 LEU PHE VAL ALA ASN ALA ILE GLY HIS PRO LEU THR LEU
SEQRES 27 C 431 GLY GLN GLN LEU VAL VAL VAL LEU THR ALA VAL LEU ALA
SEQRES 28 C 431 SER ILE GLY THR ALA GLY VAL PRO GLY ALA GLY ALA ILE
SEQRES 29 C 431 MET LEU ALA MET VAL LEU GLN SER VAL GLY LEU ASP LEU
SEQRES 30 C 431 THR PRO GLY SER PRO VAL ALA LEU ALA TYR ALA MET ILE
SEQRES 31 C 431 LEU GLY ILE ASP ALA ILE LEU ASP MET GLY ARG THR MET
SEQRES 32 C 431 VAL ASN VAL THR GLY ASP LEU ALA GLY THR VAL ILE VAL
SEQRES 33 C 431 ALA LYS THR GLU LYS GLU LEU ASP GLU SER LYS TRP ILE
SEQRES 34 C 431 SER HIS
HET PG4 A 501 13
HET PG4 B 501 13
HET PG4 C 501 13
HET PG4 C 502 13
HETNAM PG4 TETRAETHYLENE GLYCOL
FORMUL 4 PG4 4(C8 H18 O5)
HELIX 1 1 TRP A 16 PHE A 35 1 20
HELIX 2 2 TYR A 37 ILE A 45 1 9
HELIX 3 3 ILE A 45 SER A 74 1 30
HELIX 4 4 SER A 76 ASN A 110 1 35
HELIX 5 5 VAL A 133 ASN A 138 1 6
HELIX 6 6 ASN A 143 LYS A 150 1 8
HELIX 7 7 GLU A 152 ASN A 172 1 21
HELIX 8 8 GLU A 175 GLY A 223 1 49
HELIX 9 9 VAL A 224 VAL A 227 5 4
HELIX 10 10 GLY A 228 ILE A 247 1 20
HELIX 11 11 ILE A 247 PHE A 256 1 10
HELIX 12 12 ASP A 259 ARG A 278 1 20
HELIX 13 13 THR A 283 GLU A 294 1 12
HELIX 14 14 ASP A 298 ASN A 313 1 16
HELIX 15 15 MET A 314 ILE A 332 1 19
HELIX 16 16 THR A 337 ALA A 351 1 15
HELIX 17 17 GLY A 360 VAL A 373 1 14
HELIX 18 18 SER A 381 ILE A 393 1 13
HELIX 19 19 ILE A 393 GLU A 420 1 28
HELIX 20 20 ASP A 424 TRP A 428 5 5
HELIX 21 21 TRP B 16 PHE B 35 1 20
HELIX 22 22 TYR B 37 ILE B 45 1 9
HELIX 23 23 ILE B 45 SER B 74 1 30
HELIX 24 24 SER B 76 ASN B 110 1 35
HELIX 25 25 VAL B 133 ASN B 138 1 6
HELIX 26 26 ASN B 143 LYS B 150 1 8
HELIX 27 27 GLU B 152 ASN B 172 1 21
HELIX 28 28 GLU B 175 GLY B 223 1 49
HELIX 29 29 VAL B 224 VAL B 227 5 4
HELIX 30 30 GLY B 228 ILE B 247 1 20
HELIX 31 31 ILE B 247 PHE B 256 1 10
HELIX 32 32 ASP B 259 ARG B 278 1 20
HELIX 33 33 SER B 279 GLU B 294 1 16
HELIX 34 34 ASP B 298 ASN B 313 1 16
HELIX 35 35 MET B 314 ILE B 332 1 19
HELIX 36 36 THR B 337 ALA B 351 1 15
HELIX 37 37 GLY B 360 VAL B 373 1 14
HELIX 38 38 SER B 381 LEU B 391 1 11
HELIX 39 39 ILE B 393 GLU B 420 1 28
HELIX 40 40 TRP C 16 PHE C 35 1 20
HELIX 41 41 TYR C 37 ILE C 45 1 9
HELIX 42 42 ILE C 45 SER C 74 1 30
HELIX 43 43 SER C 76 ASN C 110 1 35
HELIX 44 44 VAL C 133 ASN C 138 1 6
HELIX 45 45 ASN C 143 LYS C 150 1 8
HELIX 46 46 GLU C 152 ASN C 172 1 21
HELIX 47 47 GLU C 175 GLY C 223 1 49
HELIX 48 48 VAL C 224 VAL C 227 5 4
HELIX 49 49 GLY C 228 ILE C 247 1 20
HELIX 50 50 ILE C 247 PHE C 256 1 10
HELIX 51 51 ASP C 259 ARG C 278 1 20
HELIX 52 52 SER C 279 GLU C 294 1 16
HELIX 53 53 ASP C 298 ASN C 313 1 16
HELIX 54 54 MET C 314 ILE C 332 1 19
HELIX 55 55 THR C 337 ILE C 353 1 17
HELIX 56 56 GLY C 360 VAL C 373 1 14
HELIX 57 57 SER C 381 ILE C 393 1 13
HELIX 58 58 ILE C 393 GLU C 420 1 28
CISPEP 1 ASP A 11 TYR A 12 0 -28.46
CISPEP 2 ASN A 114 VAL A 115 0 -17.30
CISPEP 3 GLY A 122 LYS A 123 0 3.42
CISPEP 4 LEU B 10 ASP B 11 0 6.60
CISPEP 5 ASN B 114 VAL B 115 0 -25.80
CISPEP 6 PRO B 379 GLY B 380 0 -4.24
CISPEP 7 GLU B 422 LEU B 423 0 -29.29
CISPEP 8 ASP C 11 TYR C 12 0 -7.72
CISPEP 9 ASN C 114 VAL C 115 0 -29.73
CISPEP 10 GLU C 422 LEU C 423 0 -27.55
SITE 1 AC1 5 ARG A 82 LYS A 86 PHE A 256 THR A 419
SITE 2 AC1 5 ASN B 174
SITE 1 AC2 1 PRO B 77
SITE 1 AC3 3 LEU C 30 GLY C 223 VAL C 226
SITE 1 AC4 2 LEU C 198 ARG C 289
CRYST1 117.570 117.570 309.510 90.00 90.00 120.00 P 32 2 1 18
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 0.008506 0.004911 0.000000 0.00000
SCALE2 0.000000 0.009821 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003231 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
