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HEADER TOXIN 02-AUG-24 9CYS
TITLE TOXIN/IMMUNITY COMPLEX FOR A T6SS LIPASE EFFECTOR FROM E. CLOACAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: I;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: T6SS LIPASE EFFECTOR;
COMPND 7 CHAIN: A;
COMPND 8 FRAGMENT: UNP RESIDUES 172-472;
COMPND 9 SYNONYM: TLE;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTER CLOACAE;
SOURCE 3 ORGANISM_TAXID: 550;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: ENTEROBACTER CLOACAE;
SOURCE 8 ORGANISM_TAXID: 550;
SOURCE 9 GENE: NCTC10005_04014;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LIPASE, TOXIN, IMMUNITY, METHYLGLYOXAL, TOXIN-IMMUNE SYSTEM COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.J.CUTHBERT,S.J.JENSEN,C.W.GOULDING,C.S.HAYES
REVDAT 1 14-AUG-24 9CYS 0
JRNL AUTH S.J.JENSEN,B.J.CUTHBERT,F.GARZA-SANCHEZ,C.C.HELOU,
JRNL AUTH 2 R.DE MIRANDA,C.W.GOULDING,C.S.HAYES
JRNL TITL ADVANCED GLYCATION END-PRODUCT (AGE) CROSSLINKING ACTIVATES
JRNL TITL 2 A TYPE 6 SECRETION SYSTEM PHOSPHOLIPASE EFFECTOR PROTEIN
JRNL REF NATURE COMMUNICATIONS 2024
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.1_4122
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.92
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 66399
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.010
REMARK 3 FREE R VALUE TEST SET COUNT : 6644
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 36.9200 - 5.4300 0.99 2130 241 0.1638 0.1796
REMARK 3 2 5.4200 - 4.3100 1.00 2063 229 0.1466 0.1744
REMARK 3 3 4.3100 - 3.7600 0.98 2027 226 0.1421 0.1700
REMARK 3 4 3.7600 - 3.4200 1.00 2029 219 0.1609 0.1916
REMARK 3 5 3.4200 - 3.1800 1.00 2032 224 0.1721 0.1985
REMARK 3 6 3.1800 - 2.9900 1.00 2016 225 0.1848 0.2073
REMARK 3 7 2.9900 - 2.8400 0.98 1995 227 0.1884 0.2020
REMARK 3 8 2.8400 - 2.7200 1.00 2019 207 0.1949 0.2209
REMARK 3 9 2.7200 - 2.6100 1.00 1999 233 0.1933 0.2319
REMARK 3 10 2.6100 - 2.5200 1.00 1984 227 0.1946 0.2274
REMARK 3 11 2.5200 - 2.4400 1.00 2024 212 0.1928 0.2259
REMARK 3 12 2.4400 - 2.3700 0.99 1983 234 0.1894 0.2121
REMARK 3 13 2.3700 - 2.3100 1.00 2011 221 0.2068 0.2449
REMARK 3 14 2.3100 - 2.2500 0.99 1995 213 0.1944 0.2417
REMARK 3 15 2.2500 - 2.2000 0.97 1958 210 0.2055 0.2491
REMARK 3 16 2.2000 - 2.1600 0.99 1982 231 0.2125 0.2396
REMARK 3 17 2.1600 - 2.1100 1.00 1994 218 0.2096 0.2511
REMARK 3 18 2.1100 - 2.0700 0.99 1965 217 0.2220 0.2596
REMARK 3 19 2.0700 - 2.0400 0.99 1976 228 0.2273 0.2532
REMARK 3 20 2.0400 - 2.0000 0.99 1998 223 0.2113 0.2509
REMARK 3 21 2.0000 - 1.9700 0.99 1982 224 0.2178 0.2680
REMARK 3 22 1.9700 - 1.9400 0.99 1968 223 0.2255 0.2481
REMARK 3 23 1.9400 - 1.9100 0.99 1945 223 0.2412 0.2819
REMARK 3 24 1.9100 - 1.8800 0.99 1983 208 0.2539 0.2681
REMARK 3 25 1.8800 - 1.8600 0.99 2026 206 0.2670 0.3148
REMARK 3 26 1.8600 - 1.8300 0.97 1909 224 0.2889 0.3059
REMARK 3 27 1.8300 - 1.8100 0.99 1945 238 0.2967 0.3490
REMARK 3 28 1.8100 - 1.7900 0.99 1987 202 0.3191 0.3769
REMARK 3 29 1.7900 - 1.7700 0.99 1920 230 0.3491 0.3285
REMARK 3 30 1.7700 - 1.7500 0.95 1910 201 0.4043 0.4803
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) : 23.210
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.34
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.05
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 9CYS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-AUG-24.
REMARK 100 THE DEPOSITION ID IS D_1000286980.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-DEC-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
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 : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66430
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 38.120
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.80600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
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 (%): 55.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4 M SODIUM CITRATE, 22% PEG3350,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 49.54050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.86950
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 59.66850
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 49.54050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.86950
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 59.66850
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 49.54050
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 55.86950
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 59.66850
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 49.54050
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 55.86950
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 59.66850
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 611 LIES ON A SPECIAL POSITION.
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 I 1
REMARK 465 MET A 160
REMARK 465 ALA A 161
REMARK 465 LYS A 162
REMARK 465 SER A 163
REMARK 465 HIS A 164
REMARK 465 HIS A 165
REMARK 465 HIS A 166
REMARK 465 HIS A 167
REMARK 465 HIS A 168
REMARK 465 GLN A 399
REMARK 465 GLU A 400
REMARK 465 VAL A 401
REMARK 465 ASN A 402
REMARK 465 LEU A 403
REMARK 465 ALA A 404
REMARK 465 GLU A 405
REMARK 465 ASP A 406
REMARK 465 TYR A 407
REMARK 465 LYS A 408
REMARK 465 MET A 409
REMARK 465 LEU A 410
REMARK 465 LYS A 411
REMARK 465 GLY A 412
REMARK 465 HIS A 413
REMARK 465 ILE A 414
REMARK 465 PRO A 415
REMARK 465 THR A 416
REMARK 465 LEU A 417
REMARK 465 ILE A 418
REMARK 465 ALA A 419
REMARK 465 LYS A 420
REMARK 465 GLU A 421
REMARK 465 GLU A 422
REMARK 465 ILE A 423
REMARK 465 SER A 424
REMARK 465 ALA A 425
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 ASP I 2 CG OD1 OD2
REMARK 470 LYS I 4 CG CD CE NZ
REMARK 470 LYS I 230 CG CD CE NZ
REMARK 470 HIS A 169 CG ND1 CD2 CE1 NE2
REMARK 470 ASP A 263 CG OD1 OD2
REMARK 470 ARG A 290 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 294 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A 295 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 309 CG CD OE1 NE2
REMARK 470 SER A 315 OG
REMARK 470 GLU A 372 CG CD OE1 OE2
REMARK 470 GLU A 381 CG CD OE1 OE2
REMARK 470 ASN A 429 CG OD1 ND2
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 A 180 C12 MIE A 505 1.32
REMARK 500 NH2 ARG A 180 C13 MIE A 505 1.32
REMARK 500 NZ LYS A 461 C13 MIE A 505 1.44
REMARK 500 O1 GOL A 504 O HOH A 601 2.05
REMARK 500 O HOH I 391 O HOH I 526 2.12
REMARK 500 OD1 ASP A 257 O HOH A 602 2.13
REMARK 500 CZ ARG A 180 C12 MIE A 505 2.14
REMARK 500 CZ ARG A 180 C13 MIE A 505 2.15
REMARK 500 O HOH I 542 O HOH I 550 2.18
REMARK 500 NH2 ARG A 180 C12 MIE A 505 2.18
REMARK 500 NH1 ARG A 180 C13 MIE A 505 2.19
REMARK 500 OE2 GLU I 174 O HOH I 301 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG A 180 NE ARG A 180 CZ 0.106
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 ARG A 180 NH1 - CZ - NH2 ANGL. DEV. = -9.6 DEGREES
REMARK 500 ARG A 180 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 180 NE - CZ - NH2 ANGL. DEV. = 5.1 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 ASN I 57 -127.38 60.80
REMARK 500 VAL A 222 -78.90 -107.64
REMARK 500 ASP A 316 99.25 -164.14
REMARK 500 SER A 341 -131.10 63.91
REMARK 500 SER A 341 -130.99 63.91
REMARK 500 GLU A 381 -129.29 59.49
REMARK 500 ALA A 382 -9.14 71.31
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 ARG A 180 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 MIE A 505
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7UBZ RELATED DB: PDB
REMARK 900 CHYMOTRYPSIN DIGESTED COMPLEX
REMARK 900 RELATED ID: 7UC1 RELATED DB: PDB
REMARK 900 TLE (S289A)/TLI COMPLEX
DBREF1 9CYS I 1 230 UNP A0A0H3CKN4_ENTCC
DBREF2 9CYS I A0A0H3CKN4 24 253
DBREF1 9CYS A 172 472 UNP A0A0M7ENE2_ENTCL
DBREF2 9CYS A A0A0M7ENE2 172 472
SEQADV 9CYS MET A 160 UNP A0A0M7ENE EXPRESSION TAG
SEQADV 9CYS ALA A 161 UNP A0A0M7ENE EXPRESSION TAG
SEQADV 9CYS LYS A 162 UNP A0A0M7ENE EXPRESSION TAG
SEQADV 9CYS SER A 163 UNP A0A0M7ENE EXPRESSION TAG
SEQADV 9CYS HIS A 164 UNP A0A0M7ENE EXPRESSION TAG
SEQADV 9CYS HIS A 165 UNP A0A0M7ENE EXPRESSION TAG
SEQADV 9CYS HIS A 166 UNP A0A0M7ENE EXPRESSION TAG
SEQADV 9CYS HIS A 167 UNP A0A0M7ENE EXPRESSION TAG
SEQADV 9CYS HIS A 168 UNP A0A0M7ENE EXPRESSION TAG
SEQADV 9CYS HIS A 169 UNP A0A0M7ENE EXPRESSION TAG
SEQADV 9CYS THR A 170 UNP A0A0M7ENE EXPRESSION TAG
SEQADV 9CYS SER A 171 UNP A0A0M7ENE EXPRESSION TAG
SEQRES 1 I 230 MET ASP LEU LYS PRO ASP ASN TYR PHE SER GLY GLN GLN
SEQRES 2 I 230 LEU THR LEU ALA ARG ALA ILE GLU ASN GLY GLU VAL ASP
SEQRES 3 I 230 GLU VAL ILE LYS LEU ALA SER GLY THR ASP LEU ASN LYS
SEQRES 4 I 230 PRO GLY LYS GLU ASP MET THR LEU LEU PHE TRP ALA VAL
SEQRES 5 I 230 MET ASN SER ILE ASN ASN GLN LYS THR PRO GLU ARG LEU
SEQRES 6 I 230 ASN VAL ILE THR MET LEU ILE LYS ALA GLY ALA ASP PRO
SEQRES 7 I 230 LEU GLN PRO ARG PRO GLN GLY LYS ASN SER PRO ALA GLU
SEQRES 8 I 230 PHE VAL LEU MET ALA ASP ASN ALA ASP TRP ILE LYS ALA
SEQRES 9 I 230 MET LEU ASN ALA GLY LEU SER PRO ASN ALA VAL ASP LYS
SEQRES 10 I 230 THR PHE GLY LYS PRO ILE ILE PHE GLN THR LEU GLU ALA
SEQRES 11 I 230 LYS ASN THR LYS THR LEU GLN ALA MET LEU ASP LYS GLY
SEQRES 12 I 230 ALA ASP ILE ASN ILE THR ASP SER LEU GLY ASN THR LEU
SEQRES 13 I 230 LEU ILE ASP ALA LEU ASP PHE HIS SER TYR ASP HIS VAL
SEQRES 14 I 230 LEU LEU LEU LEU GLU ARG GLY ALA ASP PRO GLU ILE LYS
SEQRES 15 I 230 ALA ASP ASN GLY TRP THR MET GLY ASN GLN LEU GLN ARG
SEQRES 16 I 230 PHE LEU ASP ARG ALA LYS VAL GLY SER ASP GLU TYR LYS
SEQRES 17 I 230 LYS LEU ASN GLU ILE LYS ASP VAL LEU ILE GLN HIS GLY
SEQRES 18 I 230 GLY LYS TRP PRO PRO THR PRO VAL LYS
SEQRES 1 A 313 MET ALA LYS SER HIS HIS HIS HIS HIS HIS THR SER THR
SEQRES 2 A 313 LYS ALA GLU ARG TRP GLN ALA ARG LYS ASP LEU ILE ALA
SEQRES 3 A 313 LYS GLY SER ASN SER LEU TYR PRO ASP ALA GLN ILE ALA
SEQRES 4 A 313 ALA LYS ARG LEU ALA ALA ASN ASN ILE ALA VAL GLU LYS
SEQRES 5 A 313 ALA LYS LEU ALA GLU ASN VAL TYR LYS THR VAL ASN PRO
SEQRES 6 A 313 LEU GLU ALA THR PRO GLY VAL PRO GLU GLY TRP LYS ASP
SEQRES 7 A 313 ILE SER ASN ASP ALA GLY ALA LEU LYS LYS TYR GLY LEU
SEQRES 8 A 313 ASP LYS GLU VAL LEU PHE ASP HIS ALA ASP THR PRO ASP
SEQRES 9 A 313 PHE LEU ALA ARG VAL TYR GLN PRO ASP SER ALA VAL PHE
SEQRES 10 A 313 GLY SER ASP MET ASN PRO THR ILE VAL PHE ARG GLY SER
SEQRES 11 A 313 ARG GLN PRO GLU PHE PHE PRO THR LYS ASN MET ALA ASP
SEQRES 12 A 313 TRP ILE ASN ASN GLY ALA GLN GLY LEU GLY MET GLU SER
SEQRES 13 A 313 ASP TYR TYR LYS ARG ALA VAL ARG LEU GLY SER ARG LEU
SEQRES 14 A 313 ALA LYS SER VAL SER LYS ILE ASP ILE ALA GLY HIS SER
SEQRES 15 A 313 LEU GLY GLY GLY LEU ALA SER ALA THR SER ILE ALA SER
SEQRES 16 A 313 GLY GLN ALA GLY TRP THR PHE ASN ALA ALA GLY LEU HIS
SEQRES 17 A 313 SER THR THR VAL GLU LYS TYR GLY GLY SER LEU LEU GLY
SEQRES 18 A 313 GLU ALA ASP ASN ILE GLN ALA TYR ARG VAL GLU GLY GLU
SEQRES 19 A 313 LEU LEU THR LYS ILE GLN GLU VAL ASN LEU ALA GLU ASP
SEQRES 20 A 313 TYR LYS MET LEU LYS GLY HIS ILE PRO THR LEU ILE ALA
SEQRES 21 A 313 LYS GLU GLU ILE SER ALA ILE MET PRO ASN ALA ALA GLY
SEQRES 22 A 313 VAL VAL HIS ASP LEU PRO GLY GLY THR GLY GLY PRO LEU
SEQRES 23 A 313 ASP ARG HIS GLY ILE GLY GLN ALA ILE ASP CYS ILE GLU
SEQRES 24 A 313 GLN GLN LYS ASP GLU ASP ILE SER ILE ILE ARG SER ARG
SEQRES 25 A 313 ALA
HET CIT A 501 13
HET GOL A 502 6
HET PGE A 503 10
HET GOL A 504 6
HET MIE A 505 3
HETNAM CIT CITRIC ACID
HETNAM GOL GLYCEROL
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM MIE METHYLGLYOXAL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 CIT C6 H8 O7
FORMUL 4 GOL 2(C3 H8 O3)
FORMUL 5 PGE C6 H14 O4
FORMUL 7 MIE C3 H4 O2
FORMUL 8 HOH *471(H2 O)
HELIX 1 AA1 LYS I 4 TYR I 8 5 5
HELIX 2 AA2 SER I 10 ASN I 22 1 13
HELIX 3 AA3 GLU I 24 SER I 33 1 10
HELIX 4 AA4 GLY I 41 MET I 45 5 5
HELIX 5 AA5 THR I 46 ASN I 54 1 9
HELIX 6 AA6 ILE I 56 LYS I 60 5 5
HELIX 7 AA7 THR I 61 ALA I 74 1 14
HELIX 8 AA8 ARG I 82 LYS I 86 5 5
HELIX 9 AA9 SER I 88 MET I 95 1 8
HELIX 10 AB1 ALA I 99 ASN I 107 1 9
HELIX 11 AB2 PRO I 122 ALA I 130 5 9
HELIX 12 AB3 THR I 133 LYS I 142 1 10
HELIX 13 AB4 THR I 155 PHE I 163 1 9
HELIX 14 AB5 SER I 165 ARG I 175 1 11
HELIX 15 AB6 THR I 188 ALA I 200 1 13
HELIX 16 AB7 SER I 204 HIS I 220 1 17
HELIX 17 AB8 THR A 172 ASN A 189 1 18
HELIX 18 AB9 TYR A 192 VAL A 218 1 27
HELIX 19 AC1 TYR A 219 THR A 221 5 3
HELIX 20 AC2 ASP A 241 LYS A 246 1 6
HELIX 21 AC3 LYS A 247 GLY A 249 5 3
HELIX 22 AC4 LYS A 252 PHE A 256 5 5
HELIX 23 AC5 ASP A 272 GLY A 277 1 6
HELIX 24 AC6 PHE A 294 LYS A 298 5 5
HELIX 25 AC7 ASP A 302 LEU A 311 1 10
HELIX 26 AC8 ASP A 316 ALA A 329 1 14
HELIX 27 AC9 SER A 341 GLY A 355 1 15
HELIX 28 AD1 HIS A 367 TYR A 374 1 8
HELIX 29 AD2 GLY A 375 LEU A 379 5 5
HELIX 30 AD3 GLU A 393 ILE A 398 1 6
HELIX 31 AD4 GLY A 443 GLY A 449 1 7
HELIX 32 AD5 GLY A 449 ARG A 471 1 23
SHEET 1 AA1 7 TRP A 235 ASP A 237 0
SHEET 2 AA1 7 LEU A 265 PRO A 271 -1 O GLN A 270 N LYS A 236
SHEET 3 AA1 7 THR A 283 ARG A 287 -1 O VAL A 285 N ARG A 267
SHEET 4 AA1 7 ASP A 336 HIS A 340 1 O ASP A 336 N ILE A 284
SHEET 5 AA1 7 GLY A 358 PHE A 361 1 O TRP A 359 N ILE A 337
SHEET 6 AA1 7 ILE A 385 VAL A 390 1 O GLN A 386 N GLY A 358
SHEET 7 AA1 7 VAL A 433 LEU A 437 1 O VAL A 433 N ILE A 385
CISPEP 1 TRP I 224 PRO I 225 0 2.70
CRYST1 99.081 111.739 119.337 90.00 90.00 90.00 I 2 2 2 8
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 0.010093 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008949 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008380 0.00000
TER 1777 LYS I 230
TER 3856 ALA A 472
MASTER 422 0 5 32 7 0 0 6 4326 2 38 43
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