HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 16-MAR-07 2P5Z
TITLE THE E. COLI C3393 PROTEIN IS A COMPONENT OF THE TYPE VI SECRETION
TITLE 2 SYSTEM AND EXHIBITS STRUCTURAL SIMILARITY TO T4 BACTERIOPHAGE TAIL
TITLE 3 PROTEINS GP27 AND GP5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYPE VI SECRETION SYSTEM COMPONENT;
COMPND 3 CHAIN: X;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI O6;
SOURCE 3 ORGANISM_TAXID: 217992;
SOURCE 4 STRAIN: O6:H1, CFT073, UPEC;
SOURCE 5 ATCC: 700928;
SOURCE 6 GENE: C3393;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: BC-PSGX3(BC)
KEYWDS STRUCTURAL GENOMICS, UNKNOWN FUNCTION, PSI-2, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS,
KEYWDS 3 NYSGXRC
EXPDTA X-RAY DIFFRACTION
AUTHOR U.A.RAMAGOPAL,J.B.BONANNO,V.SRIDHAR,C.LAU,R.TORO,T.GHEYI,M.MALETIC,
AUTHOR 2 J.C.FREEMAN,J.M.SAUDER,S.K.BURLEY,S.C.ALMO,NEW YORK SGX RESEARCH
AUTHOR 3 CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 9 21-FEB-24 2P5Z 1 REMARK
REVDAT 8 03-FEB-21 2P5Z 1 AUTHOR JRNL SEQADV
REVDAT 7 14-NOV-18 2P5Z 1 AUTHOR
REVDAT 6 18-OCT-17 2P5Z 1 REMARK
REVDAT 5 13-JUL-11 2P5Z 1 VERSN
REVDAT 4 31-MAR-09 2P5Z 1 JRNL
REVDAT 3 24-MAR-09 2P5Z 1 COMPND JRNL TITLE
REVDAT 2 24-FEB-09 2P5Z 1 VERSN
REVDAT 1 03-APR-07 2P5Z 0
JRNL AUTH P.G.LEIMAN,M.BASLER,U.A.RAMAGOPAL,J.B.BONANNO,J.M.SAUDER,
JRNL AUTH 2 S.PUKATZKI,S.K.BURLEY,S.C.ALMO,J.J.MEKALANOS
JRNL TITL TYPE VI SECRETION APPARATUS AND PHAGE TAIL-ASSOCIATED
JRNL TITL 2 PROTEIN COMPLEXES SHARE A COMMON EVOLUTIONARY ORIGIN.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 106 4154 2009
JRNL REFN ISSN 0027-8424
JRNL PMID 19251641
JRNL DOI 10.1073/PNAS.0813360106
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 19100
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 983
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1321
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.86
REMARK 3 BIN R VALUE (WORKING SET) : 0.3180
REMARK 3 BIN FREE R VALUE SET COUNT : 89
REMARK 3 BIN FREE R VALUE : 0.4570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2891
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 62
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.57000
REMARK 3 B22 (A**2) : 1.57000
REMARK 3 B33 (A**2) : -2.35000
REMARK 3 B12 (A**2) : 0.78000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.395
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.283
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.218
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.191
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2959 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4001 ; 1.874 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 356 ; 8.515 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 145 ;34.553 ;22.690
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 502 ;20.271 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;17.154 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 439 ; 0.141 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2259 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1203 ; 0.160 ; 0.100
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1957 ; 0.322 ; 0.300
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 203 ; 0.211 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 38 ; 0.111 ; 0.100
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.182 ; 0.500
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1832 ; 2.896 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2894 ; 4.634 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1263 ; 3.105 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1107 ; 4.658 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2P5Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000042008.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-FEB-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97930
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19128
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 15.50
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : 0.09500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 15.70
REMARK 200 R MERGE FOR SHELL (I) : 0.75300
REMARK 200 R SYM FOR SHELL (I) : 0.55800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.5, 21% PEG 3350, PH
REMARK 280 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,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 -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 0.00000
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 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 40.29200
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 40.29200
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 40.29200
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: BIOLOGICAL UNIT APPEARS TO BE TRIMER
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 50070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X
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 BIOMT1 2 -0.500000 -0.866025 0.000000 116.35100
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 58.17550
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 100.76292
REMARK 350 BIOMT3 3 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 X -1
REMARK 465 SER X 0
REMARK 465 LEU X 1
REMARK 465 GLU X 2
REMARK 465 ALA X 3
REMARK 465 LEU X 4
REMARK 465 MET X 5
REMARK 465 ASN X 6
REMARK 465 VAL X 7
REMARK 465 GLN X 8
REMARK 465 PHE X 9
REMARK 465 PHE X 10
REMARK 465 ASP X 11
REMARK 465 HIS X 12
REMARK 465 ALA X 13
REMARK 465 HIS X 14
REMARK 465 PRO X 71
REMARK 465 PRO X 72
REMARK 465 VAL X 73
REMARK 465 GLN X 74
REMARK 465 GLY X 75
REMARK 465 MET X 76
REMARK 465 PRO X 77
REMARK 465 VAL X 78
REMARK 465 GLN X 79
REMARK 465 THR X 80
REMARK 465 HIS X 216
REMARK 465 PRO X 217
REMARK 465 SER X 218
REMARK 465 GLY X 219
REMARK 465 LEU X 220
REMARK 465 PHE X 221
REMARK 465 ASP X 222
REMARK 465 GLY X 223
REMARK 465 GLU X 224
REMARK 465 VAL X 238
REMARK 465 GLU X 239
REMARK 465 LYS X 240
REMARK 465 SER X 241
REMARK 465 VAL X 242
REMARK 465 SER X 243
REMARK 465 THR X 244
REMARK 465 ARG X 245
REMARK 465 ASP X 246
REMARK 465 TYR X 247
REMARK 465 ASN X 248
REMARK 465 TYR X 249
REMARK 465 ARG X 250
REMARK 465 GLU X 251
REMARK 465 ALA X 252
REMARK 465 THR X 253
REMARK 465 ALA X 254
REMARK 465 GLU X 255
REMARK 465 MET X 256
REMARK 465 THR X 257
REMARK 465 THR X 258
REMARK 465 GLY X 259
REMARK 465 GLN X 260
REMARK 465 HIS X 261
REMARK 465 ASP X 262
REMARK 465 ALA X 263
REMARK 465 THR X 264
REMARK 465 GLY X 265
REMARK 465 GLY X 266
REMARK 465 ASP X 267
REMARK 465 ASN X 268
REMARK 465 THR X 269
REMARK 465 THR X 270
REMARK 465 TYR X 271
REMARK 465 GLY X 272
REMARK 465 GLU X 273
REMARK 465 ALA X 274
REMARK 465 TYR X 275
REMARK 465 HIS X 276
REMARK 465 TYR X 277
REMARK 465 ALA X 278
REMARK 465 ASP X 279
REMARK 465 ASN X 280
REMARK 465 PHE X 281
REMARK 465 LEU X 282
REMARK 465 GLN X 283
REMARK 465 GLN X 284
REMARK 465 GLY X 285
REMARK 465 ASP X 286
REMARK 465 LYS X 287
REMARK 465 GLU X 288
REMARK 465 ALA X 289
REMARK 465 ALA X 290
REMARK 465 GLU X 291
REMARK 465 THR X 392
REMARK 465 VAL X 393
REMARK 465 LYS X 394
REMARK 465 ASN X 395
REMARK 465 ASP X 414
REMARK 465 GLN X 429
REMARK 465 SER X 430
REMARK 465 ARG X 431
REMARK 465 PRO X 432
REMARK 465 TYR X 433
REMARK 465 ALA X 434
REMARK 465 GLY X 435
REMARK 465 ASP X 436
REMARK 465 THR X 437
REMARK 465 TYR X 438
REMARK 465 GLY X 439
REMARK 465 LEU X 440
REMARK 465 HIS X 441
REMARK 465 LEU X 442
REMARK 465 PRO X 443
REMARK 465 HIS X 469
REMARK 465 ASP X 470
REMARK 465 SER X 471
REMARK 465 ALA X 472
REMARK 465 HIS X 473
REMARK 465 THR X 474
REMARK 465 ASP X 475
REMARK 465 HIS X 476
REMARK 465 VAL X 477
REMARK 465 THR X 478
REMARK 465 ILE X 479
REMARK 465 GLN X 480
REMARK 465 ASN X 481
REMARK 465 GLU X 482
REMARK 465 GLY X 483
REMARK 465 HIS X 484
REMARK 465 HIS X 485
REMARK 465 HIS X 486
REMARK 465 HIS X 487
REMARK 465 HIS X 488
REMARK 465 HIS X 489
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 LEU X 212 CD1
REMARK 470 ARG X 215 CG CD NE CZ NH1 NH2
REMARK 470 ARG X 415 CG CD NE CZ NH1 NH2
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 PRO X 213 C - N - CA ANGL. DEV. = 29.6 DEGREES
REMARK 500 PRO X 213 C - N - CD ANGL. DEV. = -28.0 DEGREES
REMARK 500 LEU X 358 CA - CB - CG ANGL. DEV. = 17.7 DEGREES
REMARK 500 LEU X 411 CA - CB - CG ANGL. DEV. = 15.7 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 LEU X 29 -73.42 -83.67
REMARK 500 ALA X 53 46.60 -152.80
REMARK 500 MET X 61 -6.06 70.72
REMARK 500 SER X 98 -165.25 -100.67
REMARK 500 PRO X 213 -161.68 53.48
REMARK 500 LEU X 214 119.43 114.29
REMARK 500 ALA X 294 -87.54 128.66
REMARK 500 PHE X 295 -90.03 49.90
REMARK 500 ARG X 354 -49.20 -147.22
REMARK 500 SER X 355 -175.78 59.55
REMARK 500 ALA X 399 131.92 157.05
REMARK 500 LYS X 403 44.73 -70.93
REMARK 500 ASP X 404 -21.19 -154.71
REMARK 500 ARG X 406 59.63 74.11
REMARK 500 LEU X 445 -27.38 -145.60
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 LEU X 212 PRO X 213 62.54
REMARK 500 PRO X 213 LEU X 214 -145.21
REMARK 500 ALA X 294 PHE X 295 56.64
REMARK 500 SER X 355 TYR X 356 -146.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-10105B RELATED DB: TARGETDB
DBREF 2P5Z X 2 481 UNP Q8FED2 Q8FED2_ECOL6 2 481
SEQADV 2P5Z MET X -1 UNP Q8FED2 CLONING ARTIFACT
SEQADV 2P5Z SER X 0 UNP Q8FED2 CLONING ARTIFACT
SEQADV 2P5Z LEU X 1 UNP Q8FED2 CLONING ARTIFACT
SEQADV 2P5Z GLU X 482 UNP Q8FED2 CLONING ARTIFACT
SEQADV 2P5Z GLY X 483 UNP Q8FED2 CLONING ARTIFACT
SEQADV 2P5Z HIS X 484 UNP Q8FED2 CLONING ARTIFACT
SEQADV 2P5Z HIS X 485 UNP Q8FED2 CLONING ARTIFACT
SEQADV 2P5Z HIS X 486 UNP Q8FED2 CLONING ARTIFACT
SEQADV 2P5Z HIS X 487 UNP Q8FED2 CLONING ARTIFACT
SEQADV 2P5Z HIS X 488 UNP Q8FED2 CLONING ARTIFACT
SEQADV 2P5Z HIS X 489 UNP Q8FED2 CLONING ARTIFACT
SEQRES 1 X 491 MET SER LEU GLU ALA LEU MET ASN VAL GLN PHE PHE ASP
SEQRES 2 X 491 HIS ALA HIS HIS LYS LEU LYS ILE ARG GLY LEU GLN SER
SEQRES 3 X 491 PRO VAL ASP VAL LEU THR PHE GLU GLY ARG GLU GLN LEU
SEQRES 4 X 491 SER THR PRO PHE ARG TYR ASP ILE GLN PHE THR SER SER
SEQRES 5 X 491 ASP LYS ALA ILE ALA PRO GLU SER VAL LEU MET GLN ASP
SEQRES 6 X 491 GLY ALA PHE SER LEU THR ALA PRO PRO VAL GLN GLY MET
SEQRES 7 X 491 PRO VAL GLN THR ALA LEU ARG THR LEU HIS GLY VAL ILE
SEQRES 8 X 491 THR GLY PHE LYS HIS LEU SER SER SER GLN ASP GLU ALA
SEQRES 9 X 491 ARG TYR GLU VAL ARG LEU GLU PRO ARG MET ALA LEU LEU
SEQRES 10 X 491 THR ARG SER ARG GLN ASN ALA ILE TYR GLN ASN GLN THR
SEQRES 11 X 491 VAL PRO GLN ILE VAL GLU LYS ILE LEU ARG GLU ARG HIS
SEQRES 12 X 491 GLN MET ARG GLY GLN ASP PHE VAL PHE ASN LEU LYS SER
SEQRES 13 X 491 GLU TYR PRO ALA ARG GLU GLN VAL MET GLN TYR GLY GLU
SEQRES 14 X 491 ASP ASP LEU THR PHE VAL SER ARG LEU LEU SER GLU VAL
SEQRES 15 X 491 GLY ILE TRP PHE ARG PHE ALA THR ASP ALA ARG LEU LYS
SEQRES 16 X 491 ILE GLU VAL ILE GLU PHE TYR ASP ASP GLN SER GLY TYR
SEQRES 17 X 491 GLU ARG GLY LEU THR LEU PRO LEU ARG HIS PRO SER GLY
SEQRES 18 X 491 LEU PHE ASP GLY GLU THR GLU ALA VAL TRP GLY LEU ASN
SEQRES 19 X 491 THR ALA TYR SER VAL VAL GLU LYS SER VAL SER THR ARG
SEQRES 20 X 491 ASP TYR ASN TYR ARG GLU ALA THR ALA GLU MET THR THR
SEQRES 21 X 491 GLY GLN HIS ASP ALA THR GLY GLY ASP ASN THR THR TYR
SEQRES 22 X 491 GLY GLU ALA TYR HIS TYR ALA ASP ASN PHE LEU GLN GLN
SEQRES 23 X 491 GLY ASP LYS GLU ALA ALA GLU SER GLY ALA PHE TYR ALA
SEQRES 24 X 491 ARG ILE ARG HIS GLU ARG TYR LEU ASN GLU GLN ALA ILE
SEQRES 25 X 491 LEU LYS GLY GLN SER THR SER SER LEU LEU MET PRO GLY
SEQRES 26 X 491 LEU GLU ILE LYS VAL GLN GLY ASP ASP ALA PRO ALA VAL
SEQRES 27 X 491 PHE ARG LYS GLY VAL LEU ILE THR GLY VAL THR THR SER
SEQRES 28 X 491 ALA ALA ARG ASP ARG SER TYR GLU LEU THR PHE THR ALA
SEQRES 29 X 491 ILE PRO TYR SER GLU ARG TYR GLY TYR ARG PRO ALA LEU
SEQRES 30 X 491 ILE PRO ARG PRO VAL MET ALA GLY THR LEU PRO ALA ARG
SEQRES 31 X 491 VAL THR SER THR VAL LYS ASN ASP ILE TYR ALA HIS ILE
SEQRES 32 X 491 ASP LYS ASP GLY ARG TYR ARG VAL ASN LEU ASP PHE ASP
SEQRES 33 X 491 ARG ASP THR TRP LYS PRO GLY TYR GLU SER LEU TRP VAL
SEQRES 34 X 491 ARG GLN SER ARG PRO TYR ALA GLY ASP THR TYR GLY LEU
SEQRES 35 X 491 HIS LEU PRO LEU LEU ALA GLY THR GLU VAL SER ILE ALA
SEQRES 36 X 491 PHE GLU GLU GLY ASN PRO ASP ARG PRO TYR ILE ALA GLY
SEQRES 37 X 491 VAL LYS HIS ASP SER ALA HIS THR ASP HIS VAL THR ILE
SEQRES 38 X 491 GLN ASN GLU GLY HIS HIS HIS HIS HIS HIS
FORMUL 2 HOH *62(H2 O)
HELIX 1 1 ALA X 55 VAL X 59 5 5
HELIX 2 2 PRO X 110 ARG X 117 5 8
HELIX 3 3 THR X 128 GLU X 139 1 12
HELIX 4 4 ASP X 168 GLY X 181 1 14
HELIX 5 5 ASP X 202 TYR X 206 5 5
HELIX 6 6 PHE X 295 GLU X 307 1 13
HELIX 7 7 PRO X 334 GLY X 340 1 7
HELIX 8 8 GLU X 456 ASN X 458 5 3
SHEET 1 A 9 LYS X 16 ILE X 19 0
SHEET 2 A 9 ASP X 63 LEU X 68 -1 O ALA X 65 N LYS X 18
SHEET 3 A 9 ARG X 83 SER X 97 -1 O LEU X 85 N PHE X 66
SHEET 4 A 9 ALA X 102 GLU X 109 -1 O GLU X 109 N VAL X 88
SHEET 5 A 9 ARG X 42 SER X 49 -1 N PHE X 47 O TYR X 104
SHEET 6 A 9 ASP X 27 GLN X 36 -1 N THR X 30 O GLN X 46
SHEET 7 A 9 VAL X 341 ALA X 351 -1 O VAL X 346 N GLU X 35
SHEET 8 A 9 LEU X 324 VAL X 328 -1 N ILE X 326 O VAL X 341
SHEET 9 A 9 GLU X 207 LEU X 212 1 N GLU X 207 O GLU X 325
SHEET 1 B10 LYS X 16 ILE X 19 0
SHEET 2 B10 ASP X 63 LEU X 68 -1 O ALA X 65 N LYS X 18
SHEET 3 B10 ARG X 83 SER X 97 -1 O LEU X 85 N PHE X 66
SHEET 4 B10 ALA X 102 GLU X 109 -1 O GLU X 109 N VAL X 88
SHEET 5 B10 ARG X 42 SER X 49 -1 N PHE X 47 O TYR X 104
SHEET 6 B10 ASP X 27 GLN X 36 -1 N THR X 30 O GLN X 46
SHEET 7 B10 VAL X 341 ALA X 351 -1 O VAL X 346 N GLU X 35
SHEET 8 B10 GLU X 357 PRO X 364 -1 O ILE X 363 N LEU X 342
SHEET 9 B10 ALA X 309 SER X 315 -1 N SER X 315 O LEU X 358
SHEET 10 B10 VAL X 228 TYR X 235 -1 N ASN X 232 O LYS X 312
SHEET 1 C 2 ALA X 122 GLN X 127 0
SHEET 2 C 2 ARG X 159 GLN X 164 -1 O ARG X 159 N GLN X 127
SHEET 1 D 3 PHE X 148 ASN X 151 0
SHEET 2 D 3 ILE X 194 TYR X 200 1 O PHE X 199 N VAL X 149
SHEET 3 D 3 TRP X 183 ASP X 189 -1 N TRP X 183 O TYR X 200
SHEET 1 E 5 SER X 424 VAL X 427 0
SHEET 2 E 5 TYR X 407 ASN X 410 -1 N VAL X 409 O LEU X 425
SHEET 3 E 5 LEU X 385 VAL X 389 -1 N ARG X 388 O ASN X 410
SHEET 4 E 5 GLU X 449 PHE X 454 -1 O ILE X 452 N LEU X 385
SHEET 5 E 5 PRO X 462 VAL X 467 -1 O ALA X 465 N SER X 451
CISPEP 1 ARG X 208 GLY X 209 0 -1.95
CISPEP 2 LEU X 214 ARG X 215 0 -17.64
CISPEP 3 SER X 292 GLY X 293 0 3.37
CISPEP 4 GLY X 293 ALA X 294 0 -16.52
CISPEP 5 GLY X 330 ASP X 331 0 -6.23
CISPEP 6 ASP X 396 ILE X 397 0 9.42
CISPEP 7 GLY X 405 ARG X 406 0 -1.63
CISPEP 8 LEU X 444 LEU X 445 0 15.75
CISPEP 9 LEU X 445 ALA X 446 0 -10.59
CISPEP 10 ALA X 465 GLY X 466 0 -14.84
CRYST1 116.351 116.351 80.584 90.00 90.00 120.00 P 63 6
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 0.008595 0.004962 0.000000 0.00000
SCALE2 0.000000 0.009924 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012409 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
