HEADER CHAPERONE 11-JUL-17 5WEZ
TITLE STRUCTURE OF THE TIR-CEST EFFECTOR-CHAPERONE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TIR CHAPERONE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 2-138;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TRANSLOCATED INTIMIN RECEPTOR TIR;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: UNP RESIDUES 32-80;
COMPND 10 SYNONYM: SECRETED EFFECTOR PROTEIN TIR;
COMPND 11 ENGINEERED: YES;
COMPND 12 OTHER_DETAILS: N-TERMINAL HIS6-TAG
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI O127:H6 (STRAIN E2348/69 /
SOURCE 3 EPEC);
SOURCE 4 ORGANISM_TAXID: 574521;
SOURCE 5 STRAIN: E2348/69 / EPEC;
SOURCE 6 GENE: CEST, E2348C_3940;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: CODON PLUS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCOLADUET-1;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI O127:H6 (STRAIN E2348/69 /
SOURCE 14 EPEC);
SOURCE 15 ORGANISM_TAXID: 574521;
SOURCE 16 STRAIN: E2348/69 / EPEC;
SOURCE 17 GENE: TIR, ESPE, E2348C_3941;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: CODON PLUS;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PCOLADUET-1
KEYWDS EFFECTOR, COMPLEX, SECRETION, TRANSLOCATION, CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.LITTLE,B.K.COOMBES
REVDAT 3 04-OCT-23 5WEZ 1 REMARK
REVDAT 2 29-AUG-18 5WEZ 1 JRNL
REVDAT 1 11-JUL-18 5WEZ 0
JRNL AUTH D.J.LITTLE,B.K.COOMBES
JRNL TITL MOLECULAR BASIS FOR CEST RECOGNITION OF TYPE III SECRETION
JRNL TITL 2 EFFECTORS IN ENTEROPATHOGENIC ESCHERICHIA COLI.
JRNL REF PLOS PATHOG. V. 14 07224 2018
JRNL REFN ESSN 1553-7374
JRNL PMID 30118511
JRNL DOI 10.1371/JOURNAL.PPAT.1007224
REMARK 2
REMARK 2 RESOLUTION. 2.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.99
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 5457
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 279
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 58.0021 - 3.4458 0.99 2621 152 0.1887 0.2442
REMARK 3 2 3.4458 - 2.7350 1.00 2557 127 0.3104 0.3185
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.380
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 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 1193
REMARK 3 ANGLE : 1.343 1625
REMARK 3 CHIRALITY : 0.058 189
REMARK 3 PLANARITY : 0.008 211
REMARK 3 DIHEDRAL : 15.811 710
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 16 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8443 36.7357 17.6135
REMARK 3 T TENSOR
REMARK 3 T11: 1.3591 T22: 1.2553
REMARK 3 T33: 1.1710 T12: 0.5508
REMARK 3 T13: 0.2251 T23: 0.3307
REMARK 3 L TENSOR
REMARK 3 L11: 1.2027 L22: 8.9308
REMARK 3 L33: 5.5862 L12: 1.1724
REMARK 3 L13: 2.2305 L23: -1.1832
REMARK 3 S TENSOR
REMARK 3 S11: 1.4802 S12: 1.6017 S13: 2.2527
REMARK 3 S21: -0.8283 S22: -1.1317 S23: -1.0002
REMARK 3 S31: -1.3566 S32: -1.7765 S33: -0.2390
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 17 THROUGH 54 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.4142 26.1702 20.3893
REMARK 3 T TENSOR
REMARK 3 T11: 1.1348 T22: 1.0171
REMARK 3 T33: 1.0424 T12: 0.3160
REMARK 3 T13: 0.0217 T23: -0.1109
REMARK 3 L TENSOR
REMARK 3 L11: 8.1043 L22: 8.3586
REMARK 3 L33: 7.2502 L12: 3.4784
REMARK 3 L13: 1.9322 L23: -5.7517
REMARK 3 S TENSOR
REMARK 3 S11: 0.6024 S12: 1.6381 S13: 0.4662
REMARK 3 S21: -1.9841 S22: -1.0377 S23: 0.6868
REMARK 3 S31: 0.8058 S32: -1.2392 S33: 0.4669
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 55 THROUGH 63 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.7785 4.4830 29.0293
REMARK 3 T TENSOR
REMARK 3 T11: 2.1660 T22: 1.4222
REMARK 3 T33: 1.9444 T12: -0.2446
REMARK 3 T13: -0.4391 T23: -0.2439
REMARK 3 L TENSOR
REMARK 3 L11: 2.4044 L22: 5.3824
REMARK 3 L33: 4.9898 L12: -3.5994
REMARK 3 L13: 3.4657 L23: -5.1852
REMARK 3 S TENSOR
REMARK 3 S11: 1.8072 S12: -1.1464 S13: 1.2363
REMARK 3 S21: -0.4698 S22: 2.7017 S23: 6.3453
REMARK 3 S31: 2.2838 S32: 2.5118 S33: -2.8150
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 64 THROUGH 105 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.3461 18.5601 33.1815
REMARK 3 T TENSOR
REMARK 3 T11: 0.8368 T22: 0.6781
REMARK 3 T33: 0.9467 T12: 0.0841
REMARK 3 T13: 0.2343 T23: -0.1776
REMARK 3 L TENSOR
REMARK 3 L11: 1.8463 L22: 8.3630
REMARK 3 L33: 9.5319 L12: -3.9652
REMARK 3 L13: 2.3109 L23: -4.7266
REMARK 3 S TENSOR
REMARK 3 S11: 0.3137 S12: 0.1046 S13: 0.0397
REMARK 3 S21: -0.9072 S22: -1.0160 S23: 0.3504
REMARK 3 S31: 1.5577 S32: -0.3386 S33: 0.5856
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 106 THROUGH 129 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.2538 18.7890 26.2017
REMARK 3 T TENSOR
REMARK 3 T11: 1.0877 T22: 0.8563
REMARK 3 T33: 1.4749 T12: 0.3634
REMARK 3 T13: 0.3672 T23: -0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 5.9379 L22: 1.3163
REMARK 3 L33: 6.3036 L12: -2.7782
REMARK 3 L13: 1.3843 L23: -1.0611
REMARK 3 S TENSOR
REMARK 3 S11: 0.6807 S12: 0.8479 S13: -0.4417
REMARK 3 S21: -3.2160 S22: -2.4475 S23: -1.2561
REMARK 3 S31: 1.6043 S32: 0.4792 S33: 1.4312
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 35 THROUGH 43 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.4338 26.5233 12.1330
REMARK 3 T TENSOR
REMARK 3 T11: 1.4423 T22: 1.8470
REMARK 3 T33: 1.3458 T12: 0.5231
REMARK 3 T13: 0.3143 T23: 0.0628
REMARK 3 L TENSOR
REMARK 3 L11: 6.4801 L22: 3.4324
REMARK 3 L33: 9.7097 L12: 2.2597
REMARK 3 L13: 6.5898 L23: 5.1245
REMARK 3 S TENSOR
REMARK 3 S11: 1.0860 S12: 4.1876 S13: 3.1403
REMARK 3 S21: -2.2735 S22: -2.2992 S23: 0.4889
REMARK 3 S31: -0.4035 S32: 0.6882 S33: -0.0607
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 44 THROUGH 48 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2172 21.4921 14.2823
REMARK 3 T TENSOR
REMARK 3 T11: 2.1010 T22: 1.9477
REMARK 3 T33: 0.8660 T12: 0.9766
REMARK 3 T13: -0.4098 T23: 0.0259
REMARK 3 L TENSOR
REMARK 3 L11: 7.3077 L22: 5.5604
REMARK 3 L33: 9.8216 L12: 6.3702
REMARK 3 L13: -8.1951 L23: -7.0746
REMARK 3 S TENSOR
REMARK 3 S11: 0.9929 S12: 2.9801 S13: -0.9788
REMARK 3 S21: -2.9999 S22: 0.8243 S23: 1.4204
REMARK 3 S31: 3.5134 S32: -0.1774 S33: -1.9219
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 49 THROUGH 53 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6886 21.8548 11.5081
REMARK 3 T TENSOR
REMARK 3 T11: 1.7574 T22: 1.2875
REMARK 3 T33: 1.5188 T12: 0.0153
REMARK 3 T13: -0.2585 T23: 0.0754
REMARK 3 L TENSOR
REMARK 3 L11: 6.0945 L22: 2.4377
REMARK 3 L33: 7.3082 L12: -1.9759
REMARK 3 L13: 2.1490 L23: -2.7948
REMARK 3 S TENSOR
REMARK 3 S11: 1.0649 S12: 0.1296 S13: 0.4628
REMARK 3 S21: 0.3833 S22: -0.9936 S23: 1.2473
REMARK 3 S31: 2.3106 S32: 0.6785 S33: -0.3851
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 65 THROUGH 75 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.1220 19.0644 23.8533
REMARK 3 T TENSOR
REMARK 3 T11: 1.6615 T22: 2.3513
REMARK 3 T33: 1.4425 T12: 0.0094
REMARK 3 T13: -0.4067 T23: -0.5632
REMARK 3 L TENSOR
REMARK 3 L11: 4.8918 L22: 4.5730
REMARK 3 L33: 6.6907 L12: -3.9197
REMARK 3 L13: -3.8750 L23: 3.7765
REMARK 3 S TENSOR
REMARK 3 S11: -3.9986 S12: -2.7931 S13: 0.8744
REMARK 3 S21: 2.0462 S22: 2.6741 S23: 1.5400
REMARK 3 S31: 1.5113 S32: -0.4699 S33: 0.6825
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 5WEZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1000228884.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JAN-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08B1-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.980
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM 7.1.1
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 5461
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.740
REMARK 200 RESOLUTION RANGE LOW (A) : 57.990
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 0.80000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: 1K3E
REMARK 200
REMARK 200 REMARK: RHOMBOHEDRONS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 MM TRIS-HCL PH 7.5, 0.2 M MGCL2,
REMARK 280 17% (W/V) PEG3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 295K
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 50.47333
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 25.23667
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 25.23667
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 50.47333
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: 2320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 MET A 0
REMARK 465 GLN A 130
REMARK 465 GLY A 131
REMARK 465 ILE A 132
REMARK 465 THR A 133
REMARK 465 LEU A 134
REMARK 465 GLU A 135
REMARK 465 ASN A 136
REMARK 465 GLU A 137
REMARK 465 HIS A 138
REMARK 465 MET B 18
REMARK 465 GLY B 19
REMARK 465 SER B 20
REMARK 465 SER B 21
REMARK 465 HIS B 22
REMARK 465 HIS B 23
REMARK 465 HIS B 24
REMARK 465 HIS B 25
REMARK 465 HIS B 26
REMARK 465 HIS B 27
REMARK 465 SER B 28
REMARK 465 GLN B 29
REMARK 465 ASP B 30
REMARK 465 PRO B 31
REMARK 465 GLY B 32
REMARK 465 GLY B 33
REMARK 465 THR B 34
REMARK 465 ARG B 54
REMARK 465 ASN B 55
REMARK 465 SER B 56
REMARK 465 MET B 57
REMARK 465 ALA B 58
REMARK 465 ASP B 59
REMARK 465 SER B 60
REMARK 465 VAL B 61
REMARK 465 ASP B 62
REMARK 465 SER B 63
REMARK 465 ARG B 64
REMARK 465 LEU B 76
REMARK 465 ALA B 77
REMARK 465 ALA B 78
REMARK 465 ALA B 79
REMARK 465 THR B 80
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 ARG A 11 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 25 CG CD OE1 OE2
REMARK 470 LYS A 57 CG CD CE NZ
REMARK 470 ASP A 61 CG OD1 OD2
REMARK 470 GLU A 68 CG CD OE1 OE2
REMARK 470 GLN A 91 CG CD OE1 NE2
REMARK 470 GLU A 107 CG CD OE1 OE2
REMARK 470 HIS A 128 CG ND1 CD2 CE1 NE2
REMARK 470 ASN A 129 CG OD1 ND2
REMARK 470 LEU B 37 CG CD1 CD2
REMARK 470 ARG B 47 CG CD NE CZ NH1 NH2
REMARK 470 PHE B 50 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU B 53 CG CD1 CD2
REMARK 470 ASP B 65 CG OD1 OD2
REMARK 470 ARG B 75 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 OE1 GLU A 114 NZ LYS A 118 2.15
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 ASP A 34 30.81 71.39
REMARK 500 GLU A 35 8.43 51.40
REMARK 500 PRO A 63 47.60 -80.21
REMARK 500 GLN A 91 27.04 49.61
REMARK 500 LEU B 44 67.70 -108.56
REMARK 500 THR B 71 144.41 -175.08
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5WEZ A 2 138 UNP P21244 CEST_ECO27 2 138
DBREF 5WEZ B 32 80 UNP B7UM99 TIR_ECO27 32 80
SEQADV 5WEZ MET A 0 UNP P21244 INITIATING METHIONINE
SEQADV 5WEZ ALA A 1 UNP P21244 EXPRESSION TAG
SEQADV 5WEZ MET B 18 UNP B7UM99 INITIATING METHIONINE
SEQADV 5WEZ GLY B 19 UNP B7UM99 EXPRESSION TAG
SEQADV 5WEZ SER B 20 UNP B7UM99 EXPRESSION TAG
SEQADV 5WEZ SER B 21 UNP B7UM99 EXPRESSION TAG
SEQADV 5WEZ HIS B 22 UNP B7UM99 EXPRESSION TAG
SEQADV 5WEZ HIS B 23 UNP B7UM99 EXPRESSION TAG
SEQADV 5WEZ HIS B 24 UNP B7UM99 EXPRESSION TAG
SEQADV 5WEZ HIS B 25 UNP B7UM99 EXPRESSION TAG
SEQADV 5WEZ HIS B 26 UNP B7UM99 EXPRESSION TAG
SEQADV 5WEZ HIS B 27 UNP B7UM99 EXPRESSION TAG
SEQADV 5WEZ SER B 28 UNP B7UM99 EXPRESSION TAG
SEQADV 5WEZ GLN B 29 UNP B7UM99 EXPRESSION TAG
SEQADV 5WEZ ASP B 30 UNP B7UM99 EXPRESSION TAG
SEQADV 5WEZ PRO B 31 UNP B7UM99 EXPRESSION TAG
SEQRES 1 A 139 MET ALA SER SER ARG SER GLU LEU LEU LEU ASP ARG PHE
SEQRES 2 A 139 ALA GLU LYS ILE GLY VAL GLY SER ILE SER PHE ASN GLU
SEQRES 3 A 139 ASN ARG LEU CYS SER PHE ALA ILE ASP GLU ILE TYR TYR
SEQRES 4 A 139 ILE SER LEU SER ASP ALA ASN ASP GLU TYR MET MET ILE
SEQRES 5 A 139 TYR GLY VAL CYS GLY LYS PHE PRO THR ASP ASN PRO ASN
SEQRES 6 A 139 PHE ALA LEU GLU ILE LEU ASN ALA ASN LEU TRP PHE ALA
SEQRES 7 A 139 GLU ASN GLY GLY PRO TYR LEU CYS TYR GLU SER GLY ALA
SEQRES 8 A 139 GLN SER LEU LEU LEU ALA LEU ARG PHE PRO LEU ASP ASP
SEQRES 9 A 139 ALA THR PRO GLU LYS LEU GLU ASN GLU ILE GLU VAL VAL
SEQRES 10 A 139 VAL LYS SER MET GLU ASN LEU TYR LEU VAL LEU HIS ASN
SEQRES 11 A 139 GLN GLY ILE THR LEU GLU ASN GLU HIS
SEQRES 1 B 63 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 B 63 PRO GLY GLY THR GLY HIS LEU ILE SER SER THR GLY ALA
SEQRES 3 B 63 LEU GLY SER ARG SER LEU PHE SER PRO LEU ARG ASN SER
SEQRES 4 B 63 MET ALA ASP SER VAL ASP SER ARG ASP ILE PRO GLY LEU
SEQRES 5 B 63 PRO THR ASN PRO SER ARG LEU ALA ALA ALA THR
HELIX 1 AA1 SER A 3 GLY A 17 1 15
HELIX 2 AA2 PHE A 65 GLY A 80 1 16
HELIX 3 AA3 THR A 105 LEU A 127 1 23
SHEET 1 AA1 7 TYR A 83 TYR A 86 0
SHEET 2 AA1 7 SER A 92 PRO A 100 -1 O ALA A 96 N TYR A 83
SHEET 3 AA1 7 TYR A 48 LYS A 57 -1 N MET A 49 O PHE A 99
SHEET 4 AA1 7 TYR A 37 SER A 42 -1 N TYR A 38 O VAL A 54
SHEET 5 AA1 7 LEU A 28 ILE A 33 -1 N CYS A 29 O LEU A 41
SHEET 6 AA1 7 SER B 48 PHE B 50 -1 O PHE B 50 N ALA A 32
SHEET 7 AA1 7 HIS B 36 LEU B 37 -1 N HIS B 36 O LEU B 49
CRYST1 66.960 66.960 75.710 90.00 90.00 120.00 P 32 2 1 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 0.014934 0.008622 0.000000 0.00000
SCALE2 0.000000 0.017245 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013208 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
