HEADER PROTEIN BINDING 26-AUG-13 4MEE
TITLE CRYSTAL STRUCTURE OF THE TRANSPORT UNIT OF THE AUTOTRANSPORTER AIDA-I
TITLE 2 FROM ESCHERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIFFUSE ADHERENCE ADHESIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (UNP RESIDUES 841-1287);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: AIDA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: UT5600;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PJM007
KEYWDS BETA BARREL, OUTER MEMBRANE PROTEIN, AUTOTRANSPORTER, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR I.GAWARZEWSKI,B.TSCHAPEK,A.HOEPPNER,S.H.SMITS,J.JOSE,L.SCHMITT
REVDAT 3 28-FEB-24 4MEE 1 SEQADV
REVDAT 2 23-JUL-14 4MEE 1 JRNL
REVDAT 1 04-JUN-14 4MEE 0
JRNL AUTH I.GAWARZEWSKI,F.DIMAIO,E.WINTERER,B.TSCHAPEK,S.H.SMITS,
JRNL AUTH 2 J.JOSE,L.SCHMITT
JRNL TITL CRYSTAL STRUCTURE OF THE TRANSPORT UNIT OF THE
JRNL TITL 2 AUTOTRANSPORTER ADHESIN INVOLVED IN DIFFUSE ADHERENCE FROM
JRNL TITL 3 ESCHERICHIA COLI.
JRNL REF J.STRUCT.BIOL. V. 187 20 2014
JRNL REFN ISSN 1047-8477
JRNL PMID 24841284
JRNL DOI 10.1016/J.JSB.2014.05.003
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 9183
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) : 0.251
REMARK 3 R VALUE (WORKING SET) : 0.248
REMARK 3 FREE R VALUE : 0.306
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 493
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 679
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.61
REMARK 3 BIN R VALUE (WORKING SET) : 0.3340
REMARK 3 BIN FREE R VALUE SET COUNT : 33
REMARK 3 BIN FREE R VALUE : 0.3480
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2234
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.09000
REMARK 3 B22 (A**2) : 3.81000
REMARK 3 B33 (A**2) : -0.72000
REMARK 3 B12 (A**2) : 0.00000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.466
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.387
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 47.436
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.902
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.837
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2287 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3105 ; 1.648 ; 1.911
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 299 ; 5.274 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 106 ;42.089 ;25.755
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 333 ;25.414 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;24.060 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 335 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1781 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1208 ; 0.797 ; 4.070
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1503 ; 1.162 ; 6.102
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1079 ; 1.129 ; 4.152
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): 2287 ; 3.698 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2243 ;10.036 ; 5.000
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 962 A 1286
REMARK 3 ORIGIN FOR THE GROUP (A): -7.7413 5.7019 -18.3516
REMARK 3 T TENSOR
REMARK 3 T11: 0.0327 T22: 0.1091
REMARK 3 T33: 0.0414 T12: 0.0182
REMARK 3 T13: -0.0059 T23: -0.0361
REMARK 3 L TENSOR
REMARK 3 L11: 1.9693 L22: 2.2289
REMARK 3 L33: 1.7715 L12: 1.1260
REMARK 3 L13: 0.6228 L23: 1.1627
REMARK 3 S TENSOR
REMARK 3 S11: -0.0705 S12: 0.3151 S13: -0.1431
REMARK 3 S21: -0.0283 S22: 0.1580 S23: -0.0853
REMARK 3 S31: -0.0117 S32: 0.0900 S33: -0.0875
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: NULL
REMARK 4
REMARK 4 4MEE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-13.
REMARK 100 THE DEPOSITION ID IS D_1000081805.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-DEC-12
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 : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : NI MIRROR + NI FILTER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9173
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3
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) : 3.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.44600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: ROSETTA
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CACODYLATE, AND 27.5 %
REMARK 280 (V/V) PEG 2000 MME, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 273K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 20.16500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.02500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.92500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.02500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.16500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.92500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 HIS A 818
REMARK 465 HIS A 819
REMARK 465 HIS A 820
REMARK 465 HIS A 821
REMARK 465 HIS A 822
REMARK 465 HIS A 823
REMARK 465 SER A 824
REMARK 465 ARG A 825
REMARK 465 ARG A 826
REMARK 465 SER A 827
REMARK 465 PRO A 828
REMARK 465 GLU A 829
REMARK 465 TYR A 830
REMARK 465 PHE A 831
REMARK 465 LYS A 832
REMARK 465 GLY A 833
REMARK 465 PRO A 834
REMARK 465 PRO A 835
REMARK 465 SER A 836
REMARK 465 PRO A 837
REMARK 465 ARG A 838
REMARK 465 SER A 839
REMARK 465 LEU A 840
REMARK 465 ASN A 841
REMARK 465 PRO A 842
REMARK 465 THR A 843
REMARK 465 LYS A 844
REMARK 465 GLU A 845
REMARK 465 SER A 846
REMARK 465 ALA A 847
REMARK 465 GLY A 848
REMARK 465 ASN A 849
REMARK 465 THR A 850
REMARK 465 LEU A 851
REMARK 465 THR A 852
REMARK 465 VAL A 853
REMARK 465 SER A 854
REMARK 465 ASN A 855
REMARK 465 TYR A 856
REMARK 465 THR A 857
REMARK 465 GLY A 858
REMARK 465 THR A 859
REMARK 465 PRO A 860
REMARK 465 GLY A 861
REMARK 465 SER A 862
REMARK 465 VAL A 863
REMARK 465 ILE A 864
REMARK 465 SER A 865
REMARK 465 LEU A 866
REMARK 465 GLY A 867
REMARK 465 GLY A 868
REMARK 465 VAL A 869
REMARK 465 LEU A 870
REMARK 465 GLU A 871
REMARK 465 GLY A 872
REMARK 465 ASP A 873
REMARK 465 ASN A 874
REMARK 465 SER A 875
REMARK 465 LEU A 876
REMARK 465 THR A 877
REMARK 465 ASP A 878
REMARK 465 ARG A 879
REMARK 465 LEU A 880
REMARK 465 VAL A 881
REMARK 465 VAL A 882
REMARK 465 LYS A 883
REMARK 465 GLY A 884
REMARK 465 ASN A 885
REMARK 465 THR A 886
REMARK 465 SER A 887
REMARK 465 GLY A 888
REMARK 465 GLN A 889
REMARK 465 SER A 890
REMARK 465 ASP A 891
REMARK 465 ILE A 892
REMARK 465 VAL A 893
REMARK 465 TYR A 894
REMARK 465 VAL A 895
REMARK 465 ASN A 896
REMARK 465 GLU A 897
REMARK 465 ASP A 898
REMARK 465 GLY A 899
REMARK 465 SER A 900
REMARK 465 GLY A 901
REMARK 465 GLY A 902
REMARK 465 GLN A 903
REMARK 465 THR A 904
REMARK 465 ARG A 905
REMARK 465 ASP A 906
REMARK 465 GLY A 907
REMARK 465 ILE A 908
REMARK 465 ASN A 909
REMARK 465 ILE A 910
REMARK 465 ILE A 911
REMARK 465 SER A 912
REMARK 465 VAL A 913
REMARK 465 GLU A 914
REMARK 465 GLY A 915
REMARK 465 ASN A 916
REMARK 465 SER A 917
REMARK 465 ASP A 918
REMARK 465 ALA A 919
REMARK 465 GLU A 920
REMARK 465 PHE A 921
REMARK 465 SER A 922
REMARK 465 LEU A 923
REMARK 465 LYS A 924
REMARK 465 ASN A 925
REMARK 465 ARG A 926
REMARK 465 VAL A 927
REMARK 465 VAL A 928
REMARK 465 ALA A 929
REMARK 465 GLY A 930
REMARK 465 ALA A 931
REMARK 465 TYR A 932
REMARK 465 ASP A 933
REMARK 465 TYR A 934
REMARK 465 THR A 935
REMARK 465 LEU A 936
REMARK 465 GLN A 937
REMARK 465 LYS A 938
REMARK 465 GLY A 939
REMARK 465 ASN A 940
REMARK 465 GLU A 941
REMARK 465 SER A 942
REMARK 465 GLY A 943
REMARK 465 THR A 944
REMARK 465 ASP A 945
REMARK 465 ASN A 946
REMARK 465 LYS A 947
REMARK 465 GLY A 948
REMARK 465 TRP A 949
REMARK 465 TYR A 950
REMARK 465 LEU A 951
REMARK 465 THR A 952
REMARK 465 SER A 953
REMARK 465 HIS A 954
REMARK 465 LEU A 955
REMARK 465 PRO A 956
REMARK 465 THR A 957
REMARK 465 SER A 958
REMARK 465 ASP A 959
REMARK 465 THR A 960
REMARK 465 ARG A 961
REMARK 465 PHE A 991
REMARK 465 ARG A 992
REMARK 465 ALA A 993
REMARK 465 MET A 994
REMARK 465 SER A 995
REMARK 465 ASP A 996
REMARK 465 ASN A 997
REMARK 465 THR A 998
REMARK 465 GLN A 999
REMARK 465 PRO A 1000
REMARK 465 GLU A 1001
REMARK 465 SER A 1002
REMARK 465 ALA A 1003
REMARK 465 GLY A 1148
REMARK 465 THR A 1202
REMARK 465 LEU A 1203
REMARK 465 ASP A 1204
REMARK 465 LYS A 1205
REMARK 465 ASP A 1206
REMARK 465 THR A 1207
REMARK 465 GLY A 1208
REMARK 465 ARG A 1209
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 LYS A 989 CG CD CE NZ
REMARK 470 GLN A 990 CG CD OE1 NE2
REMARK 470 ARG A1013 CG CD NE CZ NH1 NH2
REMARK 470 PHE A1041 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 HIS A1042 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A1045 CG CD OE1 NE2
REMARK 470 LYS A1061 CG CD CE NZ
REMARK 470 TYR A1067 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A1071 CG CD CE NZ
REMARK 470 ARG A1074 CG CD NE CZ NH1 NH2
REMARK 470 ASP A1116 CG OD1 OD2
REMARK 470 TRP A1143 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A1143 CZ3 CH2
REMARK 470 GLU A1147 CG CD OE1 OE2
REMARK 470 LYS A1184 CG CD CE NZ
REMARK 470 TRP A1197 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A1197 CZ3 CH2
REMARK 470 LYS A1200 CG CD CE NZ
REMARK 470 SER A1201 OG
REMARK 470 GLU A1210 CG CD OE1 OE2
REMARK 470 PHE A1211 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP A1232 CG OD1 OD2
REMARK 470 LYS A1283 CG CD CE NZ
REMARK 470 SER A1285 OG
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 OD2 ASP A 1020 OD1 ASN A 1023 1.61
REMARK 500 NZ LYS A 1063 CD1 ILE A 1065 2.01
REMARK 500 CE2 TYR A 1106 NE1 TRP A 1108 2.09
REMARK 500 OD1 ASN A 1175 OG1 THR A 1177 2.14
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 A1125 CA - CB - CG ANGL. DEV. = 17.7 DEGREES
REMARK 500 LEU A1258 CA - CB - CG ANGL. DEV. = 15.6 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 A 986 -5.15 78.85
REMARK 500 LYS A1040 68.49 -151.28
REMARK 500 ASN A1094 13.05 82.60
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4MEE A 840 1286 UNP D7PPP4 D7PPP4_ECOLX 841 1287
SEQADV 4MEE HIS A 818 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE HIS A 819 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE HIS A 820 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE HIS A 821 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE HIS A 822 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE HIS A 823 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE SER A 824 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE ARG A 825 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE ARG A 826 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE SER A 827 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE PRO A 828 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE GLU A 829 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE TYR A 830 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE PHE A 831 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE LYS A 832 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE GLY A 833 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE PRO A 834 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE PRO A 835 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE SER A 836 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE PRO A 837 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE ARG A 838 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE SER A 839 UNP D7PPP4 EXPRESSION TAG
SEQADV 4MEE THR A 975 UNP D7PPP4 ALA 976 CONFLICT
SEQADV 4MEE ARG A 1008 UNP D7PPP4 LYS 1009 CONFLICT
SEQADV 4MEE SER A 1212 UNP D7PPP4 ARG 1213 CONFLICT
SEQRES 1 A 469 HIS HIS HIS HIS HIS HIS SER ARG ARG SER PRO GLU TYR
SEQRES 2 A 469 PHE LYS GLY PRO PRO SER PRO ARG SER LEU ASN PRO THR
SEQRES 3 A 469 LYS GLU SER ALA GLY ASN THR LEU THR VAL SER ASN TYR
SEQRES 4 A 469 THR GLY THR PRO GLY SER VAL ILE SER LEU GLY GLY VAL
SEQRES 5 A 469 LEU GLU GLY ASP ASN SER LEU THR ASP ARG LEU VAL VAL
SEQRES 6 A 469 LYS GLY ASN THR SER GLY GLN SER ASP ILE VAL TYR VAL
SEQRES 7 A 469 ASN GLU ASP GLY SER GLY GLY GLN THR ARG ASP GLY ILE
SEQRES 8 A 469 ASN ILE ILE SER VAL GLU GLY ASN SER ASP ALA GLU PHE
SEQRES 9 A 469 SER LEU LYS ASN ARG VAL VAL ALA GLY ALA TYR ASP TYR
SEQRES 10 A 469 THR LEU GLN LYS GLY ASN GLU SER GLY THR ASP ASN LYS
SEQRES 11 A 469 GLY TRP TYR LEU THR SER HIS LEU PRO THR SER ASP THR
SEQRES 12 A 469 ARG GLN TYR ARG PRO GLU ASN GLY SER TYR ALA THR ASN
SEQRES 13 A 469 MET THR LEU ALA ASN SER LEU PHE LEU MET ASP LEU ASN
SEQRES 14 A 469 GLU ARG LYS GLN PHE ARG ALA MET SER ASP ASN THR GLN
SEQRES 15 A 469 PRO GLU SER ALA SER VAL TRP MET ARG ILE THR GLY GLY
SEQRES 16 A 469 ARG SER SER GLY LYS LEU ASN ASP GLY GLN ASN LYS THR
SEQRES 17 A 469 THR THR ASN GLN PHE ILE ASN GLN LEU GLY GLY ASP ILE
SEQRES 18 A 469 TYR LYS PHE HIS ALA GLU GLN LEU GLY ASP PHE THR LEU
SEQRES 19 A 469 GLY ILE MET GLY GLY TYR ALA ASN ALA LYS GLY LYS THR
SEQRES 20 A 469 ILE ASN TYR THR SER ASN LYS ALA ALA ARG ASN THR LEU
SEQRES 21 A 469 ASP GLY TYR SER VAL GLY VAL TYR GLY THR TRP TYR GLN
SEQRES 22 A 469 ASN GLY GLU ASN ALA THR GLY LEU PHE ALA GLU THR TRP
SEQRES 23 A 469 MET GLN TYR ASN TRP PHE ASN ALA SER VAL LYS GLY ASP
SEQRES 24 A 469 GLY LEU GLU GLU GLU LYS TYR ASN LEU ASN GLY LEU THR
SEQRES 25 A 469 ALA SER ALA GLY GLY GLY TYR ASN LEU ASN VAL HIS THR
SEQRES 26 A 469 TRP THR SER PRO GLU GLY ILE THR GLY GLU PHE TRP LEU
SEQRES 27 A 469 GLN PRO HIS LEU GLN ALA VAL TRP MET GLY VAL THR PRO
SEQRES 28 A 469 ASP THR HIS GLN GLU ASP ASN GLY THR VAL VAL GLN GLY
SEQRES 29 A 469 ALA GLY LYS ASN ASN ILE GLN THR LYS ALA GLY ILE ARG
SEQRES 30 A 469 ALA SER TRP LYS VAL LYS SER THR LEU ASP LYS ASP THR
SEQRES 31 A 469 GLY ARG GLU PHE SER PRO TYR ILE GLU ALA ASN TRP ILE
SEQRES 32 A 469 HIS ASN THR HIS GLU PHE GLY VAL LYS MET SER ASP ASP
SEQRES 33 A 469 SER GLN LEU LEU SER GLY SER ARG ASN GLN GLY GLU ILE
SEQRES 34 A 469 LYS THR GLY ILE GLU GLY VAL ILE THR GLN ASN LEU SER
SEQRES 35 A 469 VAL ASN GLY GLY VAL ALA TYR GLN ALA GLY GLY HIS GLY
SEQRES 36 A 469 SER ASN ALA ILE SER GLY ALA LEU GLY ILE LYS TYR SER
SEQRES 37 A 469 PHE
HELIX 1 1 PRO A 965 LEU A 980 1 16
SHEET 1 A14 HIS A1042 ALA A1043 0
SHEET 2 A14 GLY A1047 ASN A1066 -1 O GLY A1047 N ALA A1043
SHEET 3 A14 ALA A1072 TYR A1089 -1 O ALA A1073 N THR A1064
SHEET 4 A14 GLY A1097 GLY A1115 -1 O LYS A1114 N ARG A1074
SHEET 5 A14 GLU A1120 THR A1144 -1 O GLY A1127 N ASN A1107
SHEET 6 A14 THR A1150 PRO A1168 -1 O TRP A1163 N ALA A1130
SHEET 7 A14 ILE A1187 LYS A1200 -1 O LYS A1190 N GLN A1160
SHEET 8 A14 TYR A1214 ASN A1222 -1 O ILE A1215 N ALA A1195
SHEET 9 A14 ASN A1242 VAL A1253 -1 O LYS A1247 N GLU A1216
SHEET 10 A14 LEU A1258 ALA A1268 -1 O VAL A1264 N THR A1248
SHEET 11 A14 ASN A1274 TYR A1284 -1 O SER A1277 N ALA A1265
SHEET 12 A14 VAL A1005 LYS A1017 -1 N MET A1007 O ILE A1282
SHEET 13 A14 ASN A1023 TYR A1039 -1 O THR A1025 N GLY A1016
SHEET 14 A14 GLY A1047 ASN A1066 -1 O GLY A1055 N LEU A1034
SHEET 1 B 4 HIS A1171 GLN A1172 0
SHEET 2 B 4 VAL A1178 ALA A1182 -1 O VAL A1179 N HIS A1171
SHEET 3 B 4 GLY A1227 MET A1230 -1 O GLY A1227 N ALA A1182
SHEET 4 B 4 GLN A1235 LEU A1237 -1 O LEU A1236 N VAL A1228
CRYST1 40.330 85.850 134.050 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.024795 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011648 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007460 0.00000
(ATOM LINES ARE NOT SHOWN.)
END