HEADER HYDROLASE 27-MAR-14 4P7O
TITLE STRUCTURE OF ESCHERICHIA COLI PGAB C-TERMINAL DOMAIN, P1 CRYSTAL FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE N-DEACETYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 310-672;
COMPND 5 SYNONYM: PGAB, POLY-BETA-1,6-GLCNAC N-DEACETYLASE;
COMPND 6 EC: 3.5.1.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: PGAB, YCDR, B1023, JW5142;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS BETA ALPHA BARREL, CARBOHYDRATE BINDING, GLYCOSYL HYDROLASE FOLD,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.LITTLE,G.LI,C.ING,B.DIFRANCESCO,N.C.BAMFORD,H.ROBINSON,M.NITZ,
AUTHOR 2 R.POMES,P.L.HOWELL
REVDAT 6 27-SEP-23 4P7O 1 REMARK
REVDAT 5 08-JAN-20 4P7O 1 REMARK
REVDAT 4 22-NOV-17 4P7O 1 SOURCE JRNL REMARK
REVDAT 3 01-OCT-14 4P7O 1 JRNL
REVDAT 2 23-JUL-14 4P7O 1 JRNL
REVDAT 1 02-JUL-14 4P7O 0
JRNL AUTH D.J.LITTLE,G.LI,C.ING,B.R.DIFRANCESCO,N.C.BAMFORD,
JRNL AUTH 2 H.ROBINSON,M.NITZ,R.POMES,P.L.HOWELL
JRNL TITL MODIFICATION AND PERIPLASMIC TRANSLOCATION OF THE BIOFILM
JRNL TITL 2 EXOPOLYSACCHARIDE POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 111 11013 2014
JRNL REFN ESSN 1091-6490
JRNL PMID 24994902
JRNL DOI 10.1073/PNAS.1406388111
REMARK 2
REMARK 2 RESOLUTION. 1.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1615)
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) : 1.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.86
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.1
REMARK 3 NUMBER OF REFLECTIONS : 115509
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.720
REMARK 3 FREE R VALUE TEST SET COUNT : 1866
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 41.8810 - 4.4763 0.99 8545 151 0.1980 0.1863
REMARK 3 2 4.4763 - 3.5536 0.95 8235 141 0.1875 0.2170
REMARK 3 3 3.5536 - 3.1046 0.96 8298 147 0.2049 0.2556
REMARK 3 4 3.1046 - 2.8208 0.96 8239 145 0.2158 0.2326
REMARK 3 5 2.8208 - 2.6186 0.96 8214 145 0.2186 0.2361
REMARK 3 6 2.6186 - 2.4643 0.96 8288 141 0.2161 0.3142
REMARK 3 7 2.4643 - 2.3409 0.96 8273 144 0.2203 0.2386
REMARK 3 8 2.3409 - 2.2390 0.81 7107 128 0.2712 0.3220
REMARK 3 9 2.2390 - 2.1528 0.82 6984 121 0.2277 0.2684
REMARK 3 10 2.1528 - 2.0785 0.95 8132 143 0.2160 0.2333
REMARK 3 11 2.0785 - 2.0135 0.93 8085 142 0.2478 0.2949
REMARK 3 12 2.0135 - 1.9560 0.95 8238 147 0.2147 0.2817
REMARK 3 13 1.9560 - 1.9045 0.82 7038 124 0.3188 0.4182
REMARK 3 14 1.9045 - 1.8580 0.86 7477 128 0.2294 0.1771
REMARK 3 15 1.8580 - 1.8158 0.94 8093 144 0.2113 0.2772
REMARK 3 16 1.8158 - 1.7771 0.94 8126 141 0.2134 0.2591
REMARK 3 17 1.7771 - 1.7416 0.94 7916 138 0.2160 0.2476
REMARK 3 18 1.7416 - 1.7087 0.94 8232 146 0.2194 0.2561
REMARK 3 19 1.7087 - 1.6782 0.94 8009 138 0.2216 0.2757
REMARK 3 20 1.6782 - 1.6497 0.94 8148 142 0.2186 0.2459
REMARK 3 21 1.6497 - 1.6231 0.93 7981 141 0.2205 0.2402
REMARK 3 22 1.6231 - 1.5982 0.93 8069 144 0.2240 0.2885
REMARK 3 23 1.5982 - 1.5746 0.93 8064 140 0.2328 0.2914
REMARK 3 24 1.5746 - 1.5525 0.93 7948 138 0.2407 0.2926
REMARK 3 25 1.5525 - 1.5315 0.92 7983 142 0.2529 0.3012
REMARK 3 26 1.5315 - 1.5116 0.91 7865 136 0.3101 0.3470
REMARK 3 27 1.5116 - 1.4927 0.91 7831 139 0.2706 0.3167
REMARK 3 28 1.4927 - 1.4747 0.81 7029 126 0.2923 0.3516
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.680
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.83
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 : 0.006 5763
REMARK 3 ANGLE : 1.075 7847
REMARK 3 CHIRALITY : 0.078 835
REMARK 3 PLANARITY : 0.005 1020
REMARK 3 DIHEDRAL : 13.402 2089
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 312 THROUGH 411 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.1874 -10.7648 66.8470
REMARK 3 T TENSOR
REMARK 3 T11: 0.1704 T22: 0.1178
REMARK 3 T33: 0.0949 T12: -0.0063
REMARK 3 T13: 0.0000 T23: 0.0132
REMARK 3 L TENSOR
REMARK 3 L11: 0.7798 L22: 0.8735
REMARK 3 L33: 1.3358 L12: 0.0560
REMARK 3 L13: -0.4480 L23: 0.0106
REMARK 3 S TENSOR
REMARK 3 S11: -0.0392 S12: 0.0209 S13: -0.0204
REMARK 3 S21: 0.0592 S22: 0.0325 S23: 0.0368
REMARK 3 S31: 0.0117 S32: -0.1155 S33: 0.0191
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 412 THROUGH 477 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.6048 5.2755 58.6109
REMARK 3 T TENSOR
REMARK 3 T11: 0.1753 T22: 0.1169
REMARK 3 T33: 0.1200 T12: -0.0017
REMARK 3 T13: -0.0160 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.2292 L22: 0.9612
REMARK 3 L33: 3.2273 L12: 0.1333
REMARK 3 L13: -0.0679 L23: -0.8385
REMARK 3 S TENSOR
REMARK 3 S11: -0.0052 S12: -0.0334 S13: 0.0266
REMARK 3 S21: 0.0420 S22: -0.0164 S23: 0.0291
REMARK 3 S31: -0.2134 S32: -0.0677 S33: 0.0100
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 478 THROUGH 499 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0467 15.4474 47.6037
REMARK 3 T TENSOR
REMARK 3 T11: 0.2957 T22: 0.1167
REMARK 3 T33: 0.2168 T12: -0.0401
REMARK 3 T13: -0.0304 T23: 0.0238
REMARK 3 L TENSOR
REMARK 3 L11: 1.9167 L22: 2.9158
REMARK 3 L33: 3.4510 L12: 0.1286
REMARK 3 L13: -1.3128 L23: 0.4503
REMARK 3 S TENSOR
REMARK 3 S11: 0.0605 S12: 0.0225 S13: 0.2883
REMARK 3 S21: -0.1003 S22: 0.0627 S23: -0.3086
REMARK 3 S31: -0.8359 S32: 0.1153 S33: -0.1083
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 500 THROUGH 529 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.8158 2.7906 57.9977
REMARK 3 T TENSOR
REMARK 3 T11: 0.1360 T22: 0.1176
REMARK 3 T33: 0.1238 T12: -0.0127
REMARK 3 T13: -0.0318 T23: -0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 1.3758 L22: 3.9614
REMARK 3 L33: 4.5641 L12: 1.2501
REMARK 3 L13: -1.7452 L23: -4.1783
REMARK 3 S TENSOR
REMARK 3 S11: 0.0372 S12: -0.0888 S13: 0.0499
REMARK 3 S21: -0.0225 S22: -0.1331 S23: -0.1491
REMARK 3 S31: 0.0145 S32: 0.4160 S33: 0.1266
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 530 THROUGH 636 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.4342 -14.3940 49.1215
REMARK 3 T TENSOR
REMARK 3 T11: 0.1806 T22: 0.0948
REMARK 3 T33: 0.0915 T12: 0.0106
REMARK 3 T13: -0.0038 T23: 0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 0.9352 L22: 1.2372
REMARK 3 L33: 1.6204 L12: 0.4597
REMARK 3 L13: 0.2129 L23: 0.5212
REMARK 3 S TENSOR
REMARK 3 S11: -0.0441 S12: 0.0316 S13: -0.0048
REMARK 3 S21: -0.0356 S22: 0.0150 S23: 0.0100
REMARK 3 S31: 0.0800 S32: -0.0040 S33: 0.0100
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 637 THROUGH 669 )
REMARK 3 ORIGIN FOR THE GROUP (A): -10.8228 -25.7760 57.0830
REMARK 3 T TENSOR
REMARK 3 T11: 0.2876 T22: 0.1134
REMARK 3 T33: 0.1096 T12: -0.0143
REMARK 3 T13: -0.0007 T23: 0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 2.4237 L22: 2.0443
REMARK 3 L33: 1.0815 L12: -0.6505
REMARK 3 L13: -0.9175 L23: 0.6180
REMARK 3 S TENSOR
REMARK 3 S11: -0.0827 S12: 0.0284 S13: -0.1963
REMARK 3 S21: 0.1229 S22: -0.0084 S23: 0.0674
REMARK 3 S31: 0.2254 S32: -0.0598 S33: 0.0524
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 312 THROUGH 411 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.8160 12.9457 7.2973
REMARK 3 T TENSOR
REMARK 3 T11: 0.1698 T22: 0.1171
REMARK 3 T33: 0.0924 T12: -0.0044
REMARK 3 T13: -0.0079 T23: 0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 1.1260 L22: 1.2779
REMARK 3 L33: 1.2001 L12: -0.1205
REMARK 3 L13: 0.5350 L23: -0.2176
REMARK 3 S TENSOR
REMARK 3 S11: -0.0476 S12: 0.0345 S13: 0.0760
REMARK 3 S21: -0.0671 S22: 0.0399 S23: 0.0345
REMARK 3 S31: -0.0594 S32: -0.1186 S33: 0.0120
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 412 THROUGH 529 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.5592 -4.1911 18.5802
REMARK 3 T TENSOR
REMARK 3 T11: 0.1836 T22: 0.1137
REMARK 3 T33: 0.1301 T12: 0.0004
REMARK 3 T13: 0.0123 T23: 0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.3710 L22: 1.3127
REMARK 3 L33: 2.7086 L12: -0.0816
REMARK 3 L13: 0.4077 L23: -1.2088
REMARK 3 S TENSOR
REMARK 3 S11: 0.0234 S12: 0.0099 S13: -0.0320
REMARK 3 S21: -0.0428 S22: -0.0284 S23: -0.0853
REMARK 3 S31: 0.1407 S32: 0.0385 S33: 0.0026
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 530 THROUGH 669 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0494 19.5047 23.5204
REMARK 3 T TENSOR
REMARK 3 T11: 0.1912 T22: 0.0966
REMARK 3 T33: 0.0989 T12: -0.0219
REMARK 3 T13: -0.0057 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.7679 L22: 1.5008
REMARK 3 L33: 1.0821 L12: -0.4229
REMARK 3 L13: 0.1308 L23: 0.1794
REMARK 3 S TENSOR
REMARK 3 S11: -0.0233 S12: -0.0027 S13: 0.0779
REMARK 3 S21: -0.0058 S22: -0.0207 S23: -0.0250
REMARK 3 S31: -0.1413 S32: -0.0233 S33: 0.0493
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 4P7O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000200872.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-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 : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK DOUBLE CRYSTAL
REMARK 200 SAGITTAL FOCUSING
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 126137
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.480
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.29900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
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: PDB ENTRY 4P7L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG5000 MME, 0.2 M AMMONIUM
REMARK 280 SULFATE, 0.1 M MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 IS THE SAME AS ASYM.
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLY A 306
REMARK 465 SER A 307
REMARK 465 HIS A 308
REMARK 465 MET A 309
REMARK 465 GLU A 310
REMARK 465 LYS A 311
REMARK 465 LYS A 424
REMARK 465 ALA A 425
REMARK 465 GLN A 426
REMARK 465 ILE A 427
REMARK 465 HIS A 428
REMARK 465 PRO A 429
REMARK 465 GLU A 430
REMARK 465 GLN A 431
REMARK 465 GLN A 614
REMARK 465 LYS A 615
REMARK 465 ASN A 616
REMARK 465 GLY A 617
REMARK 465 GLN A 618
REMARK 465 LYS A 670
REMARK 465 ASN A 671
REMARK 465 ASP A 672
REMARK 465 GLY B 306
REMARK 465 SER B 307
REMARK 465 HIS B 308
REMARK 465 MET B 309
REMARK 465 GLU B 310
REMARK 465 LYS B 311
REMARK 465 LYS B 424
REMARK 465 ALA B 425
REMARK 465 GLN B 426
REMARK 465 ILE B 427
REMARK 465 HIS B 428
REMARK 465 PRO B 429
REMARK 465 GLU B 430
REMARK 465 GLN B 431
REMARK 465 LYS B 615
REMARK 465 ASN B 616
REMARK 465 GLY B 617
REMARK 465 GLN B 618
REMARK 465 LYS B 670
REMARK 465 ASN B 671
REMARK 465 ASP B 672
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 GLU A 501 CG CD OE1 OE2
REMARK 470 LYS A 504 CG CD CE NZ
REMARK 470 LYS A 562 CG CD CE NZ
REMARK 470 LYS A 601 CG CD CE NZ
REMARK 470 LYS A 640 CG CD CE NZ
REMARK 470 LYS B 562 CG CD CE NZ
REMARK 470 GLN B 599 CG CD OE1 NE2
REMARK 470 LYS B 601 CG CD CE NZ
REMARK 470 GLN B 614 CG CD OE1 NE2
REMARK 470 HIS B 619 CG ND1 CD2 CE1 NE2
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 466 O HOH A 949 2.03
REMARK 500 O HOH A 761 O HOH A 780 2.12
REMARK 500 OE1 GLN A 611 O HOH A 897 2.13
REMARK 500 O HOH B 949 O HOH B 1065 2.14
REMARK 500 O HOH A 796 O HOH A 1047 2.14
REMARK 500 O HOH B 1039 O HOH B 1064 2.15
REMARK 500 O HOH B 790 O HOH B 960 2.16
REMARK 500 O HOH B 764 O HOH B 978 2.18
REMARK 500 O HOH A 949 O HOH A 1089 2.18
REMARK 500 O HOH A 974 O HOH A 1036 2.19
REMARK 500 O HOH B 951 O HOH B 1030 2.19
REMARK 500 OD2 ASP A 358 O HOH A 952 2.19
REMARK 500 O HOH A 992 O HOH A 1064 2.19
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 358 68.74 -160.23
REMARK 500 ASP A 409 126.57 -36.99
REMARK 500 PHE A 663 -43.41 -134.71
REMARK 500 ASP B 358 57.31 -156.35
REMARK 500 ASP B 409 126.96 -38.97
REMARK 500 PHE B 663 -40.75 -136.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 921 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH A 969 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH A 983 DISTANCE = 7.22 ANGSTROMS
REMARK 525 HOH A 987 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH A 991 DISTANCE = 7.99 ANGSTROMS
REMARK 525 HOH A1013 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH A1042 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH A1058 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH A1061 DISTANCE = 6.98 ANGSTROMS
REMARK 525 HOH A1062 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH A1065 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH A1079 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH A1084 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A1093 DISTANCE = 7.51 ANGSTROMS
REMARK 525 HOH A1100 DISTANCE = 6.92 ANGSTROMS
REMARK 525 HOH A1101 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH B 983 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH B 984 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH B1000 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH B1001 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH B1021 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B1024 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH B1043 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH B1077 DISTANCE = 6.52 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4P7L RELATED DB: PDB
REMARK 900 ESCHERICHIA COLI PGAB C-TERMINAL DOMAIN APO FORM, P212121 CRYSTAL
REMARK 900 FORM
REMARK 900 RELATED ID: 4P7N RELATED DB: PDB
REMARK 900 ESCHERICHIA COLI PGAB C-TERMINAL DOMAIN IN COMPLEX WITH GLUCOSAMINE
REMARK 900 RELATED ID: 4P7Q RELATED DB: PDB
REMARK 900 ESCHERICHIA COLI PGAB C-TERMINAL DOMAIN IN COMPLEX WITH N-
REMARK 900 ACETYLGLUCOSAMINE
REMARK 900 RELATED ID: 4P7R RELATED DB: PDB
REMARK 900 ESCHERICHIA COLI PGAB C-TERMINAL DOMAIN IN COMPLEX WITH A POLY-
REMARK 900 ALPHA-1,6-N-ACETYL-D-GLUCOSAMINE (PNAG) HEXAMER
DBREF 4P7O A 310 672 UNP P75906 PGAB_ECOLI 310 672
DBREF 4P7O B 310 672 UNP P75906 PGAB_ECOLI 310 672
SEQADV 4P7O GLY A 306 UNP P75906 EXPRESSION TAG
SEQADV 4P7O SER A 307 UNP P75906 EXPRESSION TAG
SEQADV 4P7O HIS A 308 UNP P75906 EXPRESSION TAG
SEQADV 4P7O MET A 309 UNP P75906 EXPRESSION TAG
SEQADV 4P7O GLY B 306 UNP P75906 EXPRESSION TAG
SEQADV 4P7O SER B 307 UNP P75906 EXPRESSION TAG
SEQADV 4P7O HIS B 308 UNP P75906 EXPRESSION TAG
SEQADV 4P7O MET B 309 UNP P75906 EXPRESSION TAG
SEQRES 1 A 367 GLY SER HIS MET GLU LYS SER PRO GLN ARG ILE MET HIS
SEQRES 2 A 367 ILE ASP LEU ASP TYR VAL TYR ASP GLU ASN LEU GLN GLN
SEQRES 3 A 367 MET ASP ARG ASN ILE ASP VAL LEU ILE GLN ARG VAL LYS
SEQRES 4 A 367 ASP MET GLN ILE SER THR VAL TYR LEU GLN ALA PHE ALA
SEQRES 5 A 367 ASP PRO ASP GLY ASP GLY LEU VAL LYS GLU VAL TRP PHE
SEQRES 6 A 367 PRO ASN ARG LEU LEU PRO MET LYS ALA ASP ILE PHE SER
SEQRES 7 A 367 ARG VAL ALA TRP GLN LEU ARG THR ARG SER GLY VAL ASN
SEQRES 8 A 367 ILE TYR ALA TRP MET PRO VAL LEU SER TRP ASP LEU ASP
SEQRES 9 A 367 PRO THR LEU THR ARG VAL LYS TYR LEU PRO THR GLY GLU
SEQRES 10 A 367 LYS LYS ALA GLN ILE HIS PRO GLU GLN TYR HIS ARG LEU
SEQRES 11 A 367 SER PRO PHE ASP ASP ARG VAL ARG ALA GLN VAL GLY MET
SEQRES 12 A 367 LEU TYR GLU ASP LEU ALA GLY HIS ALA ALA PHE ASP GLY
SEQRES 13 A 367 ILE LEU PHE HIS ASP ASP ALA LEU LEU SER ASP TYR GLU
SEQRES 14 A 367 ASP ALA SER ALA PRO ALA ILE THR ALA TYR GLN GLN ALA
SEQRES 15 A 367 GLY PHE SER GLY SER LEU SER GLU ILE ARG GLN ASN PRO
SEQRES 16 A 367 GLU GLN PHE LYS GLN TRP ALA ARG PHE LYS SER ARG ALA
SEQRES 17 A 367 LEU THR ASP PHE THR LEU GLU LEU SER ALA ARG VAL LYS
SEQRES 18 A 367 ALA ILE ARG GLY PRO HIS ILE LYS THR ALA ARG ASN ILE
SEQRES 19 A 367 PHE ALA LEU PRO VAL ILE GLN PRO GLU SER GLU ALA TRP
SEQRES 20 A 367 PHE ALA GLN ASN TYR ALA ASP PHE LEU LYS SER TYR ASP
SEQRES 21 A 367 TRP THR ALA ILE MET ALA MET PRO TYR LEU GLU GLY VAL
SEQRES 22 A 367 ALA GLU LYS SER ALA ASP GLN TRP LEU ILE GLN LEU THR
SEQRES 23 A 367 ASN GLN ILE LYS ASN ILE PRO GLN ALA LYS ASP LYS SER
SEQRES 24 A 367 ILE LEU GLU LEU GLN ALA GLN ASN TRP GLN LYS ASN GLY
SEQRES 25 A 367 GLN HIS GLN ALA ILE SER SER GLN GLN LEU ALA HIS TRP
SEQRES 26 A 367 MET SER LEU LEU GLN LEU ASN GLY VAL LYS ASN TYR GLY
SEQRES 27 A 367 TYR TYR PRO ASP ASN PHE LEU HIS ASN GLN PRO GLU ILE
SEQRES 28 A 367 ASP LEU ILE ARG PRO GLU PHE SER THR ALA TRP TYR PRO
SEQRES 29 A 367 LYS ASN ASP
SEQRES 1 B 367 GLY SER HIS MET GLU LYS SER PRO GLN ARG ILE MET HIS
SEQRES 2 B 367 ILE ASP LEU ASP TYR VAL TYR ASP GLU ASN LEU GLN GLN
SEQRES 3 B 367 MET ASP ARG ASN ILE ASP VAL LEU ILE GLN ARG VAL LYS
SEQRES 4 B 367 ASP MET GLN ILE SER THR VAL TYR LEU GLN ALA PHE ALA
SEQRES 5 B 367 ASP PRO ASP GLY ASP GLY LEU VAL LYS GLU VAL TRP PHE
SEQRES 6 B 367 PRO ASN ARG LEU LEU PRO MET LYS ALA ASP ILE PHE SER
SEQRES 7 B 367 ARG VAL ALA TRP GLN LEU ARG THR ARG SER GLY VAL ASN
SEQRES 8 B 367 ILE TYR ALA TRP MET PRO VAL LEU SER TRP ASP LEU ASP
SEQRES 9 B 367 PRO THR LEU THR ARG VAL LYS TYR LEU PRO THR GLY GLU
SEQRES 10 B 367 LYS LYS ALA GLN ILE HIS PRO GLU GLN TYR HIS ARG LEU
SEQRES 11 B 367 SER PRO PHE ASP ASP ARG VAL ARG ALA GLN VAL GLY MET
SEQRES 12 B 367 LEU TYR GLU ASP LEU ALA GLY HIS ALA ALA PHE ASP GLY
SEQRES 13 B 367 ILE LEU PHE HIS ASP ASP ALA LEU LEU SER ASP TYR GLU
SEQRES 14 B 367 ASP ALA SER ALA PRO ALA ILE THR ALA TYR GLN GLN ALA
SEQRES 15 B 367 GLY PHE SER GLY SER LEU SER GLU ILE ARG GLN ASN PRO
SEQRES 16 B 367 GLU GLN PHE LYS GLN TRP ALA ARG PHE LYS SER ARG ALA
SEQRES 17 B 367 LEU THR ASP PHE THR LEU GLU LEU SER ALA ARG VAL LYS
SEQRES 18 B 367 ALA ILE ARG GLY PRO HIS ILE LYS THR ALA ARG ASN ILE
SEQRES 19 B 367 PHE ALA LEU PRO VAL ILE GLN PRO GLU SER GLU ALA TRP
SEQRES 20 B 367 PHE ALA GLN ASN TYR ALA ASP PHE LEU LYS SER TYR ASP
SEQRES 21 B 367 TRP THR ALA ILE MET ALA MET PRO TYR LEU GLU GLY VAL
SEQRES 22 B 367 ALA GLU LYS SER ALA ASP GLN TRP LEU ILE GLN LEU THR
SEQRES 23 B 367 ASN GLN ILE LYS ASN ILE PRO GLN ALA LYS ASP LYS SER
SEQRES 24 B 367 ILE LEU GLU LEU GLN ALA GLN ASN TRP GLN LYS ASN GLY
SEQRES 25 B 367 GLN HIS GLN ALA ILE SER SER GLN GLN LEU ALA HIS TRP
SEQRES 26 B 367 MET SER LEU LEU GLN LEU ASN GLY VAL LYS ASN TYR GLY
SEQRES 27 B 367 TYR TYR PRO ASP ASN PHE LEU HIS ASN GLN PRO GLU ILE
SEQRES 28 B 367 ASP LEU ILE ARG PRO GLU PHE SER THR ALA TRP TYR PRO
SEQRES 29 B 367 LYS ASN ASP
FORMUL 3 HOH *814(H2 O)
HELIX 1 AA1 ASP A 320 VAL A 324 5 5
HELIX 2 AA2 ASN A 328 GLN A 347 1 20
HELIX 3 AA3 ILE A 381 SER A 393 1 13
HELIX 4 AA4 ASP A 439 GLY A 455 1 17
HELIX 5 AA5 SER A 477 GLY A 488 1 12
HELIX 6 AA6 SER A 492 GLN A 498 1 7
HELIX 7 AA7 ASN A 499 GLY A 530 1 32
HELIX 8 AA8 PHE A 540 GLN A 546 1 7
HELIX 9 AA9 PRO A 547 PHE A 553 5 7
HELIX 10 AB1 ASN A 556 TYR A 564 1 9
HELIX 11 AB2 ALA A 579 LYS A 581 5 3
HELIX 12 AB3 SER A 582 ASN A 596 1 15
HELIX 13 AB4 GLN A 599 ASP A 602 5 4
HELIX 14 AB5 SER A 623 ASN A 637 1 15
HELIX 15 AB6 ASN A 648 ASN A 652 5 5
HELIX 16 AB7 GLU A 655 ARG A 660 1 6
HELIX 17 AB8 PRO A 661 PHE A 663 5 3
HELIX 18 AB9 ASP B 320 VAL B 324 5 5
HELIX 19 AC1 ASN B 328 GLN B 347 1 20
HELIX 20 AC2 ILE B 381 SER B 393 1 13
HELIX 21 AC3 ASP B 439 ALA B 457 1 19
HELIX 22 AC4 SER B 477 ALA B 487 1 11
HELIX 23 AC5 SER B 492 ASN B 499 1 8
HELIX 24 AC6 ASN B 499 GLY B 530 1 32
HELIX 25 AC7 PHE B 540 GLN B 546 1 7
HELIX 26 AC8 PRO B 547 PHE B 553 5 7
HELIX 27 AC9 ASN B 556 TYR B 564 1 9
HELIX 28 AD1 ALA B 579 LYS B 581 5 3
HELIX 29 AD2 SER B 582 ASN B 596 1 15
HELIX 30 AD3 ALA B 600 ASP B 602 5 3
HELIX 31 AD4 SER B 623 ASN B 637 1 15
HELIX 32 AD5 ASN B 648 ASN B 652 5 5
HELIX 33 AD6 GLU B 655 ARG B 660 1 6
HELIX 34 AD7 PRO B 661 PHE B 663 5 3
SHEET 1 AA1 9 ARG A 315 ILE A 319 0
SHEET 2 AA1 9 THR A 350 GLN A 354 1 O TYR A 352 N ILE A 319
SHEET 3 AA1 9 ASN A 396 MET A 401 1 O TYR A 398 N LEU A 353
SHEET 4 AA1 9 GLY A 461 PHE A 464 1 O LEU A 463 N ALA A 399
SHEET 5 AA1 9 LYS A 534 ILE A 539 1 O ALA A 536 N PHE A 464
SHEET 6 AA1 9 TRP A 566 MET A 570 1 O MET A 570 N ILE A 539
SHEET 7 AA1 9 SER A 604 GLN A 609 1 O GLU A 607 N ILE A 569
SHEET 8 AA1 9 TYR A 642 TYR A 645 1 O GLY A 643 N LEU A 608
SHEET 9 AA1 9 ARG A 315 ILE A 319 1 N HIS A 318 O TYR A 644
SHEET 1 AA2 2 GLN A 611 ASN A 612 0
SHEET 2 AA2 2 GLN A 620 ALA A 621 -1 O GLN A 620 N ASN A 612
SHEET 1 AA3 9 ARG B 315 ILE B 319 0
SHEET 2 AA3 9 THR B 350 GLN B 354 1 O TYR B 352 N ILE B 319
SHEET 3 AA3 9 ASN B 396 MET B 401 1 O TRP B 400 N LEU B 353
SHEET 4 AA3 9 GLY B 461 PHE B 464 1 O LEU B 463 N ALA B 399
SHEET 5 AA3 9 LYS B 534 ILE B 539 1 O ALA B 536 N PHE B 464
SHEET 6 AA3 9 TRP B 566 MET B 570 1 O MET B 570 N ILE B 539
SHEET 7 AA3 9 SER B 604 GLN B 609 1 O GLU B 607 N ILE B 569
SHEET 8 AA3 9 TYR B 642 TYR B 645 1 O GLY B 643 N LEU B 608
SHEET 9 AA3 9 ARG B 315 ILE B 319 1 N HIS B 318 O TYR B 644
SHEET 1 AA4 2 GLN B 611 ASN B 612 0
SHEET 2 AA4 2 GLN B 620 ALA B 621 -1 O GLN B 620 N ASN B 612
CISPEP 1 GLU A 474 ASP A 475 0 -16.07
CISPEP 2 TYR A 645 PRO A 646 0 -7.02
CISPEP 3 GLN A 653 PRO A 654 0 2.39
CISPEP 4 GLU B 474 ASP B 475 0 -15.09
CISPEP 5 TYR B 645 PRO B 646 0 -5.42
CISPEP 6 GLN B 653 PRO B 654 0 -2.09
CRYST1 41.618 54.016 86.460 101.70 98.30 90.19 P 1 2
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 0.024028 0.000081 0.003599 0.00000
SCALE2 0.000000 0.018513 0.003888 0.00000
SCALE3 0.000000 0.000000 0.011943 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
