| content |
HEADER HYDROLASE 24-MAR-13 4JUI
TITLE CRYSTAL STRUCTURE OF TANNASE FROM FROM LACTOBACILLUS PLANTARUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TANNASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS PLANTARUM;
SOURCE 3 ORGANISM_TAXID: 1590;
SOURCE 4 GENE: TANLPL;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS GALLATE, HYDROLASE, HYDROLYSIS, TANNINS
EXPDTA X-RAY DIFFRACTION
AUTHOR B.REN,M.WU,Q.WANG,X.PENG,H.WEN,W.J.MCKINSTRY,Q.CHEN
REVDAT 1 22-MAY-13 4JUI 0
JRNL AUTH B.REN,M.WU,Q.WANG,X.PENG,H.WEN,W.J.MCKINSTRY,Q.CHEN
JRNL TITL CRYSTAL STRUCTURE OF TANNASE FROM LACTOBACILLUS PLANTARUM
JRNL REF J.MOL.BIOL. 2013
JRNL REFN ESSN 1089-8638
JRNL PMID 23648840
JRNL DOI 10.1016/J.JMB.2013.04.032
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.52
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.4
REMARK 3 NUMBER OF REFLECTIONS : 90551
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.180
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.690
REMARK 3 FREE R VALUE TEST SET COUNT : 1530
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 19.5241 - 3.7725 0.98 8702 156 0.1346 0.1341
REMARK 3 2 3.7725 - 2.9978 0.98 8665 152 0.1426 0.1610
REMARK 3 3 2.9978 - 2.6199 0.96 8525 148 0.1600 0.2296
REMARK 3 4 2.6199 - 2.3808 0.95 8443 144 0.1550 0.1909
REMARK 3 5 2.3808 - 2.2104 0.94 8309 140 0.1542 0.1411
REMARK 3 6 2.2104 - 2.0803 0.92 8120 137 0.1520 0.2092
REMARK 3 7 2.0803 - 1.9762 0.90 7958 137 0.1583 0.1976
REMARK 3 8 1.9762 - 1.8902 0.89 7855 136 0.1723 0.2022
REMARK 3 9 1.8902 - 1.8175 0.86 7609 126 0.1754 0.2479
REMARK 3 10 1.8175 - 1.7548 0.85 7497 130 0.1851 0.2185
REMARK 3 11 1.7548 - 1.7000 0.83 7338 124 0.1904 0.2529
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.84
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 7533
REMARK 3 ANGLE : 1.058 10264
REMARK 3 CHIRALITY : 0.071 1147
REMARK 3 PLANARITY : 0.004 1340
REMARK 3 DIHEDRAL : 14.313 2707
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (chain A and resid 1:51)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.3614 114.8073 88.1600
REMARK 3 T TENSOR
REMARK 3 T11: 0.3165 T22: 0.1065
REMARK 3 T33: 0.0980 T12: -0.0104
REMARK 3 T13: -0.0148 T23: -0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 0.7483 L22: 1.1360
REMARK 3 L33: 2.0623 L12: -0.1334
REMARK 3 L13: -0.0664 L23: -0.1491
REMARK 3 S TENSOR
REMARK 3 S11: 0.0108 S12: -0.0641 S13: 0.0763
REMARK 3 S21: 0.0870 S22: 0.0151 S23: 0.0424
REMARK 3 S31: -0.3954 S32: 0.0771 S33: 0.0018
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (chain A and resid 52:127)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6439 106.2992 84.8485
REMARK 3 T TENSOR
REMARK 3 T11: 0.2090 T22: 0.0819
REMARK 3 T33: 0.0813 T12: 0.0121
REMARK 3 T13: -0.0090 T23: 0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 0.7494 L22: 0.8362
REMARK 3 L33: 3.0143 L12: 0.0097
REMARK 3 L13: 0.6951 L23: 0.0307
REMARK 3 S TENSOR
REMARK 3 S11: -0.0431 S12: -0.0290 S13: 0.0902
REMARK 3 S21: 0.0825 S22: -0.0037 S23: 0.0405
REMARK 3 S31: -0.3161 S32: -0.1212 S33: 0.0444
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (chain A and resid 128:229)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9078 98.7381 74.0715
REMARK 3 T TENSOR
REMARK 3 T11: 0.1324 T22: 0.1279
REMARK 3 T33: 0.0527 T12: 0.0126
REMARK 3 T13: -0.0005 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 0.2958 L22: 1.9281
REMARK 3 L33: 1.5814 L12: 0.4038
REMARK 3 L13: 0.2969 L23: 0.9308
REMARK 3 S TENSOR
REMARK 3 S11: 0.0021 S12: 0.0304 S13: 0.0369
REMARK 3 S21: -0.0260 S22: 0.0008 S23: -0.0198
REMARK 3 S31: -0.1161 S32: 0.1485 S33: 0.0004
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (chain A and resid 230:242)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8068 104.1674 76.2288
REMARK 3 T TENSOR
REMARK 3 T11: 0.7756 T22: 1.0871
REMARK 3 T33: 1.3061 T12: 0.0338
REMARK 3 T13: 0.0220 T23: -0.3000
REMARK 3 L TENSOR
REMARK 3 L11: 7.0461 L22: 3.6852
REMARK 3 L33: 5.7136 L12: 3.6049
REMARK 3 L13: 4.1019 L23: -0.3758
REMARK 3 S TENSOR
REMARK 3 S11: -0.1339 S12: -1.0319 S13: 0.8455
REMARK 3 S21: 0.3667 S22: -0.1474 S23: 0.0039
REMARK 3 S31: -0.6308 S32: -0.1984 S33: 0.2136
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (chain A and resid 243:282)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.5935 80.2204 62.3439
REMARK 3 T TENSOR
REMARK 3 T11: 0.1990 T22: 0.1434
REMARK 3 T33: 0.0653 T12: 0.0653
REMARK 3 T13: 0.0028 T23: -0.0417
REMARK 3 L TENSOR
REMARK 3 L11: 1.0575 L22: 1.7610
REMARK 3 L33: 2.3428 L12: 0.8558
REMARK 3 L13: 0.1324 L23: 0.2641
REMARK 3 S TENSOR
REMARK 3 S11: -0.2267 S12: -0.3186 S13: 0.1843
REMARK 3 S21: 0.1694 S22: 0.0947 S23: 0.0309
REMARK 3 S31: 0.0482 S32: -0.1098 S33: 0.0799
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (chain A and resid 283:461)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.3945 84.9230 71.8328
REMARK 3 T TENSOR
REMARK 3 T11: 0.1983 T22: 0.1063
REMARK 3 T33: 0.0569 T12: 0.0152
REMARK 3 T13: -0.0110 T23: -0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.4874 L22: 1.0025
REMARK 3 L33: 1.3120 L12: 0.1727
REMARK 3 L13: 0.0613 L23: 0.2543
REMARK 3 S TENSOR
REMARK 3 S11: 0.0138 S12: -0.0059 S13: 0.0201
REMARK 3 S21: 0.0848 S22: 0.0180 S23: -0.0086
REMARK 3 S31: 0.2567 S32: 0.0294 S33: -0.0115
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (chain A and resid 462:469)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.1997 92.4264 93.4088
REMARK 3 T TENSOR
REMARK 3 T11: 0.2593 T22: 0.1554
REMARK 3 T33: 0.1141 T12: 0.0321
REMARK 3 T13: -0.0723 T23: 0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 4.1776 L22: 3.2640
REMARK 3 L33: 6.2783 L12: -0.1291
REMARK 3 L13: -1.0659 L23: -1.3303
REMARK 3 S TENSOR
REMARK 3 S11: -0.0564 S12: -0.4029 S13: 0.0593
REMARK 3 S21: 0.3238 S22: 0.0211 S23: -0.2939
REMARK 3 S31: -0.1017 S32: 0.5301 S33: 0.1002
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 4JUI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-APR-13.
REMARK 100 THE RCSB ID CODE IS RCSB078520.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 90575
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 65.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 0.30500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG 3000, 0.1M TRI-SODIUM
REMARK 280 CITRATE PH 5.5, VAPOR DIFFUSION, TEMPERATURE 281K
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 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 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 O HOH A 943 O HOH A 1068 1.80
REMARK 500 OE1 GLN A 310 O HOH A 1030 1.80
REMARK 500 O HOH A 820 O HOH A 939 1.83
REMARK 500 O HOH B 1155 O HOH B 1156 1.84
REMARK 500 O HOH A 717 O HOH B 1154 1.93
REMARK 500 O HOH B 1176 O HOH B 1177 1.94
REMARK 500 O HOH A 826 O HOH A 1044 1.95
REMARK 500 NE2 GLN B 350 O HOH B 1160 1.95
REMARK 500 O HOH B 976 O HOH B 1202 1.95
REMARK 500 O HOH B 987 O HOH B 1060 1.96
REMARK 500 O HOH A 863 O HOH A 869 1.97
REMARK 500 O HOH A 989 O HOH A 1060 1.98
REMARK 500 OD1 ASN A 31 O HOH A 823 1.98
REMARK 500 O HOH B 802 O HOH B 999 1.99
REMARK 500 O HOH B 943 O HOH B 1208 1.99
REMARK 500 O HOH B 822 O HOH B 1052 2.00
REMARK 500 O HOH B 924 O HOH B 991 2.01
REMARK 500 O HOH B 1145 O HOH B 1172 2.01
REMARK 500 O HOH A 751 O HOH B 894 2.02
REMARK 500 OE1 GLN A 310 O HOH A 854 2.04
REMARK 500 OE1 GLN B 271 O HOH B 959 2.04
REMARK 500 O HOH B 1063 O HOH B 1187 2.04
REMARK 500 NH2 ARG A 64 O HOH A 1076 2.08
REMARK 500 NE2 GLN A 350 O HOH A 944 2.08
REMARK 500 ND2 ASN A 325 O HOH A 1091 2.08
REMARK 500 OE1 GLU B 182 O HOH B 917 2.10
REMARK 500 O HOH B 651 O HOH B 1185 2.10
REMARK 500 OE1 GLN A 22 O HOH A 645 2.11
REMARK 500 O HOH A 832 O HOH B 601 2.11
REMARK 500 O HOH B 1173 O HOH B 1174 2.11
REMARK 500 O HOH B 962 O HOH B 1052 2.13
REMARK 500 O HOH B 1157 O HOH B 1158 2.13
REMARK 500 O HOH A 1077 O HOH B 1128 2.13
REMARK 500 OG1 THR B 401 O HOH B 861 2.14
REMARK 500 O HOH B 1166 O HOH B 1167 2.15
REMARK 500 OE2 GLU A 357 O09 EGR A 501 2.15
REMARK 500 NE2 GLN B 298 O HOH B 801 2.15
REMARK 500 O HOH B 920 O HOH B 1214 2.16
REMARK 500 ND2 ASN B 94 O HOH B 850 2.16
REMARK 500 O HOH B 991 O HOH B 1218 2.16
REMARK 500 O HOH A 821 O HOH A 934 2.17
REMARK 500 O HOH A 1035 O HOH A 1063 2.17
REMARK 500 O HOH A 702 O HOH A 938 2.17
REMARK 500 O HOH A 763 O HOH A 1051 2.18
REMARK 500 OD1 ASN B 31 O HOH B 986 2.19
REMARK 500 ND2 ASN A 94 O HOH A 974 2.19
REMARK 500 N ALA B 233 O HOH B 1204 2.19
REMARK 500 OE2 GLU A 244 O HOH A 912 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 ALA A 163 -118.90 64.06
REMARK 500 CYS A 204 58.48 30.22
REMARK 500 ARG A 228 -158.07 -151.29
REMARK 500 ALA A 233 -154.02 -71.28
REMARK 500 THR A 340 145.37 78.29
REMARK 500 ALA A 344 -157.35 -84.38
REMARK 500 PHE A 371 15.87 -141.93
REMARK 500 PRO B 130 31.59 -99.01
REMARK 500 ALA B 163 -116.35 65.04
REMARK 500 CYS B 204 54.26 32.93
REMARK 500 ARG B 228 -150.23 -147.05
REMARK 500 THR B 340 148.59 82.11
REMARK 500 ALA B 344 -156.93 -82.54
REMARK 500 PHE B 371 16.22 -144.85
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 A1083 DISTANCE = 6.23 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EGR A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EGR B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 506
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4J0C RELATED DB: PDB
REMARK 900 RELATED ID: 4J0D RELATED DB: PDB
REMARK 900 RELATED ID: 4J0G RELATED DB: PDB
REMARK 900 RELATED ID: 4J0H RELATED DB: PDB
REMARK 900 RELATED ID: 4J0I RELATED DB: PDB
REMARK 900 RELATED ID: 4J0J RELATED DB: PDB
REMARK 900 RELATED ID: 4J0K RELATED DB: PDB
DBREF 4JUI A 1 469 UNP B3Y018 B3Y018_LACPN 1 469
DBREF 4JUI B 1 469 UNP B3Y018 B3Y018_LACPN 1 469
SEQADV 4JUI SER A 0 UNP B3Y018 EXPRESSION TAG
SEQADV 4JUI ALA A 163 UNP B3Y018 SER 163 ENGINEERED MUTATION
SEQADV 4JUI SER B 0 UNP B3Y018 EXPRESSION TAG
SEQADV 4JUI ALA B 163 UNP B3Y018 SER 163 ENGINEERED MUTATION
SEQRES 1 A 470 SER MET SER ASN ARG LEU ILE PHE ASP ALA ASP TRP LEU
SEQRES 2 A 470 VAL PRO GLU GLN VAL GLN VAL ALA GLY GLN ALA ILE GLN
SEQRES 3 A 470 TYR TYR ALA ALA ARG ASN ILE GLN TYR VAL GLN HIS PRO
SEQRES 4 A 470 VAL ALA ALA ILE GLN VAL LEU ASN VAL PHE VAL PRO ALA
SEQRES 5 A 470 ALA TYR LEU HIS GLY SER SER VAL ASN GLY TYR GLN ARG
SEQRES 6 A 470 ALA THR ALA PRO ILE LEU MET PRO ASN THR VAL GLY GLY
SEQRES 7 A 470 TYR LEU PRO GLY PRO ALA ASP ASP PRO GLN ARG VAL THR
SEQRES 8 A 470 TRP PRO THR ASN ALA GLY THR ILE GLN GLN ALA LEU LYS
SEQRES 9 A 470 ARG GLY TYR VAL VAL VAL ALA ALA GLY ILE ARG GLY ARG
SEQRES 10 A 470 THR THR VAL ASP LYS SER GLY GLN ARG VAL GLY GLN ALA
SEQRES 11 A 470 PRO ALA PHE ILE VAL ASP MET LYS ALA ALA ILE ARG TYR
SEQRES 12 A 470 VAL LYS TYR ASN GLN GLY ARG LEU PRO GLY ASP ALA ASN
SEQRES 13 A 470 ARG ILE ILE THR ASN GLY THR ALA ALA GLY GLY ALA THR
SEQRES 14 A 470 SER ALA LEU ALA GLY ALA SER GLY ASN SER ALA TYR PHE
SEQRES 15 A 470 GLU PRO ALA LEU THR ALA LEU GLY ALA ALA PRO ALA THR
SEQRES 16 A 470 ASP ASP ILE PHE ALA VAL SER ALA TYR CYS PRO ILE HIS
SEQRES 17 A 470 ASN LEU GLU HIS ALA ASP MET ALA TYR GLU TRP GLN PHE
SEQRES 18 A 470 ASN GLY ILE ASN ASP TRP HIS ARG TYR GLN PRO VAL ALA
SEQRES 19 A 470 GLY THR THR LYS ASN GLY ARG PRO LYS PHE GLU PRO VAL
SEQRES 20 A 470 SER GLY GLN LEU THR VAL GLU GLU GLN ALA LEU SER LEU
SEQRES 21 A 470 ALA LEU LYS ALA GLN PHE SER THR TYR LEU ASN GLN LEU
SEQRES 22 A 470 LYS LEU THR ALA SER ASP GLY THR HIS LEU THR LEU ASN
SEQRES 23 A 470 GLU ALA GLY MET GLY SER PHE ARG ASP VAL VAL ARG GLN
SEQRES 24 A 470 LEU LEU ILE SER SER ALA GLN THR ALA PHE ASP GLN GLY
SEQRES 25 A 470 THR ASP ILE HIS LYS TYR ALA GLY PHE VAL VAL THR GLY
SEQRES 26 A 470 ASN GLN VAL THR ASP LEU ASP LEU SER ALA TYR LEU LYS
SEQRES 27 A 470 SER LEU THR ARG MET LYS ALA VAL PRO ALA PHE ASP GLN
SEQRES 28 A 470 LEU ASP LEU THR SER PRO GLU ASN ASN LEU PHE GLY ASP
SEQRES 29 A 470 ALA THR ALA LYS ALA LYS HIS PHE THR ALA LEU ALA GLN
SEQRES 30 A 470 THR ARG SER THR VAL THR ALA GLN LEU ALA ASP ALA GLU
SEQRES 31 A 470 LEU ILE GLN ALA ILE ASN PRO LEU SER TYR LEU THR THR
SEQRES 32 A 470 THR SER SER GLN VAL ALA LYS HIS TRP ARG ILE ARG HIS
SEQRES 33 A 470 GLY ALA ALA ASP ARG ASP THR SER PHE ALA ILE PRO ILE
SEQRES 34 A 470 ILE LEU ALA ILE MET LEU GLU ASN HIS GLY TYR GLY ILE
SEQRES 35 A 470 ASP PHE ALA LEU PRO TRP ASP ILE PRO HIS SER GLY ASP
SEQRES 36 A 470 TYR ASP LEU GLY ASP LEU PHE SER TRP ILE ASP GLY LEU
SEQRES 37 A 470 CYS GLN
SEQRES 1 B 470 SER MET SER ASN ARG LEU ILE PHE ASP ALA ASP TRP LEU
SEQRES 2 B 470 VAL PRO GLU GLN VAL GLN VAL ALA GLY GLN ALA ILE GLN
SEQRES 3 B 470 TYR TYR ALA ALA ARG ASN ILE GLN TYR VAL GLN HIS PRO
SEQRES 4 B 470 VAL ALA ALA ILE GLN VAL LEU ASN VAL PHE VAL PRO ALA
SEQRES 5 B 470 ALA TYR LEU HIS GLY SER SER VAL ASN GLY TYR GLN ARG
SEQRES 6 B 470 ALA THR ALA PRO ILE LEU MET PRO ASN THR VAL GLY GLY
SEQRES 7 B 470 TYR LEU PRO GLY PRO ALA ASP ASP PRO GLN ARG VAL THR
SEQRES 8 B 470 TRP PRO THR ASN ALA GLY THR ILE GLN GLN ALA LEU LYS
SEQRES 9 B 470 ARG GLY TYR VAL VAL VAL ALA ALA GLY ILE ARG GLY ARG
SEQRES 10 B 470 THR THR VAL ASP LYS SER GLY GLN ARG VAL GLY GLN ALA
SEQRES 11 B 470 PRO ALA PHE ILE VAL ASP MET LYS ALA ALA ILE ARG TYR
SEQRES 12 B 470 VAL LYS TYR ASN GLN GLY ARG LEU PRO GLY ASP ALA ASN
SEQRES 13 B 470 ARG ILE ILE THR ASN GLY THR ALA ALA GLY GLY ALA THR
SEQRES 14 B 470 SER ALA LEU ALA GLY ALA SER GLY ASN SER ALA TYR PHE
SEQRES 15 B 470 GLU PRO ALA LEU THR ALA LEU GLY ALA ALA PRO ALA THR
SEQRES 16 B 470 ASP ASP ILE PHE ALA VAL SER ALA TYR CYS PRO ILE HIS
SEQRES 17 B 470 ASN LEU GLU HIS ALA ASP MET ALA TYR GLU TRP GLN PHE
SEQRES 18 B 470 ASN GLY ILE ASN ASP TRP HIS ARG TYR GLN PRO VAL ALA
SEQRES 19 B 470 GLY THR THR LYS ASN GLY ARG PRO LYS PHE GLU PRO VAL
SEQRES 20 B 470 SER GLY GLN LEU THR VAL GLU GLU GLN ALA LEU SER LEU
SEQRES 21 B 470 ALA LEU LYS ALA GLN PHE SER THR TYR LEU ASN GLN LEU
SEQRES 22 B 470 LYS LEU THR ALA SER ASP GLY THR HIS LEU THR LEU ASN
SEQRES 23 B 470 GLU ALA GLY MET GLY SER PHE ARG ASP VAL VAL ARG GLN
SEQRES 24 B 470 LEU LEU ILE SER SER ALA GLN THR ALA PHE ASP GLN GLY
SEQRES 25 B 470 THR ASP ILE HIS LYS TYR ALA GLY PHE VAL VAL THR GLY
SEQRES 26 B 470 ASN GLN VAL THR ASP LEU ASP LEU SER ALA TYR LEU LYS
SEQRES 27 B 470 SER LEU THR ARG MET LYS ALA VAL PRO ALA PHE ASP GLN
SEQRES 28 B 470 LEU ASP LEU THR SER PRO GLU ASN ASN LEU PHE GLY ASP
SEQRES 29 B 470 ALA THR ALA LYS ALA LYS HIS PHE THR ALA LEU ALA GLN
SEQRES 30 B 470 THR ARG SER THR VAL THR ALA GLN LEU ALA ASP ALA GLU
SEQRES 31 B 470 LEU ILE GLN ALA ILE ASN PRO LEU SER TYR LEU THR THR
SEQRES 32 B 470 THR SER SER GLN VAL ALA LYS HIS TRP ARG ILE ARG HIS
SEQRES 33 B 470 GLY ALA ALA ASP ARG ASP THR SER PHE ALA ILE PRO ILE
SEQRES 34 B 470 ILE LEU ALA ILE MET LEU GLU ASN HIS GLY TYR GLY ILE
SEQRES 35 B 470 ASP PHE ALA LEU PRO TRP ASP ILE PRO HIS SER GLY ASP
SEQRES 36 B 470 TYR ASP LEU GLY ASP LEU PHE SER TRP ILE ASP GLY LEU
SEQRES 37 B 470 CYS GLN
HET EGR A 501 14
HET PG4 A 502 13
HET PEG A 503 7
HET PGE A 504 10
HET PEG A 505 7
HET PEG A 506 7
HET PEG A 507 7
HET EGR B 501 14
HET PGE B 502 10
HET PEG B 503 7
HET PEG B 504 7
HET PEG B 505 7
HET PEG B 506 7
HETNAM EGR ETHYL 3,4,5-TRIHYDROXYBENZOATE
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PGE TRIETHYLENE GLYCOL
HETSYN EGR ETHYL GALLATE
FORMUL 3 EGR 2(C9 H10 O5)
FORMUL 4 PG4 C8 H18 O5
FORMUL 5 PEG 8(C4 H10 O3)
FORMUL 6 PGE 2(C6 H14 O4)
FORMUL 16 HOH *1132(H2 O)
HELIX 1 1 ASP A 8 LEU A 12 5 5
HELIX 2 2 ALA A 52 HIS A 55 5 4
HELIX 3 3 ASN A 94 ARG A 104 1 11
HELIX 4 4 PRO A 130 ASN A 146 1 17
HELIX 5 5 ALA A 163 SER A 175 1 13
HELIX 6 6 SER A 178 TYR A 180 5 3
HELIX 7 7 PHE A 181 GLY A 189 1 9
HELIX 8 8 ASN A 208 ASN A 221 1 14
HELIX 9 9 THR A 251 LEU A 272 1 22
HELIX 10 10 GLY A 290 GLN A 310 1 21
HELIX 11 11 ASP A 313 TYR A 317 5 5
HELIX 12 12 ASP A 331 THR A 340 1 10
HELIX 13 13 SER A 355 PHE A 361 1 7
HELIX 14 14 THR A 372 ARG A 378 1 7
HELIX 15 15 ASP A 387 ILE A 394 1 8
HELIX 16 16 ASN A 395 LEU A 400 5 6
HELIX 17 17 PHE A 424 HIS A 437 1 14
HELIX 18 18 ASP A 456 GLN A 469 1 14
HELIX 19 19 ASP B 8 LEU B 12 5 5
HELIX 20 20 ALA B 52 HIS B 55 5 4
HELIX 21 21 ASN B 94 GLY B 105 1 12
HELIX 22 22 PRO B 130 ASN B 146 1 17
HELIX 23 23 ALA B 163 SER B 175 1 13
HELIX 24 24 SER B 178 TYR B 180 5 3
HELIX 25 25 PHE B 181 GLY B 189 1 9
HELIX 26 26 ASN B 208 ASN B 221 1 14
HELIX 27 27 THR B 251 LEU B 272 1 22
HELIX 28 28 GLY B 290 ASP B 309 1 20
HELIX 29 29 ASP B 313 TYR B 317 5 5
HELIX 30 30 ASP B 331 THR B 340 1 10
HELIX 31 31 SER B 355 PHE B 361 1 7
HELIX 32 32 THR B 372 ARG B 378 1 7
HELIX 33 33 ASP B 387 ILE B 394 1 8
HELIX 34 34 ASN B 395 LEU B 400 5 6
HELIX 35 35 PHE B 424 HIS B 437 1 14
HELIX 36 36 ASP B 456 GLN B 469 1 14
SHEET 1 A 9 VAL A 13 VAL A 19 0
SHEET 2 A 9 GLN A 22 GLN A 33 -1 O ILE A 24 N VAL A 17
SHEET 3 A 9 VAL A 44 PRO A 50 -1 O VAL A 47 N ALA A 29
SHEET 4 A 9 VAL A 107 ALA A 111 -1 O VAL A 108 N PHE A 48
SHEET 5 A 9 ILE A 69 PRO A 72 1 N LEU A 70 O VAL A 107
SHEET 6 A 9 ILE A 157 THR A 162 1 O ILE A 158 N MET A 71
SHEET 7 A 9 ALA A 199 TYR A 203 1 O TYR A 203 N GLY A 161
SHEET 8 A 9 HIS A 410 ARG A 414 1 O HIS A 410 N VAL A 200
SHEET 9 A 9 GLY A 440 ALA A 444 1 O GLY A 440 N TRP A 411
SHEET 1 B 2 ASP A 225 PRO A 231 0
SHEET 2 B 2 PHE A 243 GLN A 249 -1 O GLU A 244 N GLN A 230
SHEET 1 C 2 PHE A 320 THR A 323 0
SHEET 2 C 2 GLN A 326 LEU A 330 -1 O GLN A 326 N THR A 323
SHEET 1 D 9 VAL B 13 VAL B 19 0
SHEET 2 D 9 GLN B 22 GLN B 33 -1 O TYR B 26 N GLU B 15
SHEET 3 D 9 VAL B 44 PRO B 50 -1 O VAL B 47 N ALA B 29
SHEET 4 D 9 VAL B 107 ALA B 111 -1 O VAL B 108 N PHE B 48
SHEET 5 D 9 ILE B 69 PRO B 72 1 N LEU B 70 O VAL B 107
SHEET 6 D 9 ILE B 157 ASN B 160 1 O ILE B 158 N MET B 71
SHEET 7 D 9 ALA B 199 TYR B 203 1 O SER B 201 N THR B 159
SHEET 8 D 9 HIS B 410 ARG B 414 1 O ARG B 412 N VAL B 200
SHEET 9 D 9 GLY B 440 ALA B 444 1 O ASP B 442 N TRP B 411
SHEET 1 E 2 ASP B 225 THR B 235 0
SHEET 2 E 2 PRO B 241 GLN B 249 -1 O VAL B 246 N ARG B 228
SHEET 1 F 2 PHE B 320 THR B 323 0
SHEET 2 F 2 GLN B 326 LEU B 330 -1 O GLN B 326 N THR B 323
CISPEP 1 TRP A 91 PRO A 92 0 -1.24
CISPEP 2 ALA A 129 PRO A 130 0 3.89
CISPEP 3 VAL A 345 PRO A 346 0 -3.21
CISPEP 4 TRP B 91 PRO B 92 0 -0.26
CISPEP 5 ALA B 129 PRO B 130 0 3.43
CISPEP 6 VAL B 345 PRO B 346 0 -6.79
SITE 1 AC1 13 GLY A 76 GLY A 77 TYR A 78 ALA A 163
SITE 2 AC1 13 ALA A 164 LYS A 343 GLU A 357 ASP A 421
SITE 3 AC1 13 HIS A 451 HOH A 711 HOH A 781 HOH A1035
SITE 4 AC1 13 HOH A1057
SITE 1 AC2 10 SER A 379 VAL A 381 THR A 382 ALA A 383
SITE 2 AC2 10 GLN B 124 LYS B 144 GLN B 147 ASN B 155
SITE 3 AC2 10 HOH B 754 HOH B1006
SITE 1 AC3 3 ASN A 224 LEU A 250 GLN A 255
SITE 1 AC4 10 TRP A 218 LYS A 262 ALA A 287 GLY A 288
SITE 2 AC4 10 MET A 289 ARG A 293 LEU A 332 SER A 333
SITE 3 AC4 10 LEU A 336 HOH A1014
SITE 1 AC5 1 HOH A 998
SITE 1 AC6 5 TYR A 180 HOH A 621 HOH A 784 PEG B 506
SITE 2 AC6 5 HOH B 899
SITE 1 AC7 4 ARG A 293 ARG A 297 SER A 333 HOH A 825
SITE 1 AC8 12 GLY B 76 GLY B 77 TYR B 78 ALA B 163
SITE 2 AC8 12 ALA B 164 ILE B 206 LYS B 343 PHE B 348
SITE 3 AC8 12 GLU B 357 ASP B 421 HIS B 451 HOH B 874
SITE 1 AC9 7 TRP B 218 LYS B 262 ALA B 287 GLY B 288
SITE 2 AC9 7 ARG B 293 SER B 333 LEU B 336
SITE 1 BC1 2 GLY B 324 ASN B 325
SITE 1 BC2 5 ILE B 432 GLU B 435 HOH B 863 HOH B1040
SITE 2 BC2 5 HOH B1132
SITE 1 BC3 7 THR A 380 VAL A 381 ARG B 141 GLU B 182
SITE 2 BC3 7 PRO B 192 ALA B 193 HOH B 973
SITE 1 BC4 4 PEG A 506 HOH A 621 TYR B 180 HOH B 979
CRYST1 47.212 62.943 84.412 70.66 85.49 79.51 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 0.021181 -0.003920 -0.000427 0.00000
SCALE2 0.000000 0.016157 -0.005520 0.00000
SCALE3 0.000000 0.000000 0.012558 0.00000
TER 3617 GLN A 469
TER 7248 GLN B 469
MASTER 465 0 13 36 26 0 26 6 8421 2 117 74
END |