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HEADER HYDROLASE 31-JAN-13 4J0K
TITLE TANNIN ACYL HYDROLASE IN COMPLEX WITH ETHYL GALLATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TANNASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: 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 TANNIN, HYDROLASE, HYDROLYSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR B.REN,M.WU,Q.WANG,X.PENG,H.WEN,Q.CHEN,W.J.MCKINSTRY
REVDAT 1 22-MAY-13 4J0K 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. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 52453
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 2663
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 19.8933 - 5.4348 0.98 2634 143 0.2006 0.2342
REMARK 3 2 5.4348 - 4.3284 0.97 2612 143 0.1685 0.1606
REMARK 3 3 4.3284 - 3.7855 0.97 2608 132 0.1599 0.1677
REMARK 3 4 3.7855 - 3.4413 0.97 2627 139 0.1626 0.2030
REMARK 3 5 3.4413 - 3.1958 0.98 2649 138 0.1687 0.2568
REMARK 3 6 3.1958 - 3.0080 0.98 2640 131 0.1843 0.2304
REMARK 3 7 3.0080 - 2.8578 0.98 2643 129 0.1798 0.2276
REMARK 3 8 2.8578 - 2.7338 0.98 2638 141 0.1826 0.2450
REMARK 3 9 2.7338 - 2.6288 0.98 2665 151 0.1803 0.2394
REMARK 3 10 2.6288 - 2.5382 0.98 2612 149 0.1903 0.2566
REMARK 3 11 2.5382 - 2.4590 0.98 2639 147 0.2019 0.2284
REMARK 3 12 2.4590 - 2.3888 0.97 2640 123 0.2040 0.2937
REMARK 3 13 2.3888 - 2.3261 0.97 2620 134 0.2219 0.3019
REMARK 3 14 2.3261 - 2.2694 0.97 2570 155 0.2315 0.2948
REMARK 3 15 2.2694 - 2.2179 0.96 2610 143 0.2421 0.3059
REMARK 3 16 2.2179 - 2.1707 0.97 2601 150 0.2522 0.2752
REMARK 3 17 2.1707 - 2.1273 0.96 2600 133 0.2670 0.3126
REMARK 3 18 2.1273 - 2.0872 0.96 2541 149 0.2917 0.3698
REMARK 3 19 2.0872 - 2.0500 0.95 2641 133 0.3005 0.3327
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 : 0.95
REMARK 3 K_SOL : 0.38
REMARK 3 B_SOL : 47.24
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.460
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.630
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 11.86580
REMARK 3 B22 (A**2) : -11.50130
REMARK 3 B33 (A**2) : -0.36450
REMARK 3 B12 (A**2) : -5.20870
REMARK 3 B13 (A**2) : 8.91240
REMARK 3 B23 (A**2) : -5.00290
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 : 0.007 7353
REMARK 3 ANGLE : 0.934 10036
REMARK 3 CHIRALITY : 0.065 1124
REMARK 3 PLANARITY : 0.004 1313
REMARK 3 DIHEDRAL : 15.552 2626
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain 'A' and (resseq 1:228)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.6857 105.1422 80.3327
REMARK 3 T TENSOR
REMARK 3 T11: 0.2629 T22: 0.1501
REMARK 3 T33: 0.1729 T12: -0.0176
REMARK 3 T13: 0.0215 T23: 0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 0.2837 L22: 0.7214
REMARK 3 L33: 0.5184 L12: -0.0089
REMARK 3 L13: -0.0640 L23: 0.2930
REMARK 3 S TENSOR
REMARK 3 S11: 0.0587 S12: -0.0288 S13: 0.0791
REMARK 3 S21: 0.1519 S22: -0.0203 S23: -0.0668
REMARK 3 S31: -0.0823 S32: -0.0108 S33: -0.0432
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resseq 243:340)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.8927 75.1466 70.9977
REMARK 3 T TENSOR
REMARK 3 T11: 0.3263 T22: 0.1368
REMARK 3 T33: 0.1431 T12: -0.0049
REMARK 3 T13: 0.0421 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 0.4728 L22: 0.4182
REMARK 3 L33: 1.5031 L12: 0.3769
REMARK 3 L13: -0.3449 L23: -0.1669
REMARK 3 S TENSOR
REMARK 3 S11: -0.0076 S12: 0.0066 S13: -0.0414
REMARK 3 S21: -0.0281 S22: -0.0390 S23: 0.0050
REMARK 3 S31: -0.0112 S32: 0.0022 S33: 0.0570
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resseq 341:469)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.4166 91.1528 70.2757
REMARK 3 T TENSOR
REMARK 3 T11: 0.2840 T22: 0.1355
REMARK 3 T33: 0.1458 T12: -0.0161
REMARK 3 T13: 0.0115 T23: -0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 0.3187 L22: 0.4013
REMARK 3 L33: 1.0222 L12: 0.0045
REMARK 3 L13: -0.0960 L23: -0.2797
REMARK 3 S TENSOR
REMARK 3 S11: 0.0167 S12: 0.0505 S13: 0.0233
REMARK 3 S21: -0.0166 S22: 0.0251 S23: -0.0717
REMARK 3 S31: 0.0335 S32: -0.0133 S33: -0.0383
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'B' and (resseq 1:209)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.7159 42.0041 33.4135
REMARK 3 T TENSOR
REMARK 3 T11: 0.0639 T22: 0.1911
REMARK 3 T33: 0.1931 T12: 0.0244
REMARK 3 T13: -0.0166 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.2813 L22: 0.4960
REMARK 3 L33: 0.1794 L12: 0.0947
REMARK 3 L13: -0.2218 L23: -0.0877
REMARK 3 S TENSOR
REMARK 3 S11: -0.0186 S12: 0.0150 S13: -0.1021
REMARK 3 S21: -0.1208 S22: -0.0080 S23: -0.1193
REMARK 3 S31: 0.0544 S32: -0.0216 S33: -0.0027
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain 'B' and (resseq 210:311)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6465 71.4168 40.0091
REMARK 3 T TENSOR
REMARK 3 T11: 0.2790 T22: 0.1741
REMARK 3 T33: 0.2070 T12: -0.0390
REMARK 3 T13: 0.0400 T23: -0.0472
REMARK 3 L TENSOR
REMARK 3 L11: 0.9748 L22: 0.6208
REMARK 3 L33: 0.6196 L12: -0.0766
REMARK 3 L13: -0.2950 L23: -0.2007
REMARK 3 S TENSOR
REMARK 3 S11: 0.0106 S12: 0.0811 S13: -0.0287
REMARK 3 S21: -0.1741 S22: 0.0194 S23: 0.0376
REMARK 3 S31: 0.0002 S32: -0.0265 S33: -0.0555
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain 'B' and (resseq 312:469)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.1107 63.6820 40.0282
REMARK 3 T TENSOR
REMARK 3 T11: 0.1118 T22: 0.1823
REMARK 3 T33: 0.1882 T12: 0.0064
REMARK 3 T13: 0.0021 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.4743 L22: 0.4431
REMARK 3 L33: 0.3452 L12: 0.0372
REMARK 3 L13: -0.2231 L23: 0.1654
REMARK 3 S TENSOR
REMARK 3 S11: 0.0544 S12: 0.0061 S13: 0.0714
REMARK 3 S21: -0.1494 S22: 0.0418 S23: -0.1022
REMARK 3 S31: -0.1028 S32: 0.0126 S33: -0.0508
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 4J0K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-FEB-13.
REMARK 100 THE RCSB ID CODE IS RCSB077443.
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) : 0.9537
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 : 52480
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.39600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.500
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 (%): 43.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRI-SODIUM CITRATE PH 5.5, 20%
REMARK 280 PEG 3000, VAPOR DIFFUSION, SITTING DROP, 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 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 TYR A 229
REMARK 465 GLN A 230
REMARK 465 PRO A 231
REMARK 465 VAL A 232
REMARK 465 ALA A 233
REMARK 465 GLY A 234
REMARK 465 THR A 235
REMARK 465 THR A 236
REMARK 465 LYS A 237
REMARK 465 ASN A 238
REMARK 465 GLY A 239
REMARK 465 ARG A 240
REMARK 465 PRO A 241
REMARK 465 LYS A 242
REMARK 465 THR A 402
REMARK 465 THR A 403
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 MET A 1 O HOH A 799 1.85
REMARK 500 OE1 GLN B 384 O HOH B 844 1.88
REMARK 500 O HOH A 813 O HOH A 835 1.91
REMARK 500 O HOH A 792 O HOH A 816 1.93
REMARK 500 O GLY B 362 O HOH B 710 1.94
REMARK 500 NZ LYS A 121 O HOH A 855 1.96
REMARK 500 O HOH A 758 O HOH A 802 2.00
REMARK 500 O HOH A 813 O HOH A 814 2.00
REMARK 500 O HOH A 714 O HOH A 746 2.01
REMARK 500 O HOH B 757 O HOH B 758 2.01
REMARK 500 O HOH A 827 O HOH A 828 2.03
REMARK 500 O HOH A 829 O HOH A 830 2.08
REMARK 500 NH2 ARG A 378 O HOH A 694 2.08
REMARK 500 O GLY B 458 OG SER B 462 2.09
REMARK 500 O HOH A 693 O HOH A 702 2.09
REMARK 500 O LEU B 150 O HOH B 717 2.11
REMARK 500 NZ LYS B 237 O HOH B 843 2.12
REMARK 500 O HOH A 709 O HOH A 817 2.13
REMARK 500 O HOH B 826 O HOH B 827 2.13
REMARK 500 O HOH B 673 O HOH B 680 2.14
REMARK 500 N SER B 277 O HOH B 811 2.14
REMARK 500 O HOH A 672 O HOH A 709 2.15
REMARK 500 O HOH A 614 O HOH A 719 2.15
REMARK 500 N ALA B 9 O HOH B 741 2.16
REMARK 500 O HOH A 746 O HOH A 847 2.16
REMARK 500 O HOH A 693 O HOH B 863 2.16
REMARK 500 OD2 ASP B 442 O HOH B 860 2.17
REMARK 500 OE1 GLN B 469 O HOH B 782 2.17
REMARK 500 NH1 ARG A 4 O HOH A 799 2.17
REMARK 500 O HOH A 644 O HOH A 833 2.17
REMARK 500 OE1 GLN A 147 O HOH A 812 2.18
REMARK 500 NZ LYS A 144 O HOH A 761 2.18
REMARK 500 NE2 GLN B 298 O HOH B 700 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O1 PEG B 503 O1 PEG B 504 1655 2.11
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 MET A 71 79.64 -116.02
REMARK 500 ASP A 85 129.33 -171.11
REMARK 500 SER A 163 -123.09 61.34
REMARK 500 CYS A 204 61.24 32.01
REMARK 500 THR A 340 145.51 79.78
REMARK 500 ALA A 344 -158.71 -77.19
REMARK 500 ASP A 349 77.48 -100.38
REMARK 500 PHE A 371 21.29 -143.63
REMARK 500 ASN B 3 104.70 -55.28
REMARK 500 PRO B 130 38.79 -96.10
REMARK 500 SER B 163 -123.71 67.67
REMARK 500 CYS B 204 53.82 32.20
REMARK 500 ARG B 228 -156.31 -144.20
REMARK 500 HIS B 315 0.63 -52.89
REMARK 500 THR B 340 155.32 71.94
REMARK 500 ALA B 344 -168.33 -79.17
REMARK 500 PHE B 348 -51.13 -120.35
REMARK 500 SER B 452 -179.76 -171.94
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 807 DISTANCE = 6.47 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 PGE A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EGR B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 504
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: 4JUI RELATED DB: PDB
DBREF 4J0K A 1 469 UNP B3Y018 B3Y018_LACPN 1 469
DBREF 4J0K B 1 469 UNP B3Y018 B3Y018_LACPN 1 469
SEQADV 4J0K SER A 0 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0K SER B 0 UNP B3Y018 EXPRESSION TAG
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 SER 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 SER 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 PGE A 502 10
HET EGR B 501 14
HET PG4 B 502 13
HET PEG B 503 7
HET PEG B 504 7
HETNAM EGR ETHYL 3,4,5-TRIHYDROXYBENZOATE
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN EGR ETHYL GALLATE
FORMUL 3 EGR 2(C9 H10 O5)
FORMUL 4 PGE C6 H14 O4
FORMUL 6 PG4 C8 H18 O5
FORMUL 7 PEG 2(C4 H10 O3)
FORMUL 9 HOH *527(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 SER 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 GLU A 210 5 3
HELIX 9 9 HIS A 211 ASN A 221 1 11
HELIX 10 10 THR A 251 LYS A 273 1 23
HELIX 11 11 GLY A 290 ASP A 309 1 20
HELIX 12 12 ASP A 313 TYR A 317 5 5
HELIX 13 13 ASP A 331 THR A 340 1 10
HELIX 14 14 SER A 355 PHE A 361 1 7
HELIX 15 15 THR A 372 ARG A 378 1 7
HELIX 16 16 ASP A 387 ILE A 394 1 8
HELIX 17 17 ASN A 395 LEU A 400 5 6
HELIX 18 18 PHE A 424 HIS A 437 1 14
HELIX 19 19 ASP A 456 GLN A 469 1 14
HELIX 20 20 ASP B 8 LEU B 12 5 5
HELIX 21 21 ALA B 52 HIS B 55 5 4
HELIX 22 22 ASN B 94 GLY B 105 1 12
HELIX 23 23 PRO B 130 ASN B 146 1 17
HELIX 24 24 ASP B 153 ASN B 155 5 3
HELIX 25 25 SER B 163 SER B 175 1 13
HELIX 26 26 SER B 178 TYR B 180 5 3
HELIX 27 27 PHE B 181 GLY B 189 1 9
HELIX 28 28 ASN B 208 ASN B 221 1 14
HELIX 29 29 THR B 251 LEU B 272 1 22
HELIX 30 30 GLY B 290 ASP B 309 1 20
HELIX 31 31 ASP B 313 TYR B 317 5 5
HELIX 32 32 ASP B 331 THR B 340 1 10
HELIX 33 33 SER B 355 PHE B 361 1 7
HELIX 34 34 THR B 372 ARG B 378 1 7
HELIX 35 35 ASP B 387 ILE B 394 1 8
HELIX 36 36 PRO B 396 THR B 401 1 6
HELIX 37 37 PHE B 424 HIS B 437 1 14
HELIX 38 38 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 TYR A 26 N GLU A 15
SHEET 3 A 9 VAL A 44 PRO A 50 -1 O VAL A 49 N TYR A 27
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 ASN A 160 1 O ILE A 158 N MET A 71
SHEET 7 A 9 ALA A 199 TYR A 203 1 O ALA A 199 N ILE A 157
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 ASP A 442 N ILE A 413
SHEET 1 B 2 ASP A 225 ARG A 228 0
SHEET 2 B 2 VAL A 246 GLN A 249 -1 O VAL A 246 N ARG A 228
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 THR B 162 1 O ILE B 158 N MET B 71
SHEET 7 D 9 ALA B 199 TYR B 203 1 O TYR B 203 N GLY B 161
SHEET 8 D 9 HIS B 410 ARG B 414 1 O HIS B 410 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 LYS B 242 N VAL B 232
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 -3.96
CISPEP 2 ALA A 129 PRO A 130 0 1.09
CISPEP 3 VAL A 345 PRO A 346 0 -3.55
CISPEP 4 TRP B 91 PRO B 92 0 -3.57
CISPEP 5 ALA B 129 PRO B 130 0 -0.31
CISPEP 6 VAL B 345 PRO B 346 0 -8.51
SITE 1 AC1 10 GLY A 76 GLY A 77 TYR A 78 SER A 163
SITE 2 AC1 10 ALA A 164 ILE A 206 LYS A 343 GLU A 357
SITE 3 AC1 10 ASP A 421 HIS A 451
SITE 1 AC2 9 TRP A 218 GLN A 219 LYS A 262 ALA A 287
SITE 2 AC2 9 GLY A 288 ARG A 293 SER A 333 LEU A 336
SITE 3 AC2 9 HOH A 836
SITE 1 AC3 10 GLY B 76 GLY B 77 TYR B 78 SER B 163
SITE 2 AC3 10 ALA B 164 LYS B 343 GLU B 357 ASP B 421
SITE 3 AC3 10 HIS B 451 HOH B 802
SITE 1 AC4 11 ALA B 65 VAL B 119 SER B 122 GLY B 123
SITE 2 AC4 11 GLN B 124 ARG B 125 ASP B 153 ASN B 155
SITE 3 AC4 11 ARG B 156 HOH B 798 HOH B 832
SITE 1 AC5 6 LEU B 353 ALA B 368 LYS B 409 HIS B 410
SITE 2 AC5 6 PEG B 504 HOH B 713
SITE 1 AC6 6 ASP B 352 THR B 354 VAL B 381 LYS B 409
SITE 2 AC6 6 HIS B 410 PEG B 503
CRYST1 46.099 62.734 83.192 70.20 87.10 79.19 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 0.021692 -0.004143 0.000310 0.00000
SCALE2 0.000000 0.016228 -0.005782 0.00000
SCALE3 0.000000 0.000000 0.012777 0.00000
TER 3491 GLN A 469
TER 7117 GLN B 469
MASTER 457 0 6 38 26 0 16 6 7646 2 65 74
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