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HEADER HYDROLASE 30-JAN-13 4J0I
TITLE TANNIN ACYL HYDROLASE IN COMPLEX WITH 3,4-DIHYDROXYBENZOATE
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 4J0I 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. 1.75 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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.74
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 86020
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 4315
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 19.7425 - 5.4016 0.98 2742 153 0.1937 0.2167
REMARK 3 2 5.4016 - 4.3019 0.97 2687 170 0.1367 0.1446
REMARK 3 3 4.3019 - 3.7624 0.96 2709 146 0.1339 0.1608
REMARK 3 4 3.7624 - 3.4204 0.96 2686 147 0.1357 0.1386
REMARK 3 5 3.4204 - 3.1763 0.96 2685 141 0.1472 0.1693
REMARK 3 6 3.1763 - 2.9897 0.97 2702 146 0.1528 0.1839
REMARK 3 7 2.9897 - 2.8404 0.97 2758 133 0.1546 0.1750
REMARK 3 8 2.8404 - 2.7171 0.98 2739 140 0.1549 0.2032
REMARK 3 9 2.7171 - 2.6127 0.98 2724 151 0.1462 0.1785
REMARK 3 10 2.6127 - 2.5228 0.98 2760 148 0.1502 0.1982
REMARK 3 11 2.5228 - 2.4440 0.97 2705 157 0.1437 0.1973
REMARK 3 12 2.4440 - 2.3743 0.97 2785 134 0.1343 0.1765
REMARK 3 13 2.3743 - 2.3119 0.97 2715 147 0.1384 0.1791
REMARK 3 14 2.3119 - 2.2556 0.97 2748 147 0.1391 0.1929
REMARK 3 15 2.2556 - 2.2044 0.97 2732 135 0.1422 0.1851
REMARK 3 16 2.2044 - 2.1575 0.98 2715 148 0.1396 0.1770
REMARK 3 17 2.1575 - 2.1144 0.97 2719 147 0.1376 0.1946
REMARK 3 18 2.1144 - 2.0745 0.97 2809 139 0.1467 0.1581
REMARK 3 19 2.0745 - 2.0375 0.97 2701 136 0.1394 0.1885
REMARK 3 20 2.0375 - 2.0030 0.97 2743 147 0.1522 0.1843
REMARK 3 21 2.0030 - 1.9707 0.97 2693 144 0.1563 0.2221
REMARK 3 22 1.9707 - 1.9404 0.97 2697 154 0.1631 0.2300
REMARK 3 23 1.9404 - 1.9119 0.97 2760 146 0.1686 0.2181
REMARK 3 24 1.9119 - 1.8850 0.97 2720 150 0.1770 0.2275
REMARK 3 25 1.8850 - 1.8596 0.97 2668 127 0.1834 0.2345
REMARK 3 26 1.8596 - 1.8354 0.96 2752 140 0.2014 0.2499
REMARK 3 27 1.8354 - 1.8125 0.96 2725 148 0.2100 0.2678
REMARK 3 28 1.8125 - 1.7907 0.96 2650 125 0.2294 0.2847
REMARK 3 29 1.7907 - 1.7699 0.96 2775 141 0.2321 0.2715
REMARK 3 30 1.7699 - 1.7500 0.96 2701 128 0.2402 0.2764
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.41
REMARK 3 B_SOL : 57.89
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.450
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.32280
REMARK 3 B22 (A**2) : -6.24560
REMARK 3 B33 (A**2) : 0.92280
REMARK 3 B12 (A**2) : -2.57660
REMARK 3 B13 (A**2) : 4.73530
REMARK 3 B23 (A**2) : -0.34260
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 : 0.008 7507
REMARK 3 ANGLE : 1.081 10270
REMARK 3 CHIRALITY : 0.072 1153
REMARK 3 PLANARITY : 0.004 1352
REMARK 3 DIHEDRAL : 13.835 2706
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): 27.3119 105.0215 80.4441
REMARK 3 T TENSOR
REMARK 3 T11: 0.1266 T22: 0.1056
REMARK 3 T33: 0.0928 T12: 0.0125
REMARK 3 T13: -0.0120 T23: 0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 0.1819 L22: 1.2719
REMARK 3 L33: 0.8200 L12: 0.0442
REMARK 3 L13: 0.0139 L23: 0.2201
REMARK 3 S TENSOR
REMARK 3 S11: 0.0126 S12: 0.0079 S13: 0.0361
REMARK 3 S21: 0.1400 S22: -0.0032 S23: -0.0392
REMARK 3 S31: -0.1505 S32: -0.0117 S33: -0.0039
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resseq 247:340)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.9393 74.2810 71.1974
REMARK 3 T TENSOR
REMARK 3 T11: 0.1893 T22: 0.1166
REMARK 3 T33: 0.1138 T12: 0.0029
REMARK 3 T13: 0.0001 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 0.5650 L22: 0.9391
REMARK 3 L33: 1.7716 L12: 0.2546
REMARK 3 L13: -0.4513 L23: -0.2997
REMARK 3 S TENSOR
REMARK 3 S11: -0.0782 S12: 0.0160 S13: -0.0217
REMARK 3 S21: -0.0385 S22: 0.0396 S23: 0.0406
REMARK 3 S31: 0.2892 S32: -0.0677 S33: 0.0422
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resseq 341:469)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.9730 91.2379 70.2158
REMARK 3 T TENSOR
REMARK 3 T11: 0.0908 T22: 0.1167
REMARK 3 T33: 0.1073 T12: 0.0194
REMARK 3 T13: -0.0058 T23: -0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 0.4078 L22: 0.9869
REMARK 3 L33: 1.1178 L12: 0.2317
REMARK 3 L13: 0.0885 L23: 0.1056
REMARK 3 S TENSOR
REMARK 3 S11: 0.0080 S12: 0.0383 S13: 0.0011
REMARK 3 S21: 0.0450 S22: 0.0344 S23: -0.0828
REMARK 3 S31: 0.0185 S32: 0.0602 S33: -0.0381
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'B' and (resseq 1:209)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.6268 41.8716 33.6487
REMARK 3 T TENSOR
REMARK 3 T11: 0.0627 T22: 0.1004
REMARK 3 T33: 0.1072 T12: 0.0037
REMARK 3 T13: 0.0020 T23: -0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 0.4260 L22: 1.1477
REMARK 3 L33: 0.5280 L12: -0.0589
REMARK 3 L13: -0.1828 L23: 0.2650
REMARK 3 S TENSOR
REMARK 3 S11: -0.0053 S12: 0.0313 S13: -0.0609
REMARK 3 S21: -0.0754 S22: -0.0058 S23: -0.0419
REMARK 3 S31: 0.0294 S32: -0.0059 S33: 0.0218
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain 'B' and (resseq 210:311)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6624 71.7940 40.0784
REMARK 3 T TENSOR
REMARK 3 T11: 0.1211 T22: 0.0979
REMARK 3 T33: 0.0972 T12: -0.0076
REMARK 3 T13: -0.0073 T23: -0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 1.2889 L22: 1.3192
REMARK 3 L33: 0.8589 L12: -0.1212
REMARK 3 L13: -0.2678 L23: 0.1063
REMARK 3 S TENSOR
REMARK 3 S11: 0.0125 S12: 0.0404 S13: 0.0256
REMARK 3 S21: -0.2163 S22: 0.0159 S23: 0.0396
REMARK 3 S31: -0.0698 S32: -0.0846 S33: -0.0403
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain 'B' and (resseq 312:469)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7368 63.7449 39.9373
REMARK 3 T TENSOR
REMARK 3 T11: 0.0733 T22: 0.1059
REMARK 3 T33: 0.0816 T12: -0.0050
REMARK 3 T13: -0.0049 T23: -0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 0.4894 L22: 0.8905
REMARK 3 L33: 0.2937 L12: -0.0656
REMARK 3 L13: -0.0269 L23: 0.1077
REMARK 3 S TENSOR
REMARK 3 S11: 0.0090 S12: -0.0315 S13: -0.0015
REMARK 3 S21: -0.0770 S22: 0.0064 S23: -0.0329
REMARK 3 S31: -0.0393 S32: 0.0227 S33: -0.0116
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 4J0I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-FEB-13.
REMARK 100 THE RCSB ID CODE IS RCSB077441.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
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 : 328191
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.53000
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 (%): 42.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
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 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 SER A -14
REMARK 465 SER A -13
REMARK 465 GLY A -12
REMARK 465 VAL A -11
REMARK 465 ASP A -10
REMARK 465 LEU A -9
REMARK 465 GLY A -8
REMARK 465 THR A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
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 PHE A 243
REMARK 465 GLU A 244
REMARK 465 PRO A 245
REMARK 465 VAL A 246
REMARK 465 MET B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 SER B -14
REMARK 465 SER B -13
REMARK 465 GLY B -12
REMARK 465 VAL B -11
REMARK 465 ASP B -10
REMARK 465 LEU B -9
REMARK 465 GLY B -8
REMARK 465 THR B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLN B -1
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 B 237 CG CD CE NZ
REMARK 470 ARG B 240 CG CD NE CZ NH1 NH2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ILE B 140 CA CB CG1 CG2 CD1
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 B 747 O HOH B 830 1.81
REMARK 500 O HOH B 878 O HOH B 888 1.82
REMARK 500 OE1 GLN B 22 O HOH B 825 1.85
REMARK 500 O HOH B 905 O HOH B 970 1.85
REMARK 500 O HOH B 973 O HOH B 980 1.85
REMARK 500 O HOH B 979 O HOH B 987 1.87
REMARK 500 O HOH B 961 O HOH B 1005 1.87
REMARK 500 O HOH B 937 O HOH B 992 1.88
REMARK 500 O HOH B 912 O HOH B 953 1.89
REMARK 500 O HOH A 735 O HOH A 794 1.89
REMARK 500 O HOH B 977 O HOH B 988 1.90
REMARK 500 O HOH B 789 O HOH B 827 1.91
REMARK 500 O HOH A 794 O HOH A 818 1.92
REMARK 500 O HOH B 964 O HOH B 992 1.92
REMARK 500 O HOH A 866 O HOH A 870 1.93
REMARK 500 O HOH A 682 O HOH A 688 1.94
REMARK 500 O HOH A 958 O HOH A 965 1.94
REMARK 500 O HOH A 912 O HOH A 942 1.94
REMARK 500 O HOH A 757 O HOH A 807 1.95
REMARK 500 O HOH B 901 O HOH B 926 1.96
REMARK 500 O HOH B 882 O HOH B 904 1.96
REMARK 500 O HOH B 978 O HOH B 982 1.96
REMARK 500 O HOH A 722 O HOH A 962 1.97
REMARK 500 O HOH B 906 O HOH B 922 1.99
REMARK 500 O HOH A 839 O HOH A 948 2.00
REMARK 500 O HOH B 972 O HOH B 985 2.00
REMARK 500 OG1 THR B 267 O HOH B 974 2.00
REMARK 500 O HOH A 947 O HOH A 964 2.01
REMARK 500 OE1 GLN A 350 OG1 THR A 354 2.02
REMARK 500 OE1 GLN A 124 O HOH A 941 2.02
REMARK 500 NZ LYS B 103 O HOH B 897 2.03
REMARK 500 O HOH B 963 O HOH B 993 2.05
REMARK 500 O HOH B 814 O HOH B 882 2.05
REMARK 500 O HOH B 951 O HOH B 984 2.06
REMARK 500 OD1 ASP A 294 NH2 ARG A 297 2.07
REMARK 500 OE1 GLN B 350 OG1 THR B 354 2.07
REMARK 500 NH2 ARG B 64 O HOH B 966 2.07
REMARK 500 O1 PG4 B 502 O HOH B 987 2.08
REMARK 500 O HOH A 855 O HOH A 859 2.12
REMARK 500 O HOH A 750 O HOH A 888 2.13
REMARK 500 O HOH A 641 O HOH A 936 2.13
REMARK 500 O HOH A 921 O HOH A 937 2.14
REMARK 500 O HOH B 876 O HOH B 927 2.15
REMARK 500 O1 PEG B 506 O HOH B 921 2.15
REMARK 500 O HOH A 910 O HOH A 928 2.15
REMARK 500 O HOH A 733 O HOH A 827 2.15
REMARK 500 O HOH B 741 O HOH B 932 2.17
REMARK 500 OE1 GLN A 350 O HOH A 895 2.17
REMARK 500 OE1 GLN B 350 O HOH B 917 2.19
REMARK 500 O HOH A 790 O HOH A 814 2.19
REMARK 500
REMARK 500 THIS ENTRY HAS 51 CLOSE CONTACTS
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 O HOH B 986 O HOH B 998 1545 2.13
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 SER A 163 -121.60 64.74
REMARK 500 CYS A 204 58.04 31.20
REMARK 500 THR A 340 145.62 79.77
REMARK 500 ALA A 344 -158.63 -83.04
REMARK 500 PHE A 371 15.51 -145.45
REMARK 500 THR A 403 46.54 -109.50
REMARK 500 PRO B 130 33.24 -98.45
REMARK 500 SER B 163 -121.58 66.92
REMARK 500 CYS B 204 56.18 35.56
REMARK 500 ARG B 228 -156.11 -150.41
REMARK 500 LYS B 237 -37.64 -35.73
REMARK 500 THR B 340 152.80 78.59
REMARK 500 ALA B 344 -156.98 -85.90
REMARK 500 PHE B 348 -53.36 -121.08
REMARK 500 PHE B 371 16.76 -144.36
REMARK 500 HIS B 451 99.64 -69.10
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 952 DISTANCE = 5.26 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DHB A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG 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 DHB B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 507
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: 4J0J RELATED DB: PDB
REMARK 900 RELATED ID: 4J0K RELATED DB: PDB
REMARK 900 RELATED ID: 4JUI RELATED DB: PDB
DBREF 4J0I A 1 469 UNP B3Y018 B3Y018_LACPN 1 469
DBREF 4J0I B 1 469 UNP B3Y018 B3Y018_LACPN 1 469
SEQADV 4J0I MET A -21 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I HIS A -20 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I HIS A -19 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I HIS A -18 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I HIS A -17 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I HIS A -16 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I HIS A -15 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I SER A -14 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I SER A -13 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I GLY A -12 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I VAL A -11 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I ASP A -10 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I LEU A -9 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I GLY A -8 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I THR A -7 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I GLU A -6 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I ASN A -5 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I LEU A -4 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I TYR A -3 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I PHE A -2 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I GLN A -1 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I SER A 0 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I MET B -21 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I HIS B -20 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I HIS B -19 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I HIS B -18 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I HIS B -17 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I HIS B -16 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I HIS B -15 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I SER B -14 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I SER B -13 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I GLY B -12 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I VAL B -11 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I ASP B -10 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I LEU B -9 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I GLY B -8 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I THR B -7 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I GLU B -6 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I ASN B -5 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I LEU B -4 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I TYR B -3 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I PHE B -2 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I GLN B -1 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0I SER B 0 UNP B3Y018 EXPRESSION TAG
SEQRES 1 A 491 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 491 GLY THR GLU ASN LEU TYR PHE GLN SER MET SER ASN ARG
SEQRES 3 A 491 LEU ILE PHE ASP ALA ASP TRP LEU VAL PRO GLU GLN VAL
SEQRES 4 A 491 GLN VAL ALA GLY GLN ALA ILE GLN TYR TYR ALA ALA ARG
SEQRES 5 A 491 ASN ILE GLN TYR VAL GLN HIS PRO VAL ALA ALA ILE GLN
SEQRES 6 A 491 VAL LEU ASN VAL PHE VAL PRO ALA ALA TYR LEU HIS GLY
SEQRES 7 A 491 SER SER VAL ASN GLY TYR GLN ARG ALA THR ALA PRO ILE
SEQRES 8 A 491 LEU MET PRO ASN THR VAL GLY GLY TYR LEU PRO GLY PRO
SEQRES 9 A 491 ALA ASP ASP PRO GLN ARG VAL THR TRP PRO THR ASN ALA
SEQRES 10 A 491 GLY THR ILE GLN GLN ALA LEU LYS ARG GLY TYR VAL VAL
SEQRES 11 A 491 VAL ALA ALA GLY ILE ARG GLY ARG THR THR VAL ASP LYS
SEQRES 12 A 491 SER GLY GLN ARG VAL GLY GLN ALA PRO ALA PHE ILE VAL
SEQRES 13 A 491 ASP MET LYS ALA ALA ILE ARG TYR VAL LYS TYR ASN GLN
SEQRES 14 A 491 GLY ARG LEU PRO GLY ASP ALA ASN ARG ILE ILE THR ASN
SEQRES 15 A 491 GLY THR SER ALA GLY GLY ALA THR SER ALA LEU ALA GLY
SEQRES 16 A 491 ALA SER GLY ASN SER ALA TYR PHE GLU PRO ALA LEU THR
SEQRES 17 A 491 ALA LEU GLY ALA ALA PRO ALA THR ASP ASP ILE PHE ALA
SEQRES 18 A 491 VAL SER ALA TYR CYS PRO ILE HIS ASN LEU GLU HIS ALA
SEQRES 19 A 491 ASP MET ALA TYR GLU TRP GLN PHE ASN GLY ILE ASN ASP
SEQRES 20 A 491 TRP HIS ARG TYR GLN PRO VAL ALA GLY THR THR LYS ASN
SEQRES 21 A 491 GLY ARG PRO LYS PHE GLU PRO VAL SER GLY GLN LEU THR
SEQRES 22 A 491 VAL GLU GLU GLN ALA LEU SER LEU ALA LEU LYS ALA GLN
SEQRES 23 A 491 PHE SER THR TYR LEU ASN GLN LEU LYS LEU THR ALA SER
SEQRES 24 A 491 ASP GLY THR HIS LEU THR LEU ASN GLU ALA GLY MET GLY
SEQRES 25 A 491 SER PHE ARG ASP VAL VAL ARG GLN LEU LEU ILE SER SER
SEQRES 26 A 491 ALA GLN THR ALA PHE ASP GLN GLY THR ASP ILE HIS LYS
SEQRES 27 A 491 TYR ALA GLY PHE VAL VAL THR GLY ASN GLN VAL THR ASP
SEQRES 28 A 491 LEU ASP LEU SER ALA TYR LEU LYS SER LEU THR ARG MET
SEQRES 29 A 491 LYS ALA VAL PRO ALA PHE ASP GLN LEU ASP LEU THR SER
SEQRES 30 A 491 PRO GLU ASN ASN LEU PHE GLY ASP ALA THR ALA LYS ALA
SEQRES 31 A 491 LYS HIS PHE THR ALA LEU ALA GLN THR ARG SER THR VAL
SEQRES 32 A 491 THR ALA GLN LEU ALA ASP ALA GLU LEU ILE GLN ALA ILE
SEQRES 33 A 491 ASN PRO LEU SER TYR LEU THR THR THR SER SER GLN VAL
SEQRES 34 A 491 ALA LYS HIS TRP ARG ILE ARG HIS GLY ALA ALA ASP ARG
SEQRES 35 A 491 ASP THR SER PHE ALA ILE PRO ILE ILE LEU ALA ILE MET
SEQRES 36 A 491 LEU GLU ASN HIS GLY TYR GLY ILE ASP PHE ALA LEU PRO
SEQRES 37 A 491 TRP ASP ILE PRO HIS SER GLY ASP TYR ASP LEU GLY ASP
SEQRES 38 A 491 LEU PHE SER TRP ILE ASP GLY LEU CYS GLN
SEQRES 1 B 491 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 491 GLY THR GLU ASN LEU TYR PHE GLN SER MET SER ASN ARG
SEQRES 3 B 491 LEU ILE PHE ASP ALA ASP TRP LEU VAL PRO GLU GLN VAL
SEQRES 4 B 491 GLN VAL ALA GLY GLN ALA ILE GLN TYR TYR ALA ALA ARG
SEQRES 5 B 491 ASN ILE GLN TYR VAL GLN HIS PRO VAL ALA ALA ILE GLN
SEQRES 6 B 491 VAL LEU ASN VAL PHE VAL PRO ALA ALA TYR LEU HIS GLY
SEQRES 7 B 491 SER SER VAL ASN GLY TYR GLN ARG ALA THR ALA PRO ILE
SEQRES 8 B 491 LEU MET PRO ASN THR VAL GLY GLY TYR LEU PRO GLY PRO
SEQRES 9 B 491 ALA ASP ASP PRO GLN ARG VAL THR TRP PRO THR ASN ALA
SEQRES 10 B 491 GLY THR ILE GLN GLN ALA LEU LYS ARG GLY TYR VAL VAL
SEQRES 11 B 491 VAL ALA ALA GLY ILE ARG GLY ARG THR THR VAL ASP LYS
SEQRES 12 B 491 SER GLY GLN ARG VAL GLY GLN ALA PRO ALA PHE ILE VAL
SEQRES 13 B 491 ASP MET LYS ALA ALA ILE ARG TYR VAL LYS TYR ASN GLN
SEQRES 14 B 491 GLY ARG LEU PRO GLY ASP ALA ASN ARG ILE ILE THR ASN
SEQRES 15 B 491 GLY THR SER ALA GLY GLY ALA THR SER ALA LEU ALA GLY
SEQRES 16 B 491 ALA SER GLY ASN SER ALA TYR PHE GLU PRO ALA LEU THR
SEQRES 17 B 491 ALA LEU GLY ALA ALA PRO ALA THR ASP ASP ILE PHE ALA
SEQRES 18 B 491 VAL SER ALA TYR CYS PRO ILE HIS ASN LEU GLU HIS ALA
SEQRES 19 B 491 ASP MET ALA TYR GLU TRP GLN PHE ASN GLY ILE ASN ASP
SEQRES 20 B 491 TRP HIS ARG TYR GLN PRO VAL ALA GLY THR THR LYS ASN
SEQRES 21 B 491 GLY ARG PRO LYS PHE GLU PRO VAL SER GLY GLN LEU THR
SEQRES 22 B 491 VAL GLU GLU GLN ALA LEU SER LEU ALA LEU LYS ALA GLN
SEQRES 23 B 491 PHE SER THR TYR LEU ASN GLN LEU LYS LEU THR ALA SER
SEQRES 24 B 491 ASP GLY THR HIS LEU THR LEU ASN GLU ALA GLY MET GLY
SEQRES 25 B 491 SER PHE ARG ASP VAL VAL ARG GLN LEU LEU ILE SER SER
SEQRES 26 B 491 ALA GLN THR ALA PHE ASP GLN GLY THR ASP ILE HIS LYS
SEQRES 27 B 491 TYR ALA GLY PHE VAL VAL THR GLY ASN GLN VAL THR ASP
SEQRES 28 B 491 LEU ASP LEU SER ALA TYR LEU LYS SER LEU THR ARG MET
SEQRES 29 B 491 LYS ALA VAL PRO ALA PHE ASP GLN LEU ASP LEU THR SER
SEQRES 30 B 491 PRO GLU ASN ASN LEU PHE GLY ASP ALA THR ALA LYS ALA
SEQRES 31 B 491 LYS HIS PHE THR ALA LEU ALA GLN THR ARG SER THR VAL
SEQRES 32 B 491 THR ALA GLN LEU ALA ASP ALA GLU LEU ILE GLN ALA ILE
SEQRES 33 B 491 ASN PRO LEU SER TYR LEU THR THR THR SER SER GLN VAL
SEQRES 34 B 491 ALA LYS HIS TRP ARG ILE ARG HIS GLY ALA ALA ASP ARG
SEQRES 35 B 491 ASP THR SER PHE ALA ILE PRO ILE ILE LEU ALA ILE MET
SEQRES 36 B 491 LEU GLU ASN HIS GLY TYR GLY ILE ASP PHE ALA LEU PRO
SEQRES 37 B 491 TRP ASP ILE PRO HIS SER GLY ASP TYR ASP LEU GLY ASP
SEQRES 38 B 491 LEU PHE SER TRP ILE ASP GLY LEU CYS GLN
HET DHB A 501 11
HET PEG A 502 7
HET PEG A 503 7
HET DHB B 501 11
HET PG4 B 502 13
HET PEG B 503 7
HET PEG B 504 7
HET PEG B 505 7
HET PEG B 506 7
HET PEG B 507 7
HETNAM DHB 3,4-DIHYDROXYBENZOIC ACID
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PG4 TETRAETHYLENE GLYCOL
FORMUL 3 DHB 2(C7 H6 O4)
FORMUL 4 PEG 7(C4 H10 O3)
FORMUL 7 PG4 C8 H18 O5
FORMUL 13 HOH *775(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 GLY A 105 1 12
HELIX 4 4 PRO A 130 ASN A 146 1 17
HELIX 5 5 ASP A 153 ASN A 155 5 3
HELIX 6 6 SER A 163 SER A 175 1 13
HELIX 7 7 SER A 178 TYR A 180 5 3
HELIX 8 8 PHE A 181 GLY A 189 1 9
HELIX 9 9 ASN A 208 ASN A 221 1 14
HELIX 10 10 THR A 251 LEU A 272 1 22
HELIX 11 11 GLY A 290 GLN A 310 1 21
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 ASN B 395 LEU B 400 5 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 GLN A 22 N VAL A 19
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 ASP A 442 N ILE A 413
SHEET 1 B 2 ASP A 225 TRP A 226 0
SHEET 2 B 2 GLY A 248 GLN A 249 -1 O GLY A 248 N TRP A 226
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 LEU B 45 N ILE B 32
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 ARG B 412 N VAL B 200
SHEET 9 D 9 GLY B 440 ALA B 444 1 O ASP B 442 N ILE B 413
SHEET 1 E 2 ASP B 225 PRO B 231 0
SHEET 2 E 2 PHE B 243 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 -1.72
CISPEP 2 ALA A 129 PRO A 130 0 4.64
CISPEP 3 VAL A 345 PRO A 346 0 -8.23
CISPEP 4 TRP B 91 PRO B 92 0 -1.47
CISPEP 5 ALA B 129 PRO B 130 0 4.03
CISPEP 6 VAL B 345 PRO B 346 0 -6.19
SITE 1 AC1 10 GLY A 76 GLY A 77 SER A 163 ALA A 164
SITE 2 AC1 10 LYS A 343 PHE A 348 GLU A 357 ASP A 421
SITE 3 AC1 10 HIS A 451 HOH A 648
SITE 1 AC2 8 TRP A 218 LYS A 262 ALA A 287 GLY A 288
SITE 2 AC2 8 ARG A 293 SER A 333 LEU A 336 HOH A 914
SITE 1 AC3 4 GLN A 100 GLY A 458 HOH A 953 GLU B 244
SITE 1 AC4 10 GLY B 76 GLY B 77 SER B 163 ALA B 164
SITE 2 AC4 10 LYS B 343 PHE B 348 GLU B 357 ASP B 421
SITE 3 AC4 10 HIS B 451 HOH B 659
SITE 1 AC5 8 ALA B 65 SER B 122 GLY B 123 GLN B 124
SITE 2 AC5 8 ASN B 155 HOH B 855 HOH B 979 HOH B 987
SITE 1 AC6 7 TRP B 218 LYS B 262 ALA B 287 GLY B 288
SITE 2 AC6 7 ARG B 293 LEU B 336 HOH B 799
SITE 1 AC7 2 GLU B 435 HOH B 880
SITE 1 AC8 6 GLU B 389 GLN B 392 SER B 398 TYR B 399
SITE 2 AC8 6 SER B 404 HOH B 836
SITE 1 AC9 5 PRO B 14 GLU B 15 GLN B 25 TYR B 27
SITE 2 AC9 5 HOH B 921
SITE 1 BC1 6 ALA B 40 ALA B 41 LYS B 121 HOH B 768
SITE 2 BC1 6 HOH B 934 HOH B 949
CRYST1 46.578 62.852 83.853 70.35 86.05 79.48 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 0.021469 -0.003988 -0.000177 0.00000
SCALE2 0.000000 0.016183 -0.005659 0.00000
SCALE3 0.000000 0.000000 0.012664 0.00000
TER 3515 GLN A 469
TER 7236 GLN B 469
MASTER 565 0 10 38 26 0 20 6 7883 2 84 76
END |