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HEADER HYDROLASE 31-JAN-13 4J0J
TITLE TANNIN ACYL HYDROLASE IN COMPLEX WITH ETHYL 3,5-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 4J0J 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. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.2_869)
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.220
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 112872
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 5659
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 19.6924 - 6.1528 0.97 3636 184 0.1787 0.1788
REMARK 3 2 6.1528 - 4.9086 0.98 3634 186 0.1868 0.2017
REMARK 3 3 4.9086 - 4.2954 0.99 3666 191 0.1533 0.1492
REMARK 3 4 4.2954 - 3.9060 0.98 3594 181 0.1543 0.1797
REMARK 3 5 3.9060 - 3.6279 0.98 3685 194 0.1708 0.1958
REMARK 3 6 3.6279 - 3.4152 0.98 3687 191 0.1630 0.2069
REMARK 3 7 3.4152 - 3.2450 0.98 3623 185 0.1694 0.2265
REMARK 3 8 3.2450 - 3.1043 0.98 3603 188 0.1760 0.2162
REMARK 3 9 3.1043 - 2.9852 0.98 3616 182 0.1730 0.2239
REMARK 3 10 2.9852 - 2.8825 0.98 3639 172 0.1763 0.1758
REMARK 3 11 2.8825 - 2.7926 0.98 3659 204 0.1874 0.2256
REMARK 3 12 2.7926 - 2.7130 0.97 3554 172 0.1887 0.2105
REMARK 3 13 2.7130 - 2.6418 0.98 3707 203 0.1827 0.2171
REMARK 3 14 2.6418 - 2.5774 0.97 3561 164 0.1792 0.2241
REMARK 3 15 2.5774 - 2.5190 0.97 3596 210 0.1886 0.2320
REMARK 3 16 2.5190 - 2.4655 0.96 3608 183 0.1843 0.2292
REMARK 3 17 2.4655 - 2.4162 0.96 3523 203 0.1794 0.2397
REMARK 3 18 2.4162 - 2.3707 0.96 3593 226 0.1818 0.2270
REMARK 3 19 2.3707 - 2.3284 0.96 3490 184 0.1916 0.2302
REMARK 3 20 2.3284 - 2.2890 0.95 3619 161 0.2025 0.2910
REMARK 3 21 2.2890 - 2.2522 0.95 3535 189 0.2042 0.2486
REMARK 3 22 2.2522 - 2.2176 0.96 3550 169 0.2039 0.2428
REMARK 3 23 2.2176 - 2.1850 0.95 3520 203 0.2115 0.2436
REMARK 3 24 2.1850 - 2.1543 0.94 3501 184 0.2163 0.2766
REMARK 3 25 2.1543 - 2.1252 0.94 3482 168 0.2233 0.2319
REMARK 3 26 2.1252 - 2.0976 0.94 3473 171 0.2174 0.2508
REMARK 3 27 2.0976 - 2.0714 0.94 3518 212 0.2417 0.2494
REMARK 3 28 2.0714 - 2.0465 0.94 3488 200 0.2464 0.3044
REMARK 3 29 2.0465 - 2.0227 0.94 3382 182 0.2574 0.3016
REMARK 3 30 2.0227 - 2.0000 0.93 3471 217 0.2658 0.3178
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.90
REMARK 3 SHRINKAGE RADIUS : 0.60
REMARK 3 K_SOL : 0.43
REMARK 3 B_SOL : 60.67
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.790
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.73350
REMARK 3 B22 (A**2) : -16.52350
REMARK 3 B33 (A**2) : -1.38440
REMARK 3 B12 (A**2) : -4.16070
REMARK 3 B13 (A**2) : 12.64530
REMARK 3 B23 (A**2) : -4.84510
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 : 0.005 7453
REMARK 3 ANGLE : 0.917 10193
REMARK 3 CHIRALITY : 0.062 1147
REMARK 3 PLANARITY : 0.004 1340
REMARK 3 DIHEDRAL : 14.815 2651
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain 'A' and (resseq 0:188)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.5678 108.9390 83.7433
REMARK 3 T TENSOR
REMARK 3 T11: 0.2644 T22: 0.1427
REMARK 3 T33: 0.1399 T12: 0.0113
REMARK 3 T13: -0.0021 T23: 0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.5179 L22: 1.6485
REMARK 3 L33: 1.8121 L12: 0.1767
REMARK 3 L13: 0.0398 L23: 0.3227
REMARK 3 S TENSOR
REMARK 3 S11: 0.0441 S12: -0.0211 S13: 0.0708
REMARK 3 S21: 0.1482 S22: 0.0318 S23: -0.1427
REMARK 3 S31: -0.2450 S32: -0.0037 S33: 0.0020
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resseq 189:272)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4495 89.4083 67.2430
REMARK 3 T TENSOR
REMARK 3 T11: 0.2077 T22: 0.2122
REMARK 3 T33: 0.2347 T12: 0.0344
REMARK 3 T13: -0.0138 T23: -0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 0.8144 L22: 2.0908
REMARK 3 L33: 1.7792 L12: 0.9954
REMARK 3 L13: 0.4224 L23: 0.7618
REMARK 3 S TENSOR
REMARK 3 S11: -0.0933 S12: 0.0217 S13: 0.3086
REMARK 3 S21: -0.0881 S22: -0.0981 S23: 0.5042
REMARK 3 S31: 0.0730 S32: -0.3282 S33: 0.0590
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resseq 273:469)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.9518 85.0419 73.3173
REMARK 3 T TENSOR
REMARK 3 T11: 0.1880 T22: 0.1584
REMARK 3 T33: 0.1206 T12: 0.0278
REMARK 3 T13: -0.0188 T23: 0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 0.3794 L22: 1.6183
REMARK 3 L33: 1.3393 L12: 0.1802
REMARK 3 L13: -0.2142 L23: 0.0259
REMARK 3 S TENSOR
REMARK 3 S11: -0.0278 S12: 0.0108 S13: -0.0041
REMARK 3 S21: 0.0661 S22: 0.0424 S23: -0.0936
REMARK 3 S31: 0.1231 S32: -0.0150 S33: -0.0164
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'B' and (resseq 0:208)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.2959 42.4589 34.3720
REMARK 3 T TENSOR
REMARK 3 T11: 0.0992 T22: 0.1597
REMARK 3 T33: 0.1650 T12: 0.0068
REMARK 3 T13: -0.0091 T23: -0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 0.4411 L22: 0.8963
REMARK 3 L33: 0.3221 L12: -0.1154
REMARK 3 L13: -0.1575 L23: 0.3668
REMARK 3 S TENSOR
REMARK 3 S11: -0.0285 S12: 0.0082 S13: -0.1207
REMARK 3 S21: -0.1163 S22: 0.0138 S23: -0.0969
REMARK 3 S31: 0.0717 S32: -0.0161 S33: -0.0024
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain 'B' and (resseq 209:235)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.5839 69.1856 38.2149
REMARK 3 T TENSOR
REMARK 3 T11: 0.2611 T22: 0.2481
REMARK 3 T33: 0.1620 T12: -0.0127
REMARK 3 T13: -0.0958 T23: -0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 0.0789 L22: 0.9387
REMARK 3 L33: 0.1241 L12: 0.0640
REMARK 3 L13: 0.0053 L23: 0.3122
REMARK 3 S TENSOR
REMARK 3 S11: -0.0114 S12: 0.1291 S13: -0.1200
REMARK 3 S21: -0.5477 S22: 0.0705 S23: 0.1836
REMARK 3 S31: -0.0370 S32: -0.0182 S33: 0.0673
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain 'B' and (resseq 236:272)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9300 69.0219 40.1278
REMARK 3 T TENSOR
REMARK 3 T11: 0.3089 T22: 0.2251
REMARK 3 T33: 0.2070 T12: 0.0650
REMARK 3 T13: -0.0384 T23: -0.0393
REMARK 3 L TENSOR
REMARK 3 L11: 0.3085 L22: 0.2131
REMARK 3 L33: 0.2132 L12: 0.1985
REMARK 3 L13: -0.2104 L23: -0.1189
REMARK 3 S TENSOR
REMARK 3 S11: 0.1870 S12: 0.0710 S13: -0.0048
REMARK 3 S21: -0.1440 S22: -0.0698 S23: 0.1167
REMARK 3 S31: 0.0426 S32: -0.0231 S33: 0.0131
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: chain 'B' and (resseq 273:469)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.1910 66.6476 41.3061
REMARK 3 T TENSOR
REMARK 3 T11: 0.1301 T22: 0.1969
REMARK 3 T33: 0.1540 T12: -0.0011
REMARK 3 T13: -0.0219 T23: -0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 0.5325 L22: 0.9772
REMARK 3 L33: 0.2721 L12: -0.0307
REMARK 3 L13: -0.1165 L23: 0.1481
REMARK 3 S TENSOR
REMARK 3 S11: 0.0123 S12: -0.0380 S13: 0.0656
REMARK 3 S21: -0.1171 S22: 0.0332 S23: -0.1006
REMARK 3 S31: -0.0651 S32: 0.0299 S33: 0.0103
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE ENTRY CONTAINS FRIEDEL PAIRS IN F_
REMARK 3 PLUS/MINUS COLUMNS
REMARK 4
REMARK 4 4J0J 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 RCSB077442.
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 : 113748
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.38000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.200
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: STRUCTURE FACTOR FILE CONTAINS FRIEDEL'S PAIRS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
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 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 SER A 163 OG
REMARK 470 SER B 163 OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 823 O HOH B 843 1.87
REMARK 500 OD2 ASP B 8 O HOH B 814 1.96
REMARK 500 O LEU B 150 O HOH B 686 1.99
REMARK 500 O HOH A 688 O HOH A 721 1.99
REMARK 500 O HOH B 829 O HOH B 837 2.01
REMARK 500 O HOH B 758 O HOH B 826 2.01
REMARK 500 OD2 ASP A 363 O HOH A 759 2.11
REMARK 500 OE2 GLU A 357 O12 E35 A 501 2.12
REMARK 500 O HOH B 671 O HOH B 673 2.13
REMARK 500 NE2 GLN A 298 O HOH A 744 2.14
REMARK 500 OG SER A 2 O HOH A 697 2.16
REMARK 500 O HOH A 715 O HOH A 726 2.16
REMARK 500 NH1 ARG A 297 O HOH A 783 2.17
REMARK 500 NE2 GLN B 271 O HOH B 803 2.17
REMARK 500 O HOH B 830 O HOH B 852 2.18
REMARK 500 ND2 ASN B 94 O HOH B 870 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 O HOH B 656 O HOH B 669 1545 2.06
REMARK 500 O HOH A 679 O HOH B 704 1556 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 PRO A 130 40.54 -103.95
REMARK 500 SER A 163 -117.08 61.36
REMARK 500 CYS A 204 57.72 29.30
REMARK 500 PRO A 231 130.68 -37.41
REMARK 500 ALA A 233 -116.70 -133.37
REMARK 500 THR A 236 -160.19 -108.39
REMARK 500 ASN A 238 26.83 -157.01
REMARK 500 THR A 340 143.37 75.01
REMARK 500 PHE A 371 18.55 -141.91
REMARK 500 PRO B 130 37.86 -99.26
REMARK 500 SER B 163 -118.60 64.32
REMARK 500 CYS B 204 57.31 30.04
REMARK 500 ARG B 228 -159.00 -151.01
REMARK 500 ALA B 233 104.62 19.36
REMARK 500 THR B 235 -163.17 -128.05
REMARK 500 THR B 236 -141.58 -97.58
REMARK 500 THR B 340 143.88 69.74
REMARK 500 PHE B 371 15.48 -143.41
REMARK 500 THR B 403 64.12 -118.34
REMARK 500 HIS B 451 97.31 -65.49
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 B 860 DISTANCE = 5.27 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE E35 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE E35 B 501
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 4J0J A 1 469 UNP B3Y018 B3Y018_LACPN 1 469
DBREF 4J0J B 1 469 UNP B3Y018 B3Y018_LACPN 1 469
SEQADV 4J0J MET A -21 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J HIS A -20 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J HIS A -19 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J HIS A -18 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J HIS A -17 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J HIS A -16 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J HIS A -15 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J SER A -14 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J SER A -13 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J GLY A -12 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J VAL A -11 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J ASP A -10 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J LEU A -9 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J GLY A -8 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J THR A -7 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J GLU A -6 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J ASN A -5 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J LEU A -4 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J TYR A -3 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J PHE A -2 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J GLN A -1 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J SER A 0 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J MET B -21 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J HIS B -20 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J HIS B -19 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J HIS B -18 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J HIS B -17 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J HIS B -16 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J HIS B -15 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J SER B -14 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J SER B -13 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J GLY B -12 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J VAL B -11 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J ASP B -10 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J LEU B -9 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J GLY B -8 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J THR B -7 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J GLU B -6 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J ASN B -5 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J LEU B -4 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J TYR B -3 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J PHE B -2 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J GLN B -1 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0J 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 E35 A 501 13
HET E35 B 501 13
HETNAM E35 ETHYL 3,5-DIHYDROXYBENZOATE
FORMUL 3 E35 2(C9 H10 O4)
FORMUL 5 HOH *501(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 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 ASN A 221 1 14
HELIX 9 9 THR A 251 LEU A 272 1 22
HELIX 10 10 GLY A 290 ASP A 309 1 20
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 SER 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 ARG A 412 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 VAL A 232 0
SHEET 2 B 2 LYS A 242 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 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 ASN B 160 1 O ILE B 158 N ILE B 69
SHEET 7 D 9 ALA B 199 TYR B 203 1 O ALA B 199 N ILE B 157
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 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 -5.64
CISPEP 2 ALA A 129 PRO A 130 0 3.68
CISPEP 3 VAL A 345 PRO A 346 0 -6.63
CISPEP 4 TRP B 91 PRO B 92 0 -3.47
CISPEP 5 ALA B 129 PRO B 130 0 1.94
CISPEP 6 VAL B 345 PRO B 346 0 -4.25
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 10 GLY B 76 GLY B 77 TYR B 78 SER B 163
SITE 2 AC2 10 ALA B 164 ILE B 206 LYS B 343 GLU B 357
SITE 3 AC2 10 ASP B 421 HIS B 451
CRYST1 46.251 62.726 83.466 70.47 86.55 79.13 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 0.021621 -0.004153 0.000067 0.00000
SCALE2 0.000000 0.016234 -0.005663 0.00000
SCALE3 0.000000 0.000000 0.012712 0.00000
TER 3617 GLN A 469
TER 7248 GLN B 469
MASTER 492 0 2 36 26 0 6 6 7699 2 26 76
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