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HEADER HYDROLASE 30-JAN-13 4J0H
TITLE TANNIN ACYL HYDROLASE IN COMPLEX WITH GALLIC ACID
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, GALLIC ACID
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 4J0H 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. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.68
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.010
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 82229
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.151
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 4103
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 19.6809 - 5.4912 0.99 2723 151 0.1670 0.1791
REMARK 3 2 5.4912 - 4.3743 0.99 2731 143 0.1252 0.1391
REMARK 3 3 4.3743 - 3.8260 0.98 2714 151 0.1214 0.1515
REMARK 3 4 3.8260 - 3.4783 0.98 2698 140 0.1298 0.1520
REMARK 3 5 3.4783 - 3.2301 0.98 2735 138 0.1429 0.1698
REMARK 3 6 3.2301 - 3.0404 0.98 2740 131 0.1463 0.1769
REMARK 3 7 3.0404 - 2.8886 0.98 2707 147 0.1550 0.1494
REMARK 3 8 2.8886 - 2.7632 0.98 2679 159 0.1469 0.2075
REMARK 3 9 2.7632 - 2.6571 0.98 2740 122 0.1481 0.1778
REMARK 3 10 2.6571 - 2.5656 0.98 2699 141 0.1494 0.1993
REMARK 3 11 2.5656 - 2.4856 0.98 2692 156 0.1397 0.2048
REMARK 3 12 2.4856 - 2.4147 0.98 2678 150 0.1431 0.1758
REMARK 3 13 2.4147 - 2.3512 0.98 2699 164 0.1361 0.1746
REMARK 3 14 2.3512 - 2.2939 0.98 2695 130 0.1406 0.1932
REMARK 3 15 2.2939 - 2.2418 0.98 2664 157 0.1424 0.1829
REMARK 3 16 2.2418 - 2.1942 0.98 2722 139 0.1497 0.1886
REMARK 3 17 2.1942 - 2.1504 0.97 2669 147 0.1474 0.1815
REMARK 3 18 2.1504 - 2.1098 0.98 2718 125 0.1466 0.1912
REMARK 3 19 2.1098 - 2.0722 0.97 2618 149 0.1505 0.2034
REMARK 3 20 2.0722 - 2.0371 0.97 2718 129 0.1485 0.2004
REMARK 3 21 2.0371 - 2.0043 0.97 2731 120 0.1548 0.1750
REMARK 3 22 2.0043 - 1.9735 0.97 2630 139 0.1620 0.2077
REMARK 3 23 1.9735 - 1.9445 0.97 2713 132 0.1634 0.2058
REMARK 3 24 1.9445 - 1.9171 0.97 2694 151 0.1677 0.2141
REMARK 3 25 1.9171 - 1.8912 0.97 2659 125 0.1731 0.2092
REMARK 3 26 1.8912 - 1.8667 0.97 2697 144 0.1932 0.2161
REMARK 3 27 1.8667 - 1.8434 0.97 2642 143 0.1907 0.2391
REMARK 3 28 1.8434 - 1.8212 0.97 2663 138 0.2121 0.2655
REMARK 3 29 1.8212 - 1.8000 0.97 2658 142 0.2362 0.2970
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 : 0.40
REMARK 3 B_SOL : 40.67
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.920
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.91
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.28400
REMARK 3 B22 (A**2) : -2.77400
REMARK 3 B33 (A**2) : -0.51000
REMARK 3 B12 (A**2) : 0.61130
REMARK 3 B13 (A**2) : 0.47890
REMARK 3 B23 (A**2) : -1.21730
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 7520
REMARK 3 ANGLE : 1.000 10255
REMARK 3 CHIRALITY : 0.066 1146
REMARK 3 PLANARITY : 0.004 1342
REMARK 3 DIHEDRAL : 13.520 2704
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 1:232)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4226 104.8445 80.6352
REMARK 3 T TENSOR
REMARK 3 T11: 0.0600 T22: 0.0629
REMARK 3 T33: 0.0442 T12: -0.0141
REMARK 3 T13: 0.0024 T23: 0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 0.0615 L22: 0.7043
REMARK 3 L33: 0.9859 L12: -0.0583
REMARK 3 L13: 0.0912 L23: 0.5742
REMARK 3 S TENSOR
REMARK 3 S11: 0.0065 S12: 0.0052 S13: 0.0203
REMARK 3 S21: -0.0654 S22: -0.0068 S23: -0.0212
REMARK 3 S31: -0.1562 S32: 0.0353 S33: -0.0002
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resseq 233:340)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.7963 77.8564 72.0640
REMARK 3 T TENSOR
REMARK 3 T11: 0.1342 T22: 0.0572
REMARK 3 T33: 0.0564 T12: -0.0087
REMARK 3 T13: 0.0017 T23: -0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 0.4234 L22: 0.4320
REMARK 3 L33: 1.2074 L12: 0.2343
REMARK 3 L13: 0.1042 L23: 0.1002
REMARK 3 S TENSOR
REMARK 3 S11: 0.0631 S12: -0.0723 S13: 0.0075
REMARK 3 S21: 0.1040 S22: -0.0673 S23: 0.0431
REMARK 3 S31: 0.1535 S32: -0.0819 S33: -0.0029
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resseq 341:469)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.9833 91.3055 70.2607
REMARK 3 T TENSOR
REMARK 3 T11: 0.0802 T22: 0.0594
REMARK 3 T33: 0.0587 T12: 0.0217
REMARK 3 T13: -0.0093 T23: -0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 0.3261 L22: 0.6475
REMARK 3 L33: 1.0836 L12: 0.0410
REMARK 3 L13: 0.1653 L23: 0.2963
REMARK 3 S TENSOR
REMARK 3 S11: 0.0384 S12: 0.0331 S13: 0.0099
REMARK 3 S21: -0.0457 S22: 0.0020 S23: -0.0364
REMARK 3 S31: 0.0905 S32: 0.0743 S33: -0.0216
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'B' and (resseq 1:209)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.6117 41.9111 33.4411
REMARK 3 T TENSOR
REMARK 3 T11: 0.0443 T22: 0.0443
REMARK 3 T33: 0.0622 T12: -0.0043
REMARK 3 T13: 0.0148 T23: 0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 0.4066 L22: 0.9845
REMARK 3 L33: 0.4293 L12: -0.1277
REMARK 3 L13: -0.0820 L23: 0.3510
REMARK 3 S TENSOR
REMARK 3 S11: -0.0272 S12: 0.0316 S13: -0.0373
REMARK 3 S21: -0.0300 S22: 0.0195 S23: -0.0762
REMARK 3 S31: 0.0617 S32: -0.0001 S33: 0.0133
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain 'B' and (resseq 210:311)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.3171 71.6230 39.4316
REMARK 3 T TENSOR
REMARK 3 T11: 0.0273 T22: 0.0321
REMARK 3 T33: 0.0418 T12: 0.0040
REMARK 3 T13: -0.0010 T23: -0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 1.0366 L22: 0.5097
REMARK 3 L33: 0.4283 L12: -0.0379
REMARK 3 L13: -0.0440 L23: -0.1623
REMARK 3 S TENSOR
REMARK 3 S11: -0.0042 S12: -0.0288 S13: 0.0211
REMARK 3 S21: -0.0304 S22: 0.0204 S23: -0.0224
REMARK 3 S31: -0.0292 S32: -0.0715 S33: -0.0339
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain 'B' and (resseq 312:469)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.6005 63.6958 39.6389
REMARK 3 T TENSOR
REMARK 3 T11: 0.0264 T22: 0.0483
REMARK 3 T33: 0.0525 T12: 0.0030
REMARK 3 T13: -0.0129 T23: -0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.4339 L22: 0.6137
REMARK 3 L33: 0.2064 L12: 0.1218
REMARK 3 L13: -0.0886 L23: -0.0551
REMARK 3 S TENSOR
REMARK 3 S11: -0.0065 S12: -0.0297 S13: 0.0278
REMARK 3 S21: -0.0189 S22: 0.0138 S23: 0.0004
REMARK 3 S31: 0.0030 S32: -0.0072 S33: 0.0019
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 4J0H 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 RCSB077440.
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 : 82235
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.45600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.300
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 (%): 44.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
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 ARG B 240 NE CZ NH1 NH2
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 ND2 ASN B 60 O HOH B 1215 1.70
REMARK 500 O HOH A 878 O HOH A 1120 1.89
REMARK 500 O HOH B 889 O HOH B 1216 1.92
REMARK 500 NE2 GLN B 384 O HOH B 1227 1.94
REMARK 500 OD2 ASP B 120 O HOH B 1202 1.94
REMARK 500 OE1 GLU B 435 O HOH B 1197 1.97
REMARK 500 O HOH A 1123 O HOH A 1147 1.97
REMARK 500 O HOH B 1025 O HOH B 1204 1.97
REMARK 500 O HOH A 888 O HOH A 1119 1.98
REMARK 500 O HOH B 1175 O HOH B 1206 1.99
REMARK 500 O HOH A 790 O HOH A 1115 1.99
REMARK 500 O HOH A 1109 O HOH A 1148 1.99
REMARK 500 O HOH B 1180 O HOH B 1210 2.00
REMARK 500 NE2 GLN B 469 O HOH B 1196 2.00
REMARK 500 O HOH A 720 O HOH A 1120 2.01
REMARK 500 O HOH B 1069 O HOH B 1201 2.01
REMARK 500 O HOH A 747 O HOH B 1212 2.01
REMARK 500 O HOH B 1176 O HOH B 1195 2.03
REMARK 500 O HOH A 990 O HOH A 1160 2.04
REMARK 500 NE2 GLN B 271 O HOH B 1032 2.04
REMARK 500 O HOH A 949 O HOH A 1114 2.05
REMARK 500 O HOH B 1000 O HOH B 1197 2.05
REMARK 500 O HOH A 958 O HOH A 1117 2.05
REMARK 500 O HOH B 1141 O HOH B 1199 2.05
REMARK 500 O HOH B 1137 O HOH B 1243 2.07
REMARK 500 O HOH B 1038 O HOH B 1205 2.09
REMARK 500 O HOH A 1019 O HOH A 1134 2.09
REMARK 500 O HOH B 1245 O HOH B 1246 2.09
REMARK 500 O HOH B 700 O HOH B 884 2.09
REMARK 500 O HOH B 1006 O HOH B 1009 2.10
REMARK 500 O HOH B 1083 O HOH B 1225 2.10
REMARK 500 O HOH B 713 O HOH B 799 2.12
REMARK 500 O HOH A 704 O HOH A 956 2.14
REMARK 500 O HOH A 1105 O HOH A 1127 2.14
REMARK 500 O HOH A 1100 O HOH A 1130 2.14
REMARK 500 OE1 GLU B 253 O HOH B 1203 2.15
REMARK 500 O HOH B 1025 O HOH B 1031 2.16
REMARK 500 O HOH A 908 O HOH A 1115 2.17
REMARK 500 O HOH A 1016 O HOH B 1212 2.18
REMARK 500 O HOH A 965 O HOH A 973 2.18
REMARK 500 O HOH A 750 O HOH A 976 2.19
REMARK 500 O HOH A 963 O HOH A 1145 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 A 1158 O HOH B 1135 1565 2.17
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 -112.38 64.84
REMARK 500 CYS A 204 56.22 29.97
REMARK 500 ARG A 228 -159.42 -139.10
REMARK 500 THR A 340 142.42 82.22
REMARK 500 PHE A 371 16.08 -145.33
REMARK 500 SER A 404 27.23 -153.43
REMARK 500 PRO B 130 31.01 -99.51
REMARK 500 SER B 163 -117.69 58.21
REMARK 500 CYS B 204 57.31 30.38
REMARK 500 ARG B 228 -153.96 -148.79
REMARK 500 THR B 340 143.14 88.06
REMARK 500 PHE B 371 18.23 -143.61
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 902 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH A1133 DISTANCE = 5.10 ANGSTROMS
REMARK 525 HOH A1161 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH B1179 DISTANCE = 7.77 ANGSTROMS
REMARK 525 HOH B1181 DISTANCE = 5.47 ANGSTROMS
REMARK 525 HOH B1245 DISTANCE = 6.44 ANGSTROMS
REMARK 525 HOH B1246 DISTANCE = 5.93 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDE 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 PEG 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 GDE B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
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: 4J0I 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 4J0H A 1 469 UNP B3Y018 B3Y018_LACPN 1 469
DBREF 4J0H B 1 469 UNP B3Y018 B3Y018_LACPN 1 469
SEQADV 4J0H MET A -21 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H HIS A -20 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H HIS A -19 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H HIS A -18 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H HIS A -17 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H HIS A -16 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H HIS A -15 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H SER A -14 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H SER A -13 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H GLY A -12 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H VAL A -11 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H ASP A -10 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H LEU A -9 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H GLY A -8 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H THR A -7 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H GLU A -6 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H ASN A -5 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H LEU A -4 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H TYR A -3 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H PHE A -2 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H GLN A -1 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H SER A 0 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H MET B -21 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H HIS B -20 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H HIS B -19 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H HIS B -18 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H HIS B -17 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H HIS B -16 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H HIS B -15 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H SER B -14 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H SER B -13 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H GLY B -12 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H VAL B -11 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H ASP B -10 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H LEU B -9 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H GLY B -8 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H THR B -7 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H GLU B -6 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H ASN B -5 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H LEU B -4 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H TYR B -3 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H PHE B -2 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H GLN B -1 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0H 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 GDE A 501 12
HET PG4 A 502 13
HET PEG A 503 7
HET PEG A 504 7
HET PEG A 505 7
HET GDE B 501 12
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
HETNAM GDE 3,4,5-TRIHYDROXYBENZOIC ACID
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN GDE GALLATE
FORMUL 3 GDE 2(C7 H6 O5)
FORMUL 4 PG4 2(C8 H18 O5)
FORMUL 5 PEG 7(C4 H10 O3)
FORMUL 14 HOH *1214(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 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 LEU A 397 THR A 402 1 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 PRO B 396 THR B 401 1 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 TYR A 26 N GLU A 15
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 ASN A 160 1 O ILE A 158 N MET A 71
SHEET 7 A 9 ALA A 199 TYR A 203 1 O SER A 201 N THR A 159
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 THR A 235 0
SHEET 2 B 2 PRO A 241 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 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 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 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 4.33
CISPEP 3 VAL A 345 PRO A 346 0 -8.57
CISPEP 4 TRP B 91 PRO B 92 0 7.97
CISPEP 5 ALA B 129 PRO B 130 0 4.06
CISPEP 6 VAL B 345 PRO B 346 0 -8.91
SITE 1 AC1 13 GLY A 76 GLY A 77 TYR A 78 SER A 163
SITE 2 AC1 13 ALA A 164 ILE A 206 LYS A 343 GLU A 357
SITE 3 AC1 13 ASP A 421 HIS A 451 HOH A 650 HOH A 717
SITE 4 AC1 13 HOH A 912
SITE 1 AC2 6 TYR A 180 HOH A 621 HOH A 771 HOH A1142
SITE 2 AC2 6 TYR B 180 HOH B 910
SITE 1 AC3 9 TRP A 218 LYS A 262 ALA A 287 GLY A 288
SITE 2 AC3 9 MET A 289 ARG A 293 SER A 333 LEU A 336
SITE 3 AC3 9 HOH A1034
SITE 1 AC4 1 GLU A 435
SITE 1 AC5 8 SER A 0 MET A 1 HIS A 37 ARG A 293
SITE 2 AC5 8 ASP A 294 ARG A 297 HOH A 704 HOH A 956
SITE 1 AC6 13 GLY B 76 GLY B 77 TYR B 78 SER B 163
SITE 2 AC6 13 ALA B 164 ILE B 206 LYS B 343 GLU B 357
SITE 3 AC6 13 ASP B 421 HIS B 451 HOH B 868 HOH B1137
SITE 4 AC6 13 HOH B1243
SITE 1 AC7 8 SER A 379 VAL A 381 THR A 382 ALA A 383
SITE 2 AC7 8 HOH A 731 LYS B 144 ASN B 155 HOH B 934
SITE 1 AC8 10 TRP B 218 LYS B 262 ALA B 287 GLY B 288
SITE 2 AC8 10 MET B 289 ARG B 293 LEU B 332 SER B 333
SITE 3 AC8 10 LEU B 336 HOH B1162
SITE 1 AC9 3 VAL B 295 ALA B 431 HOH B1186
SITE 1 BC1 4 ASP B 10 GLY B 324 ASN B 325 HOH B1109
SITE 1 BC2 3 LEU A 250 GLN A 255 HOH A1121
CRYST1 47.551 62.960 84.474 70.74 85.18 79.55 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 0.021030 -0.003879 -0.000558 0.00000
SCALE2 0.000000 0.016151 -0.005476 0.00000
SCALE3 0.000000 0.000000 0.012544 0.00000
TER 3609 GLN A 469
TER 7244 GLN B 469
MASTER 533 0 11 36 26 0 24 6 8483 2 99 76
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