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HEADER HYDROLASE 30-JAN-13 4J0C
TITLE TANNIN ACYL HYDROLASE FROM LACTOBACILLUS PLANTARUM (NATIVE STRUCTURE)
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, TANNASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WU,Q.WANG,X.PENG,H.WEN,Q.CHEN,W.J.MCKINSTRY
REVDAT 1 22-MAY-13 4J0C 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. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.68
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 100915
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 5038
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 19.6782 - 3.5486 0.98 9851 489 0.1788 0.1880
REMARK 3 2 3.5486 - 2.8193 0.98 9780 555 0.1544 0.1800
REMARK 3 3 2.8193 - 2.4637 0.97 9695 530 0.1466 0.1765
REMARK 3 4 2.4637 - 2.2387 0.97 9740 515 0.1379 0.1727
REMARK 3 5 2.2387 - 2.0785 0.97 9683 514 0.1356 0.1731
REMARK 3 6 2.0785 - 1.9560 0.96 9627 520 0.1453 0.1792
REMARK 3 7 1.9560 - 1.8582 0.96 9581 477 0.1591 0.2025
REMARK 3 8 1.8582 - 1.7773 0.96 9661 490 0.1866 0.2324
REMARK 3 9 1.7773 - 1.7090 0.95 9553 486 0.2190 0.2670
REMARK 3 10 1.7090 - 1.6500 0.87 8706 462 0.2693 0.2948
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.43
REMARK 3 B_SOL : 64.69
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.020
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.61
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 9.45330
REMARK 3 B22 (A**2) : -7.55680
REMARK 3 B33 (A**2) : -0.69100
REMARK 3 B12 (A**2) : -4.51680
REMARK 3 B13 (A**2) : 2.82990
REMARK 3 B23 (A**2) : -1.28570
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 : 0.009 7221
REMARK 3 ANGLE : 1.187 9850
REMARK 3 CHIRALITY : 0.078 1109
REMARK 3 PLANARITY : 0.005 1292
REMARK 3 DIHEDRAL : 13.266 2571
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (chain A and resid 1:51)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.7688 115.0219 87.3948
REMARK 3 T TENSOR
REMARK 3 T11: 0.3410 T22: 0.1061
REMARK 3 T33: 0.1301 T12: 0.0057
REMARK 3 T13: -0.0009 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.0935 L22: 0.2213
REMARK 3 L33: 0.2882 L12: -0.1233
REMARK 3 L13: 0.0041 L23: 0.0371
REMARK 3 S TENSOR
REMARK 3 S11: 0.0451 S12: 0.0010 S13: 0.0585
REMARK 3 S21: 0.2436 S22: 0.0247 S23: -0.0162
REMARK 3 S31: -0.2333 S32: -0.0291 S33: -0.0068
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (chain A and resid 52:127)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.2251 106.3228 84.8521
REMARK 3 T TENSOR
REMARK 3 T11: 0.2016 T22: 0.0846
REMARK 3 T33: 0.0883 T12: 0.0142
REMARK 3 T13: -0.0168 T23: 0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 0.1906 L22: 0.5186
REMARK 3 L33: 0.4310 L12: 0.0481
REMARK 3 L13: -0.0085 L23: 0.0949
REMARK 3 S TENSOR
REMARK 3 S11: -0.0165 S12: 0.0059 S13: 0.0390
REMARK 3 S21: 0.1931 S22: 0.0245 S23: -0.0266
REMARK 3 S31: -0.2607 S32: -0.0601 S33: 0.0643
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (chain A and resid 128:228)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.1225 98.7696 74.0389
REMARK 3 T TENSOR
REMARK 3 T11: 0.1226 T22: 0.1006
REMARK 3 T33: 0.1004 T12: 0.0077
REMARK 3 T13: -0.0154 T23: 0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 0.0982 L22: 0.5838
REMARK 3 L33: 0.5243 L12: -0.1257
REMARK 3 L13: -0.1482 L23: 0.0684
REMARK 3 S TENSOR
REMARK 3 S11: 0.0109 S12: 0.0425 S13: 0.0139
REMARK 3 S21: -0.0063 S22: 0.0079 S23: -0.0813
REMARK 3 S31: -0.0959 S32: 0.0092 S33: -0.0087
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (chain A and resid 247:282)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.1534 78.5993 61.3381
REMARK 3 T TENSOR
REMARK 3 T11: 0.1605 T22: 0.1234
REMARK 3 T33: 0.0823 T12: 0.0228
REMARK 3 T13: 0.0075 T23: -0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 0.2339 L22: 0.4471
REMARK 3 L33: 0.6225 L12: 0.1228
REMARK 3 L13: 0.1941 L23: -0.1598
REMARK 3 S TENSOR
REMARK 3 S11: -0.0910 S12: -0.0016 S13: -0.0476
REMARK 3 S21: -0.1734 S22: 0.0571 S23: 0.0417
REMARK 3 S31: 0.2805 S32: -0.0771 S33: 0.0571
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (chain A and resid 283:461)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.4236 84.6538 71.4276
REMARK 3 T TENSOR
REMARK 3 T11: 0.1133 T22: 0.0945
REMARK 3 T33: 0.0814 T12: 0.0077
REMARK 3 T13: -0.0020 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.2547 L22: 0.5403
REMARK 3 L33: 0.5834 L12: 0.0795
REMARK 3 L13: 0.0384 L23: 0.2050
REMARK 3 S TENSOR
REMARK 3 S11: -0.0228 S12: 0.0235 S13: 0.0027
REMARK 3 S21: 0.0409 S22: 0.0227 S23: -0.0228
REMARK 3 S31: 0.0908 S32: -0.0159 S33: -0.0009
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (chain A and resid 462:469)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.3260 92.8663 93.4296
REMARK 3 T TENSOR
REMARK 3 T11: 0.2626 T22: 0.1329
REMARK 3 T33: 0.1209 T12: 0.0171
REMARK 3 T13: -0.0681 T23: -0.0217
REMARK 3 L TENSOR
REMARK 3 L11: 1.4833 L22: 0.0012
REMARK 3 L33: 0.1515 L12: -0.0032
REMARK 3 L13: -0.1115 L23: -0.0044
REMARK 3 S TENSOR
REMARK 3 S11: -0.0309 S12: -0.2545 S13: 0.0946
REMARK 3 S21: 0.1119 S22: 0.0902 S23: -0.0985
REMARK 3 S31: -0.0348 S32: 0.0837 S33: 0.0086
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (chain B and resid 1:51)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.5332 34.7516 28.1963
REMARK 3 T TENSOR
REMARK 3 T11: 0.1161 T22: 0.1042
REMARK 3 T33: 0.1450 T12: 0.0047
REMARK 3 T13: 0.0122 T23: -0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 0.3086 L22: 0.4668
REMARK 3 L33: 0.6380 L12: 0.0883
REMARK 3 L13: -0.2253 L23: -0.1502
REMARK 3 S TENSOR
REMARK 3 S11: -0.0476 S12: 0.0488 S13: -0.0787
REMARK 3 S21: -0.1503 S22: 0.0018 S23: 0.0129
REMARK 3 S31: 0.1390 S32: -0.0293 S33: 0.0338
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (chain B and resid 52:127)
REMARK 3 ORIGIN FOR THE GROUP (A): 38.9274 44.2610 29.2237
REMARK 3 T TENSOR
REMARK 3 T11: -0.0513 T22: 0.0431
REMARK 3 T33: 0.0982 T12: 0.0608
REMARK 3 T13: 0.0379 T23: -0.0263
REMARK 3 L TENSOR
REMARK 3 L11: 0.1047 L22: 0.9062
REMARK 3 L33: 0.2177 L12: 0.0402
REMARK 3 L13: 0.0186 L23: 0.1115
REMARK 3 S TENSOR
REMARK 3 S11: -0.0013 S12: -0.0373 S13: -0.1490
REMARK 3 S21: -0.3607 S22: -0.0005 S23: 0.0319
REMARK 3 S31: 0.0892 S32: -0.0652 S33: 0.0432
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (chain B and resid 128:231)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.0413 51.2304 41.0819
REMARK 3 T TENSOR
REMARK 3 T11: 0.0209 T22: 0.0894
REMARK 3 T33: 0.0824 T12: 0.0075
REMARK 3 T13: -0.0137 T23: 0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 0.1481 L22: 1.2011
REMARK 3 L33: 0.1998 L12: -0.1379
REMARK 3 L13: 0.0165 L23: 0.2960
REMARK 3 S TENSOR
REMARK 3 S11: 0.0142 S12: -0.0312 S13: -0.0509
REMARK 3 S21: -0.0800 S22: -0.0274 S23: -0.0240
REMARK 3 S31: 0.0108 S32: -0.0335 S33: -0.0118
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (chain B and resid 245:282)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.6556 72.8313 47.0239
REMARK 3 T TENSOR
REMARK 3 T11: 0.0485 T22: 0.0835
REMARK 3 T33: 0.0718 T12: 0.0001
REMARK 3 T13: -0.0048 T23: -0.0418
REMARK 3 L TENSOR
REMARK 3 L11: 0.2337 L22: 0.5007
REMARK 3 L33: 0.5177 L12: -0.1275
REMARK 3 L13: 0.0555 L23: 0.0511
REMARK 3 S TENSOR
REMARK 3 S11: 0.0290 S12: 0.1000 S13: -0.0719
REMARK 3 S21: -0.0918 S22: 0.0035 S23: -0.0347
REMARK 3 S31: -0.1080 S32: 0.1264 S33: -0.1170
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (chain B and resid 283:461)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7606 66.4802 40.5640
REMARK 3 T TENSOR
REMARK 3 T11: 0.0451 T22: 0.0681
REMARK 3 T33: 0.0695 T12: 0.0062
REMARK 3 T13: -0.0067 T23: 0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 0.4267 L22: 0.8612
REMARK 3 L33: 0.3497 L12: -0.1082
REMARK 3 L13: -0.0181 L23: 0.3027
REMARK 3 S TENSOR
REMARK 3 S11: 0.0048 S12: -0.0795 S13: 0.0013
REMARK 3 S21: -0.1120 S22: 0.0230 S23: -0.0245
REMARK 3 S31: -0.0748 S32: 0.0114 S33: -0.0089
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (chain B and resid 462:469)
REMARK 3 ORIGIN FOR THE GROUP (A): 54.3054 53.2565 32.0311
REMARK 3 T TENSOR
REMARK 3 T11: 0.0767 T22: 0.1354
REMARK 3 T33: 0.2157 T12: 0.0103
REMARK 3 T13: 0.0286 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 0.0267 L22: 0.0335
REMARK 3 L33: 1.2450 L12: -0.0280
REMARK 3 L13: -0.1513 L23: 0.1832
REMARK 3 S TENSOR
REMARK 3 S11: -0.0434 S12: 0.0123 S13: -0.1624
REMARK 3 S21: -0.0737 S22: 0.0490 S23: -0.2448
REMARK 3 S31: 0.0068 S32: 0.3193 S33: -0.0428
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 4J0C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-FEB-13.
REMARK 100 THE RCSB ID CODE IS RCSB077435.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-NOV-10
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 : 100941
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.55000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
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 (%): 42.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRI-SODIUM CITRATE PH 5.5, 20%
REMARK 280 PEG 3000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 281K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 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 465 VAL B 232
REMARK 465 ALA B 233
REMARK 465 GLY B 234
REMARK 465 THR B 235
REMARK 465 THR B 236
REMARK 465 LYS B 237
REMARK 465 ASN B 238
REMARK 465 GLY B 239
REMARK 465 ARG B 240
REMARK 465 PRO B 241
REMARK 465 LYS B 242
REMARK 465 PHE B 243
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 OG SER A 404 OE1 GLN A 406 1.93
REMARK 500 O HOH B 914 O HOH B 937 2.03
REMARK 500 O HOH B 651 O HOH B 916 2.05
REMARK 500 O HOH A 786 O HOH A 787 2.05
REMARK 500 O HOH A 792 O HOH A 862 2.10
REMARK 500 O HOH B 842 O HOH B 917 2.12
REMARK 500 O HOH B 715 O HOH B 839 2.12
REMARK 500 O HOH A 727 O HOH A 864 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 840 O HOH B 857 1565 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 -124.35 65.50
REMARK 500 CYS A 204 57.73 36.51
REMARK 500 THR A 340 147.02 77.35
REMARK 500 PHE A 371 20.74 -141.64
REMARK 500 THR A 401 -4.86 -59.64
REMARK 500 TYR B 78 19.00 59.64
REMARK 500 PRO B 130 36.06 -98.53
REMARK 500 SER B 163 -127.93 72.00
REMARK 500 CYS B 204 59.65 34.80
REMARK 500 THR B 340 152.39 78.03
REMARK 500 ALA B 344 -159.73 -87.29
REMARK 500 PHE B 371 16.54 -143.53
REMARK 500 THR B 403 74.18 -119.76
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 885 DISTANCE = 5.66 ANGSTROMS
REMARK 525 HOH B 944 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH B 963 DISTANCE = 5.56 ANGSTROMS
REMARK 525 HOH B 964 DISTANCE = 9.31 ANGSTROMS
REMARK 525 HOH B 965 DISTANCE = 10.10 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG 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 1PE B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4J0D RELATED DB: PDB
REMARK 900 RELATED ID: 4J0G RELATED DB: PDB
REMARK 900 RELATED ID: 4J0H RELATED DB: PDB
REMARK 900 RELATED ID: 4J0I RELATED DB: PDB
REMARK 900 RELATED ID: 4J0J RELATED DB: PDB
REMARK 900 RELATED ID: 4J0K RELATED DB: PDB
REMARK 900 RELATED ID: 4JUI RELATED DB: PDB
DBREF 4J0C A 1 469 UNP B3Y018 B3Y018_LACPN 1 469
DBREF 4J0C B 1 469 UNP B3Y018 B3Y018_LACPN 1 469
SEQADV 4J0C MET A -21 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C HIS A -20 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C HIS A -19 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C HIS A -18 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C HIS A -17 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C HIS A -16 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C HIS A -15 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C SER A -14 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C SER A -13 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C GLY A -12 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C VAL A -11 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C ASP A -10 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C LEU A -9 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C GLY A -8 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C THR A -7 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C GLU A -6 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C ASN A -5 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C LEU A -4 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C TYR A -3 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C PHE A -2 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C GLN A -1 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C SER A 0 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C MET B -21 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C HIS B -20 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C HIS B -19 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C HIS B -18 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C HIS B -17 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C HIS B -16 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C HIS B -15 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C SER B -14 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C SER B -13 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C GLY B -12 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C VAL B -11 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C ASP B -10 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C LEU B -9 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C GLY B -8 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C THR B -7 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C GLU B -6 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C ASN B -5 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C LEU B -4 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C TYR B -3 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C PHE B -2 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C GLN B -1 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0C 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 PEG A 501 7
HET PEG A 502 7
HET 1PE B 501 16
HET PEG B 502 7
HET PEG B 503 7
HET PEG B 504 7
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 3 PEG 5(C4 H10 O3)
FORMUL 5 1PE C10 H22 O6
FORMUL 9 HOH *679(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 GLN B 310 1 21
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 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 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 TRP B 411
SHEET 1 E 2 ASP B 225 TYR B 229 0
SHEET 2 E 2 PRO B 245 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 -5.41
CISPEP 2 ALA A 129 PRO A 130 0 5.76
CISPEP 3 VAL A 345 PRO A 346 0 -11.35
CISPEP 4 TRP B 91 PRO B 92 0 -0.43
CISPEP 5 ALA B 129 PRO B 130 0 3.07
CISPEP 6 VAL B 345 PRO B 346 0 -8.10
SITE 1 AC1 6 ARG A 412 ARG A 414 ASP A 442 ASP A 459
SITE 2 AC1 6 HOH A 636 HOH A 779
SITE 1 AC2 7 TRP A 218 LYS A 262 ALA A 287 GLY A 288
SITE 2 AC2 7 ARG A 293 SER A 333 LEU A 336
SITE 1 AC3 10 ALA B 65 THR B 66 SER B 122 GLY B 123
SITE 2 AC3 10 GLN B 124 ASP B 153 ASN B 155 ARG B 156
SITE 3 AC3 10 HOH B 602 HOH B 870
SITE 1 AC4 6 TRP B 218 LYS B 262 ALA B 287 GLY B 288
SITE 2 AC4 6 ARG B 293 LEU B 336
SITE 1 AC5 3 PRO B 14 GLU B 15 GLN B 25
SITE 1 AC6 7 SER B 0 ASN B 3 GLN B 33 ASP B 329
SITE 2 AC6 7 LEU B 330 HOH B 684 HOH B 839
CRYST1 46.458 62.791 83.803 70.39 86.01 79.41 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 0.021525 -0.004024 -0.000188 0.00000
SCALE2 0.000000 0.016202 -0.005650 0.00000
SCALE3 0.000000 0.000000 0.012668 0.00000
TER 3480 GLN A 469
TER 7009 GLN B 469
MASTER 568 0 6 38 26 0 12 6 7675 2 51 76
END |