| 6keu-pdb | HEADER HYDROLASE 05-JUL-19 6KEU
TITLE WILDTYPE E53, A MICROBIAL HSL ESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B, C, D
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ERYTHROBACTER LONGUS;
SOURCE 3 ORGANISM_TAXID: 1044
KEYWDS ESTERASE, HYDROLASE, HORMONE-SENSITIVE LIPASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.C.YANG,Z.Y.LI,X.W.XU,J.X.LI
REVDAT 1 08-JUL-20 6KEU 0
JRNL AUTH X.C.YANG,H.YINGYI,Z.Y.LI,J.SHULING,R.ZHEN,W.ZHAO,C.HENGLIN,
JRNL AUTH 2 J.X.LI,X.W.XU
JRNL TITL WILDTYPE E53, A MICROBIAL HSL ESTERASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 139423
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.179
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.430
REMARK 3 FREE R VALUE TEST SET COUNT : 6865
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 42.4900 - 5.9700 0.99 9707 145 0.1502 0.1310
REMARK 3 2 5.9700 - 4.7400 1.00 9836 142 0.1420 0.1450
REMARK 3 3 4.7400 - 4.1400 1.00 9798 145 0.1161 0.1263
REMARK 3 4 4.1400 - 3.7600 1.00 9852 144 0.1320 0.1464
REMARK 3 5 3.7600 - 3.4900 1.00 9791 142 0.1453 0.1848
REMARK 3 6 3.4900 - 3.2900 1.00 9813 141 0.1536 0.1707
REMARK 3 7 3.2900 - 3.1200 1.00 9858 143 0.1660 0.1844
REMARK 3 8 3.1200 - 2.9900 1.00 9777 139 0.1707 0.1853
REMARK 3 9 2.9900 - 2.8700 1.00 9830 145 0.1708 0.1886
REMARK 3 10 2.8700 - 2.7700 1.00 9810 145 0.1690 0.2072
REMARK 3 11 2.7700 - 2.6900 1.00 9784 138 0.1663 0.2115
REMARK 3 12 2.6900 - 2.6100 1.00 9801 140 0.1662 0.2017
REMARK 3 13 2.6100 - 2.5400 1.00 9812 140 0.1665 0.2069
REMARK 3 14 2.5400 - 2.4800 1.00 9881 142 0.1667 0.1890
REMARK 3 15 2.4800 - 2.4200 1.00 9741 142 0.1692 0.2083
REMARK 3 16 2.4200 - 2.3700 1.00 9835 146 0.1680 0.1990
REMARK 3 17 2.3700 - 2.3200 1.00 9838 142 0.1615 0.1861
REMARK 3 18 2.3200 - 2.2800 1.00 9728 138 0.1595 0.1975
REMARK 3 19 2.2800 - 2.2400 1.00 9901 140 0.1594 0.1661
REMARK 3 20 2.2400 - 2.2000 1.00 9744 140 0.1623 0.2276
REMARK 3 21 2.2000 - 2.1700 1.00 9919 149 0.1696 0.1784
REMARK 3 22 2.1700 - 2.1300 1.00 9719 142 0.1714 0.1767
REMARK 3 23 2.1300 - 2.1000 1.00 9861 143 0.1774 0.2844
REMARK 3 24 2.1000 - 2.0700 1.00 9749 142 0.1787 0.2066
REMARK 3 25 2.0700 - 2.0400 1.00 9910 140 0.1810 0.2258
REMARK 3 26 2.0400 - 2.0200 1.00 9701 143 0.1856 0.2055
REMARK 3 27 2.0200 - 1.9900 1.00 9469 138 0.1849 0.2118
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.82
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 9502
REMARK 3 ANGLE : 0.825 12920
REMARK 3 CHIRALITY : 0.053 1476
REMARK 3 PLANARITY : 0.006 1705
REMARK 3 DIHEDRAL : 7.376 5708
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 6KEU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JUL-19.
REMARK 100 THE DEPOSITION ID IS D_1300012823.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-SEP-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 139433
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990
REMARK 200 RESOLUTION RANGE LOW (A) : 47.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 1.920
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 27.4200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.32200
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MR-ROSETTA
REMARK 200 STARTING MODEL: 4YPV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG MME550, BIS-TRIS, CALCIUM
REMARK 280 CHLORIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,-Y,-Z+1/2
REMARK 290 4555 -X+1/2,-Y,Z+1/2
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 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 35.30250
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 110.61950
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.30250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 110.61950
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH D 803 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 839 LIES ON A SPECIAL POSITION.
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 THR A 313
REMARK 465 ALA A 314
REMARK 465 THR B 313
REMARK 465 ALA B 314
REMARK 465 THR C 313
REMARK 465 ALA C 314
REMARK 465 THR D 313
REMARK 465 ALA D 314
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 THR A 4 OG1 CG2
REMARK 470 GLU A 76 CG CD OE1 OE2
REMARK 470 GLU A 79 CG CD OE1 OE2
REMARK 470 THR B 4 OG1 CG2
REMARK 470 THR C 4 OG1 CG2
REMARK 470 GLU C 76 CG CD OE1 OE2
REMARK 470 GLU C 79 CG CD OE1 OE2
REMARK 470 THR D 4 OG1 CG2
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 A 635 O HOH A 824 1.90
REMARK 500 OE2 GLU D 280 O HOH D 501 1.92
REMARK 500 OE1 GLU B 204 O HOH B 501 1.95
REMARK 500 O HOH A 501 O HOH A 849 2.01
REMARK 500 NH1 ARG C 47 O HOH C 501 2.03
REMARK 500 O HOH C 727 O HOH C 843 2.04
REMARK 500 O HOH C 556 O HOH C 767 2.11
REMARK 500 O HOH C 761 O HOH C 799 2.11
REMARK 500 O HOH C 533 O HOH C 768 2.11
REMARK 500 O HOH C 743 O HOH C 843 2.12
REMARK 500 NH2 ARG C 47 O HOH C 502 2.13
REMARK 500 O HOH C 767 O HOH C 871 2.14
REMARK 500 O HOH D 692 O HOH D 734 2.14
REMARK 500 O HOH C 800 O HOH C 815 2.15
REMARK 500 O HOH B 739 O HOH B 753 2.15
REMARK 500 NZ LYS B 214 O HOH B 501 2.16
REMARK 500 NZ LYS A 12 O HOH A 501 2.16
REMARK 500 O HOH A 640 O HOH A 854 2.17
REMARK 500 O HOH B 725 O HOH B 805 2.17
REMARK 500 O HOH A 607 O HOH A 774 2.18
REMARK 500 O HOH A 742 O HOH A 827 2.18
REMARK 500 O HOH C 802 O HOH C 875 2.18
REMARK 500 O HOH C 727 O HOH C 743 2.18
REMARK 500 O HOH C 556 O HOH C 657 2.19
REMARK 500 O HOH B 666 O HOH B 786 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 526 O HOH B 526 2754 1.80
REMARK 500 O HOH B 801 O HOH B 801 2754 1.90
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 ASP A 96 -162.16 -162.70
REMARK 500 SER A 162 -114.87 64.96
REMARK 500 LEU A 186 139.53 -170.19
REMARK 500 PHE A 191 67.54 20.04
REMARK 500 VAL A 211 -72.84 70.84
REMARK 500 ASP B 96 -162.78 -163.93
REMARK 500 SER B 162 -111.46 62.26
REMARK 500 PHE B 191 67.06 19.66
REMARK 500 VAL B 211 -71.21 67.96
REMARK 500 ASP C 96 -160.13 -166.31
REMARK 500 SER C 162 -114.53 63.30
REMARK 500 PHE C 191 65.33 21.02
REMARK 500 VAL C 211 -72.09 71.53
REMARK 500 ASP D 96 -160.09 -166.47
REMARK 500 SER D 162 -112.59 61.91
REMARK 500 LEU D 186 141.33 -171.92
REMARK 500 PHE D 191 66.89 20.13
REMARK 500 VAL D 211 -69.72 68.31
REMARK 500 HIS D 284 147.85 -38.76
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 934 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH C 901 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH D 846 DISTANCE = 6.53 ANGSTROMS
REMARK 525 HOH D 847 DISTANCE = 6.60 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue D8F A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue D8F B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue D8F C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6NA C 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue D8F D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 410
DBREF1 6KEU A 4 314 UNP A0A074MDU6_ERYLO
DBREF2 6KEU A A0A074MDU6 4 314
DBREF1 6KEU B 4 314 UNP A0A074MDU6_ERYLO
DBREF2 6KEU B A0A074MDU6 4 314
DBREF1 6KEU C 4 314 UNP A0A074MDU6_ERYLO
DBREF2 6KEU C A0A074MDU6 4 314
DBREF1 6KEU D 4 314 UNP A0A074MDU6_ERYLO
DBREF2 6KEU D A0A074MDU6 4 314
SEQRES 1 A 311 THR PRO PHE ILE ARG PRO ASP MET LYS ALA PHE LEU GLU
SEQRES 2 A 311 ALA ILE ALA ALA MET ALA GLY PRO THR LEU ALA GLU MET
SEQRES 3 A 311 THR LEU GLU GLU ALA ARG ALA SER TYR VAL ALA LEU HIS
SEQRES 4 A 311 GLY MET ALA ASP ARG PRO ALA ARG GLU LEU ALA VAL ILE
SEQRES 5 A 311 ARG ASN LEU SER CYS PRO GLY PRO ALA GLY ASP ILE PRO
SEQRES 6 A 311 LEU ARG LEU TYR ASP ALA ARG GLU SER ARG GLU ALA GLY
SEQRES 7 A 311 PRO VAL ILE THR PHE TYR HIS GLY GLY GLY PHE VAL ILE
SEQRES 8 A 311 GLY ASP LEU ASP THR HIS HIS ASN LEU CYS THR GLU ILE
SEQRES 9 A 311 ALA ALA LEU MET ASP LEU PRO VAL VAL ALA VAL ASP TYR
SEQRES 10 A 311 ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA ALA ILE GLU
SEQRES 11 A 311 ASP CYS GLU ALA ALA THR ARG TRP VAL ALA SER SER PRO
SEQRES 12 A 311 SER GLU LEU GLY ARG THR ALA SER GLY VAL ILE PRO ILE
SEQRES 13 A 311 GLY ASP SER ALA GLY GLY ASN ALA THR ILE VAL VAL SER
SEQRES 14 A 311 GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL PRO VAL VAL
SEQRES 15 A 311 LEU GLN VAL PRO ILE PHE PRO LEU ALA SER ASP ALA VAL
SEQRES 16 A 311 GLY SER ALA SER LEU GLU ALA PHE ALA GLU GLY PHE VAL
SEQRES 17 A 311 LEU THR LYS ALA SER ILE GLU PHE PHE ASP THR ALA TYR
SEQRES 18 A 311 LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE PRO ILE LEU
SEQRES 19 A 311 GLY ASP HIS THR ALA ALA PRO PRO THR ILE VAL ALA THR
SEQRES 20 A 311 ALA SER LEU ASP PRO ILE ARG ASP SER GLY ARG ASP TYR
SEQRES 21 A 311 ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP VAL VAL TYR
SEQRES 22 A 311 LEU GLU MET GLU GLY VAL THR HIS SER PHE THR ASN ILE
SEQRES 23 A 311 ARG ALA ALA VAL PRO SER THR GLN GLY ASP LEU GLU ARG
SEQRES 24 A 311 ILE ILE ALA ALA MET LYS MET MET LEU GLY THR ALA
SEQRES 1 B 311 THR PRO PHE ILE ARG PRO ASP MET LYS ALA PHE LEU GLU
SEQRES 2 B 311 ALA ILE ALA ALA MET ALA GLY PRO THR LEU ALA GLU MET
SEQRES 3 B 311 THR LEU GLU GLU ALA ARG ALA SER TYR VAL ALA LEU HIS
SEQRES 4 B 311 GLY MET ALA ASP ARG PRO ALA ARG GLU LEU ALA VAL ILE
SEQRES 5 B 311 ARG ASN LEU SER CYS PRO GLY PRO ALA GLY ASP ILE PRO
SEQRES 6 B 311 LEU ARG LEU TYR ASP ALA ARG GLU SER ARG GLU ALA GLY
SEQRES 7 B 311 PRO VAL ILE THR PHE TYR HIS GLY GLY GLY PHE VAL ILE
SEQRES 8 B 311 GLY ASP LEU ASP THR HIS HIS ASN LEU CYS THR GLU ILE
SEQRES 9 B 311 ALA ALA LEU MET ASP LEU PRO VAL VAL ALA VAL ASP TYR
SEQRES 10 B 311 ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA ALA ILE GLU
SEQRES 11 B 311 ASP CYS GLU ALA ALA THR ARG TRP VAL ALA SER SER PRO
SEQRES 12 B 311 SER GLU LEU GLY ARG THR ALA SER GLY VAL ILE PRO ILE
SEQRES 13 B 311 GLY ASP SER ALA GLY GLY ASN ALA THR ILE VAL VAL SER
SEQRES 14 B 311 GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL PRO VAL VAL
SEQRES 15 B 311 LEU GLN VAL PRO ILE PHE PRO LEU ALA SER ASP ALA VAL
SEQRES 16 B 311 GLY SER ALA SER LEU GLU ALA PHE ALA GLU GLY PHE VAL
SEQRES 17 B 311 LEU THR LYS ALA SER ILE GLU PHE PHE ASP THR ALA TYR
SEQRES 18 B 311 LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE PRO ILE LEU
SEQRES 19 B 311 GLY ASP HIS THR ALA ALA PRO PRO THR ILE VAL ALA THR
SEQRES 20 B 311 ALA SER LEU ASP PRO ILE ARG ASP SER GLY ARG ASP TYR
SEQRES 21 B 311 ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP VAL VAL TYR
SEQRES 22 B 311 LEU GLU MET GLU GLY VAL THR HIS SER PHE THR ASN ILE
SEQRES 23 B 311 ARG ALA ALA VAL PRO SER THR GLN GLY ASP LEU GLU ARG
SEQRES 24 B 311 ILE ILE ALA ALA MET LYS MET MET LEU GLY THR ALA
SEQRES 1 C 311 THR PRO PHE ILE ARG PRO ASP MET LYS ALA PHE LEU GLU
SEQRES 2 C 311 ALA ILE ALA ALA MET ALA GLY PRO THR LEU ALA GLU MET
SEQRES 3 C 311 THR LEU GLU GLU ALA ARG ALA SER TYR VAL ALA LEU HIS
SEQRES 4 C 311 GLY MET ALA ASP ARG PRO ALA ARG GLU LEU ALA VAL ILE
SEQRES 5 C 311 ARG ASN LEU SER CYS PRO GLY PRO ALA GLY ASP ILE PRO
SEQRES 6 C 311 LEU ARG LEU TYR ASP ALA ARG GLU SER ARG GLU ALA GLY
SEQRES 7 C 311 PRO VAL ILE THR PHE TYR HIS GLY GLY GLY PHE VAL ILE
SEQRES 8 C 311 GLY ASP LEU ASP THR HIS HIS ASN LEU CYS THR GLU ILE
SEQRES 9 C 311 ALA ALA LEU MET ASP LEU PRO VAL VAL ALA VAL ASP TYR
SEQRES 10 C 311 ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA ALA ILE GLU
SEQRES 11 C 311 ASP CYS GLU ALA ALA THR ARG TRP VAL ALA SER SER PRO
SEQRES 12 C 311 SER GLU LEU GLY ARG THR ALA SER GLY VAL ILE PRO ILE
SEQRES 13 C 311 GLY ASP SER ALA GLY GLY ASN ALA THR ILE VAL VAL SER
SEQRES 14 C 311 GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL PRO VAL VAL
SEQRES 15 C 311 LEU GLN VAL PRO ILE PHE PRO LEU ALA SER ASP ALA VAL
SEQRES 16 C 311 GLY SER ALA SER LEU GLU ALA PHE ALA GLU GLY PHE VAL
SEQRES 17 C 311 LEU THR LYS ALA SER ILE GLU PHE PHE ASP THR ALA TYR
SEQRES 18 C 311 LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE PRO ILE LEU
SEQRES 19 C 311 GLY ASP HIS THR ALA ALA PRO PRO THR ILE VAL ALA THR
SEQRES 20 C 311 ALA SER LEU ASP PRO ILE ARG ASP SER GLY ARG ASP TYR
SEQRES 21 C 311 ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP VAL VAL TYR
SEQRES 22 C 311 LEU GLU MET GLU GLY VAL THR HIS SER PHE THR ASN ILE
SEQRES 23 C 311 ARG ALA ALA VAL PRO SER THR GLN GLY ASP LEU GLU ARG
SEQRES 24 C 311 ILE ILE ALA ALA MET LYS MET MET LEU GLY THR ALA
SEQRES 1 D 311 THR PRO PHE ILE ARG PRO ASP MET LYS ALA PHE LEU GLU
SEQRES 2 D 311 ALA ILE ALA ALA MET ALA GLY PRO THR LEU ALA GLU MET
SEQRES 3 D 311 THR LEU GLU GLU ALA ARG ALA SER TYR VAL ALA LEU HIS
SEQRES 4 D 311 GLY MET ALA ASP ARG PRO ALA ARG GLU LEU ALA VAL ILE
SEQRES 5 D 311 ARG ASN LEU SER CYS PRO GLY PRO ALA GLY ASP ILE PRO
SEQRES 6 D 311 LEU ARG LEU TYR ASP ALA ARG GLU SER ARG GLU ALA GLY
SEQRES 7 D 311 PRO VAL ILE THR PHE TYR HIS GLY GLY GLY PHE VAL ILE
SEQRES 8 D 311 GLY ASP LEU ASP THR HIS HIS ASN LEU CYS THR GLU ILE
SEQRES 9 D 311 ALA ALA LEU MET ASP LEU PRO VAL VAL ALA VAL ASP TYR
SEQRES 10 D 311 ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA ALA ILE GLU
SEQRES 11 D 311 ASP CYS GLU ALA ALA THR ARG TRP VAL ALA SER SER PRO
SEQRES 12 D 311 SER GLU LEU GLY ARG THR ALA SER GLY VAL ILE PRO ILE
SEQRES 13 D 311 GLY ASP SER ALA GLY GLY ASN ALA THR ILE VAL VAL SER
SEQRES 14 D 311 GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL PRO VAL VAL
SEQRES 15 D 311 LEU GLN VAL PRO ILE PHE PRO LEU ALA SER ASP ALA VAL
SEQRES 16 D 311 GLY SER ALA SER LEU GLU ALA PHE ALA GLU GLY PHE VAL
SEQRES 17 D 311 LEU THR LYS ALA SER ILE GLU PHE PHE ASP THR ALA TYR
SEQRES 18 D 311 LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE PRO ILE LEU
SEQRES 19 D 311 GLY ASP HIS THR ALA ALA PRO PRO THR ILE VAL ALA THR
SEQRES 20 D 311 ALA SER LEU ASP PRO ILE ARG ASP SER GLY ARG ASP TYR
SEQRES 21 D 311 ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP VAL VAL TYR
SEQRES 22 D 311 LEU GLU MET GLU GLY VAL THR HIS SER PHE THR ASN ILE
SEQRES 23 D 311 ARG ALA ALA VAL PRO SER THR GLN GLY ASP LEU GLU ARG
SEQRES 24 D 311 ILE ILE ALA ALA MET LYS MET MET LEU GLY THR ALA
HET D8F A 401 17
HET SO4 A 402 5
HET EDO A 403 4
HET EDO A 404 4
HET GOL A 405 6
HET D8F B 401 17
HET SO4 B 402 5
HET SO4 B 403 5
HET SO4 B 404 5
HET EDO B 405 4
HET EDO B 406 4
HET EDO B 407 4
HET EDO B 408 4
HET EDO B 409 4
HET D8F C 401 17
HET EDO C 402 4
HET EDO C 403 4
HET EDO C 404 4
HET EDO C 405 4
HET 6NA C 406 8
HET D8F D 401 17
HET SO4 D 402 5
HET SO4 D 403 5
HET EDO D 404 4
HET EDO D 405 4
HET EDO D 406 4
HET EDO D 407 4
HET EDO D 408 4
HET EDO D 409 4
HET EDO D 410 4
HETNAM D8F (4-NITROPHENYL) HEXANOATE
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETNAM 6NA HEXANOIC ACID
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 D8F 4(C12 H15 N O4)
FORMUL 6 SO4 6(O4 S 2-)
FORMUL 7 EDO 18(C2 H6 O2)
FORMUL 9 GOL C3 H8 O3
FORMUL 24 6NA C6 H12 O2
FORMUL 35 HOH *1534(H2 O)
HELIX 1 AA1 ARG A 8 ALA A 22 1 15
HELIX 2 AA2 THR A 30 ASP A 46 1 17
HELIX 3 AA3 HIS A 100 ASP A 112 1 13
HELIX 4 AA4 PRO A 129 SER A 144 1 16
HELIX 5 AA5 SER A 162 LYS A 178 1 17
HELIX 6 AA6 SER A 200 PHE A 206 1 7
HELIX 7 AA7 THR A 213 LYS A 225 1 13
HELIX 8 AA8 PHE A 234 GLY A 238 5 5
HELIX 9 AA9 ILE A 256 ALA A 270 1 15
HELIX 10 AB1 SER A 285 ILE A 289 5 5
HELIX 11 AB2 SER A 295 GLY A 312 1 18
HELIX 12 AB3 ARG B 8 ALA B 22 1 15
HELIX 13 AB4 THR B 30 ASP B 46 1 17
HELIX 14 AB5 HIS B 100 ASP B 112 1 13
HELIX 15 AB6 PRO B 129 SER B 144 1 16
HELIX 16 AB7 SER B 145 GLY B 150 5 6
HELIX 17 AB8 SER B 162 LYS B 178 1 17
HELIX 18 AB9 SER B 200 PHE B 206 1 7
HELIX 19 AC1 THR B 213 LYS B 225 1 13
HELIX 20 AC2 PHE B 234 GLY B 238 5 5
HELIX 21 AC3 ILE B 256 ALA B 270 1 15
HELIX 22 AC4 SER B 285 ILE B 289 5 5
HELIX 23 AC5 PRO B 294 GLY B 312 1 19
HELIX 24 AC6 ARG C 8 ALA C 22 1 15
HELIX 25 AC7 THR C 25 MET C 29 5 5
HELIX 26 AC8 THR C 30 ASP C 46 1 17
HELIX 27 AC9 HIS C 100 ASP C 112 1 13
HELIX 28 AD1 PRO C 129 SER C 144 1 16
HELIX 29 AD2 SER C 162 LYS C 178 1 17
HELIX 30 AD3 SER C 200 PHE C 206 1 7
HELIX 31 AD4 THR C 213 LYS C 225 1 13
HELIX 32 AD5 PHE C 234 GLY C 238 5 5
HELIX 33 AD6 ILE C 256 ALA C 270 1 15
HELIX 34 AD7 SER C 285 ILE C 289 5 5
HELIX 35 AD8 SER C 295 GLY C 312 1 18
HELIX 36 AD9 ARG D 8 ALA D 22 1 15
HELIX 37 AE1 THR D 30 ASP D 46 1 17
HELIX 38 AE2 HIS D 100 ASP D 112 1 13
HELIX 39 AE3 PRO D 129 SER D 144 1 16
HELIX 40 AE4 SER D 145 GLY D 150 5 6
HELIX 41 AE5 SER D 162 LYS D 178 1 17
HELIX 42 AE6 SER D 200 PHE D 206 1 7
HELIX 43 AE7 THR D 213 LYS D 225 1 13
HELIX 44 AE8 PHE D 234 GLY D 238 5 5
HELIX 45 AE9 ILE D 256 ALA D 270 1 15
HELIX 46 AF1 SER D 285 ILE D 289 5 5
HELIX 47 AF2 SER D 295 GLY D 312 1 18
SHEET 1 AA1 6 VAL A 54 PRO A 61 0
SHEET 2 AA1 6 ASP A 66 ASP A 73 -1 O LEU A 71 N ARG A 56
SHEET 3 AA1 6 VAL A 115 VAL A 118 -1 O VAL A 115 N TYR A 72
SHEET 4 AA1 6 GLY A 81 TYR A 87 1 N ILE A 84 O VAL A 116
SHEET 5 AA1 6 ALA A 153 ASP A 161 1 O ILE A 157 N VAL A 83
SHEET 6 AA1 6 VAL A 188 ILE A 190 1 O ILE A 190 N GLY A 160
SHEET 1 AA2 4 THR A 246 ALA A 251 0
SHEET 2 AA2 4 VAL A 274 MET A 279 1 O VAL A 275 N VAL A 248
SHEET 3 AA2 4 VAL B 274 MET B 279 -1 O VAL B 274 N TYR A 276
SHEET 4 AA2 4 THR B 246 ALA B 251 1 N VAL B 248 O LEU B 277
SHEET 1 AA3 6 VAL B 54 CYS B 60 0
SHEET 2 AA3 6 ILE B 67 ASP B 73 -1 O ILE B 67 N CYS B 60
SHEET 3 AA3 6 VAL B 115 VAL B 118 -1 O VAL B 115 N TYR B 72
SHEET 4 AA3 6 GLY B 81 TYR B 87 1 N ILE B 84 O VAL B 116
SHEET 5 AA3 6 ALA B 153 ASP B 161 1 O ILE B 157 N VAL B 83
SHEET 6 AA3 6 VAL B 188 ILE B 190 1 O ILE B 190 N GLY B 160
SHEET 1 AA4 6 VAL C 54 GLY C 62 0
SHEET 2 AA4 6 GLY C 65 ASP C 73 -1 O ILE C 67 N CYS C 60
SHEET 3 AA4 6 VAL C 115 VAL C 118 -1 O VAL C 115 N TYR C 72
SHEET 4 AA4 6 GLY C 81 TYR C 87 1 N ILE C 84 O VAL C 116
SHEET 5 AA4 6 ALA C 153 ASP C 161 1 O ILE C 157 N VAL C 83
SHEET 6 AA4 6 VAL C 188 ILE C 190 1 O ILE C 190 N GLY C 160
SHEET 1 AA5 4 THR C 246 ALA C 251 0
SHEET 2 AA5 4 VAL C 274 MET C 279 1 O MET C 279 N THR C 250
SHEET 3 AA5 4 VAL D 274 MET D 279 -1 O TYR D 276 N VAL C 274
SHEET 4 AA5 4 THR D 246 ALA D 251 1 N VAL D 248 O VAL D 275
SHEET 1 AA6 6 VAL D 54 GLY D 62 0
SHEET 2 AA6 6 GLY D 65 ASP D 73 -1 O ILE D 67 N CYS D 60
SHEET 3 AA6 6 VAL D 115 VAL D 118 -1 O VAL D 115 N TYR D 72
SHEET 4 AA6 6 GLY D 81 TYR D 87 1 N ILE D 84 O VAL D 116
SHEET 5 AA6 6 ALA D 153 ASP D 161 1 O ILE D 157 N VAL D 83
SHEET 6 AA6 6 VAL D 188 ILE D 190 1 O ILE D 190 N GLY D 160
CISPEP 1 ALA A 123 PRO A 124 0 -1.08
CISPEP 2 PHE A 128 PRO A 129 0 3.46
CISPEP 3 ALA B 123 PRO B 124 0 0.78
CISPEP 4 PHE B 128 PRO B 129 0 5.87
CISPEP 5 ALA C 123 PRO C 124 0 -0.34
CISPEP 6 PHE C 128 PRO C 129 0 2.78
CISPEP 7 ALA D 123 PRO D 124 0 0.38
CISPEP 8 PHE D 128 PRO D 129 0 7.21
SITE 1 AC1 10 TYR A 38 GLY A 90 GLY A 91 SER A 162
SITE 2 AC1 10 ALA A 163 LEU A 212 HIS A 284 SER A 285
SITE 3 AC1 10 HOH A 713 HOH A 760
SITE 1 AC2 3 ARG A 75 GLU A 76 SER A 77
SITE 1 AC3 7 ARG A 140 PRO A 179 ALA A 180 HOH A 540
SITE 2 AC3 7 HOH A 541 HOH A 632 HOH A 718
SITE 1 AC4 5 ARG A 257 ARG A 261 HOH A 502 HOH A 693
SITE 2 AC4 5 HOH B 592
SITE 1 AC5 7 ASP A 96 ASP A 119 TYR A 120 LEU A 122
SITE 2 AC5 7 HOH A 536 HOH A 567 HOH A 578
SITE 1 AC6 11 TYR B 38 GLY B 90 GLY B 91 SER B 162
SITE 2 AC6 11 ALA B 163 LEU B 193 LEU B 212 PHE B 220
SITE 3 AC6 11 HIS B 284 SER B 285 HOH B 563
SITE 1 AC7 2 ARG B 50 GLU B 51
SITE 1 AC8 3 GLU A 280 ARG B 272 HOH B 632
SITE 1 AC9 1 ARG B 75
SITE 1 AD1 5 ARG B 75 GLU B 76 SER B 77 HOH B 575
SITE 2 AD1 5 HOH B 672
SITE 1 AD2 7 ARG B 8 SER B 295 GLY B 298 ASP B 299
SITE 2 AD2 7 HOH B 513 HOH B 665 HOH B 745
SITE 1 AD3 2 THR B 30 GLU B 32
SITE 1 AD4 2 LYS B 12 GLU B 16
SITE 1 AD5 3 GLY B 23 THR B 25 HOH B 532
SITE 1 AD6 11 TYR C 38 GLY C 90 GLY C 91 SER C 162
SITE 2 AD6 11 ALA C 163 LEU C 193 LEU C 212 PHE C 220
SITE 3 AD6 11 HIS C 284 SER C 285 HOH C 684
SITE 1 AD7 5 ARG C 140 PRO C 179 ALA C 180 HOH C 573
SITE 2 AD7 5 HOH C 681
SITE 1 AD8 3 GLU C 79 ALA C 80 THR C 152
SITE 1 AD9 1 ARG C 50
SITE 1 AE1 5 ARG C 302 HOH C 597 HOH C 742 MET D 309
SITE 2 AE1 5 MET D 310
SITE 1 AE2 3 ARG C 257 ARG C 261 HOH D 549
SITE 1 AE3 11 TYR D 38 GLY D 90 GLY D 91 SER D 162
SITE 2 AE3 11 ALA D 163 LEU D 212 PHE D 220 HIS D 284
SITE 3 AE3 11 SER D 285 HOH D 610 HOH D 703
SITE 1 AE4 4 THR D 30 LEU D 31 EDO D 410 HOH D 628
SITE 1 AE5 1 ARG D 75
SITE 1 AE6 4 ARG D 140 ALA D 180 HOH D 621 HOH D 674
SITE 1 AE7 3 ARG D 75 GLU D 76 SER D 77
SITE 1 AE8 4 ARG D 257 ARG D 261 HOH D 531 HOH D 711
SITE 1 AE9 4 PRO D 146 SER D 147 HOH D 562 HOH D 691
SITE 1 AF1 7 ASP D 98 HIS D 101 ASN D 102 HOH D 510
SITE 2 AF1 7 HOH D 586 HOH D 676 HOH D 727
SITE 1 AF2 4 ILE D 55 ASN D 57 ARG D 70 HIS D 101
SITE 1 AF3 6 LEU D 26 MET D 29 THR D 30 LEU D 31
SITE 2 AF3 6 PHE D 219 SO4 D 402
CRYST1 70.605 129.888 221.239 90.00 90.00 90.00 P 21 2 21 16
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 0.014163 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007699 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004520 0.00000
TER 2282 GLY A 312
TER 4572 GLY B 312
TER 6854 GLY C 312
TER 9144 GLY D 312
MASTER 478 0 30 47 32 0 47 610858 4 184 96
END
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