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HEADER HYDROLASE 06-JUL-19 6KF7
TITLE MICROBIAL HORMONE-SENSITIVE LIPASE E53 MUTANT S285G
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ERYTHROBACTER LONGUS;
SOURCE 3 ORGANISM_TAXID: 1044;
SOURCE 4 GENE: EH31_02760;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS ESTERASE, MICROBIAL HORMONE-SENSITIVE LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.XIAOCHEN,L.ZHENGYANG,X.XUEWEI,L.JIXI
REVDAT 1 08-JUL-20 6KF7 0
JRNL AUTH Y.XIAOCHEN
JRNL TITL MICROBIAL HORMONE-SENSITIVE LIPASE E53 MUTANT S285G
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.53
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 186898
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 9409
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 48.5300 - 5.5800 0.99 6329 315 0.1722 0.1777
REMARK 3 2 5.5800 - 4.4300 1.00 6122 284 0.1454 0.1570
REMARK 3 3 4.4300 - 3.8700 1.00 6045 342 0.1341 0.1456
REMARK 3 4 3.8700 - 3.5200 1.00 5991 325 0.1444 0.1627
REMARK 3 5 3.5200 - 3.2700 1.00 6012 301 0.1519 0.1751
REMARK 3 6 3.2700 - 3.0700 1.00 5936 315 0.1574 0.1875
REMARK 3 7 3.0700 - 2.9200 1.00 5994 321 0.1669 0.1861
REMARK 3 8 2.9200 - 2.7900 1.00 5946 328 0.1673 0.2008
REMARK 3 9 2.7900 - 2.6900 1.00 5929 323 0.1664 0.2047
REMARK 3 10 2.6900 - 2.5900 1.00 5878 337 0.1691 0.1960
REMARK 3 11 2.5900 - 2.5100 1.00 5906 355 0.1729 0.2036
REMARK 3 12 2.5100 - 2.4400 1.00 5941 294 0.1753 0.2137
REMARK 3 13 2.4400 - 2.3800 1.00 5935 298 0.1755 0.1964
REMARK 3 14 2.3800 - 2.3200 1.00 5910 305 0.1775 0.2029
REMARK 3 15 2.3200 - 2.2700 1.00 5921 310 0.1726 0.2003
REMARK 3 16 2.2700 - 2.2200 1.00 5866 335 0.1747 0.2030
REMARK 3 17 2.2200 - 2.1700 1.00 5902 325 0.1809 0.2119
REMARK 3 18 2.1700 - 2.1300 1.00 5857 321 0.1826 0.2065
REMARK 3 19 2.1300 - 2.0900 1.00 5904 302 0.1918 0.2338
REMARK 3 20 2.0900 - 2.0600 1.00 5843 333 0.1896 0.2175
REMARK 3 21 2.0600 - 2.0200 1.00 5873 287 0.1873 0.2167
REMARK 3 22 2.0200 - 1.9900 1.00 5874 308 0.1908 0.2188
REMARK 3 23 1.9900 - 1.9600 1.00 5859 310 0.2045 0.2423
REMARK 3 24 1.9600 - 1.9400 0.99 5869 315 0.2136 0.2531
REMARK 3 25 1.9400 - 1.9100 1.00 5855 293 0.2256 0.2405
REMARK 3 26 1.9100 - 1.8900 0.99 5905 289 0.2208 0.2482
REMARK 3 27 1.8900 - 1.8600 1.00 5798 322 0.2229 0.2328
REMARK 3 28 1.8600 - 1.8400 0.99 5880 313 0.2358 0.2603
REMARK 3 29 1.8400 - 1.8200 1.00 5826 306 0.2489 0.2707
REMARK 3 30 1.8200 - 1.8000 0.95 5583 297 0.2669 0.2817
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.175
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.941
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.48
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.49
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 9545
REMARK 3 ANGLE : 0.833 12956
REMARK 3 CHIRALITY : 0.052 1471
REMARK 3 PLANARITY : 0.006 1708
REMARK 3 DIHEDRAL : 8.309 5709
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 6KF7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JUL-19.
REMARK 100 THE DEPOSITION ID IS D_1300012868.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAY-17
REMARK 200 TEMPERATURE (KELVIN) : 80
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 : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97916
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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 186934
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 48.530
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.11900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.7560
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) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.54800
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: PHASER
REMARK 200 STARTING MODEL: 4YPV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CALCIUM CHLORIDE, BIS-TRIS, PEG MME
REMARK 280 550, PH 6.5, 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 35.32850
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 109.73200
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.32850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 109.73200
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 B 782 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 794 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 MET A 1
REMARK 465 THR A 2
REMARK 465 ASP A 3
REMARK 465 THR A 313
REMARK 465 ALA A 314
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ASP B 3
REMARK 465 THR B 313
REMARK 465 ALA B 314
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 ASP C 3
REMARK 465 THR C 313
REMARK 465 ALA C 314
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 ASP D 3
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 51 CG CD OE1 OE2
REMARK 470 GLU A 76 CG CD OE1 OE2
REMARK 470 GLU A 79 CG CD OE1 OE2
REMARK 470 LYS A 178 CG CD CE NZ
REMARK 470 THR B 4 OG1 CG2
REMARK 470 LYS B 178 CG CD CE NZ
REMARK 470 PRO B 294 CB CG
REMARK 470 THR C 4 OG1 CG2
REMARK 470 GLU C 79 CG CD OE1 OE2
REMARK 470 LYS C 178 CG CD CE NZ
REMARK 470 THR D 4 OG1 CG2
REMARK 470 LYS D 178 CG CD CE NZ
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 162 CAL D8F A 401 1.78
REMARK 500 OG SER C 162 CAL D8F C 401 1.85
REMARK 500 OG SER B 162 CAL D8F B 401 1.86
REMARK 500 OG SER D 162 CAL D8F D 401 1.92
REMARK 500 OG SER B 162 CAQ D8F B 401 1.96
REMARK 500 O1 EDO B 402 O HOH B 501 2.00
REMARK 500 OG SER C 162 CAQ D8F C 401 2.01
REMARK 500 OAB D8F A 401 O HOH A 501 2.05
REMARK 500 OG SER D 162 CAQ D8F D 401 2.05
REMARK 500 OG SER A 162 CAQ D8F A 401 2.05
REMARK 500 O HOH B 669 O HOH B 788 2.06
REMARK 500 O HOH C 746 O HOH C 864 2.06
REMARK 500 O HOH D 635 O HOH D 736 2.10
REMARK 500 O HOH B 718 O HOH B 774 2.10
REMARK 500 O HOH C 608 O HOH C 746 2.13
REMARK 500 O HOH A 780 O HOH A 785 2.14
REMARK 500 O HOH A 503 O HOH A 580 2.17
REMARK 500 O HOH D 651 O HOH D 756 2.17
REMARK 500 O HOH A 758 O HOH B 649 2.17
REMARK 500 O HOH D 756 O HOH D 795 2.18
REMARK 500 O HOH C 679 O HOH C 824 2.18
REMARK 500 O HOH A 581 O HOH A 782 2.18
REMARK 500 O HOH B 722 O HOH B 816 2.18
REMARK 500 O HOH D 756 O HOH D 779 2.18
REMARK 500 O HOH C 738 O HOH C 815 2.19
REMARK 500 O HOH A 655 O HOH B 579 2.19
REMARK 500 O HOH D 687 O HOH D 739 2.19
REMARK 500 O HOH A 783 O HOH A 820 2.19
REMARK 500 O HOH C 578 O HOH C 781 2.19
REMARK 500 O HOH A 543 O HOH A 809 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 D 501 O HOH D 501 2754 1.78
REMARK 500 O HOH D 716 O HOH D 716 2754 1.79
REMARK 500 O HOH B 753 O HOH B 753 2555 2.04
REMARK 500 O HOH B 742 O HOH B 753 2555 2.07
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 -160.64 -164.49
REMARK 500 PRO A 129 33.65 -99.69
REMARK 500 SER A 162 -119.05 65.06
REMARK 500 PHE A 191 64.69 24.62
REMARK 500 VAL A 211 -71.61 73.95
REMARK 500 ASP B 96 -159.44 -165.09
REMARK 500 SER B 162 -119.55 62.09
REMARK 500 LEU B 186 141.06 -171.76
REMARK 500 PHE B 191 65.95 22.58
REMARK 500 VAL B 211 -69.64 68.10
REMARK 500 ALA C 22 -132.24 55.86
REMARK 500 ASP C 96 -161.14 -163.53
REMARK 500 SER C 162 -119.38 64.92
REMARK 500 LEU C 186 139.25 -173.20
REMARK 500 PHE C 191 63.58 23.89
REMARK 500 VAL C 211 -71.24 71.21
REMARK 500 ASP D 96 -160.10 -164.72
REMARK 500 SER D 162 -118.64 61.69
REMARK 500 PHE D 191 64.84 22.44
REMARK 500 VAL D 211 -68.29 67.01
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 867 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH A 868 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH C 887 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH C 888 DISTANCE = 5.92 ANGSTROMS
REMARK 525 HOH C 889 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH C 890 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH D 828 DISTANCE = 6.35 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 EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6NA A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6NA C 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE C 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO D 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide D8F B 401 and SER B
REMARK 800 162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide D8F C 401 and SER C
REMARK 800 162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide D8F D 401 and SER D
REMARK 800 162
DBREF1 6KF7 A 1 314 UNP A0A074MDU6_ERYLO
DBREF2 6KF7 A A0A074MDU6 1 314
DBREF1 6KF7 B 1 314 UNP A0A074MDU6_ERYLO
DBREF2 6KF7 B A0A074MDU6 1 314
DBREF1 6KF7 C 1 314 UNP A0A074MDU6_ERYLO
DBREF2 6KF7 C A0A074MDU6 1 314
DBREF1 6KF7 D 1 314 UNP A0A074MDU6_ERYLO
DBREF2 6KF7 D A0A074MDU6 1 314
SEQADV 6KF7 GLY A 285 UNP A0A074MDU SER 285 ENGINEERED MUTATION
SEQADV 6KF7 GLY B 285 UNP A0A074MDU SER 285 ENGINEERED MUTATION
SEQADV 6KF7 GLY C 285 UNP A0A074MDU SER 285 ENGINEERED MUTATION
SEQADV 6KF7 GLY D 285 UNP A0A074MDU SER 285 ENGINEERED MUTATION
SEQRES 1 A 314 MET THR ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA
SEQRES 2 A 314 PHE LEU GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU
SEQRES 3 A 314 ALA GLU MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL
SEQRES 4 A 314 ALA LEU HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU
SEQRES 5 A 314 ALA VAL ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY
SEQRES 6 A 314 ASP ILE PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG
SEQRES 7 A 314 GLU ALA GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY
SEQRES 8 A 314 PHE VAL ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS
SEQRES 9 A 314 THR GLU ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA
SEQRES 10 A 314 VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA
SEQRES 11 A 314 ALA ILE GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA
SEQRES 12 A 314 SER SER PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL
SEQRES 13 A 314 ILE PRO ILE GLY ASP SER ALA GLY GLY ASN ALA THR ILE
SEQRES 14 A 314 VAL VAL SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL
SEQRES 15 A 314 PRO VAL VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER
SEQRES 16 A 314 ASP ALA VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU
SEQRES 17 A 314 GLY PHE VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP
SEQRES 18 A 314 THR ALA TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE
SEQRES 19 A 314 PRO ILE LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE
SEQRES 20 A 314 VAL ALA THR ALA SER LEU ASP PRO ILE ARG ASP SER GLY
SEQRES 21 A 314 ARG ASP TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP
SEQRES 22 A 314 VAL VAL TYR LEU GLU MET GLU GLY VAL THR HIS GLY PHE
SEQRES 23 A 314 THR ASN ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP
SEQRES 24 A 314 LEU GLU ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY
SEQRES 25 A 314 THR ALA
SEQRES 1 B 314 MET THR ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA
SEQRES 2 B 314 PHE LEU GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU
SEQRES 3 B 314 ALA GLU MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL
SEQRES 4 B 314 ALA LEU HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU
SEQRES 5 B 314 ALA VAL ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY
SEQRES 6 B 314 ASP ILE PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG
SEQRES 7 B 314 GLU ALA GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY
SEQRES 8 B 314 PHE VAL ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS
SEQRES 9 B 314 THR GLU ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA
SEQRES 10 B 314 VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA
SEQRES 11 B 314 ALA ILE GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA
SEQRES 12 B 314 SER SER PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL
SEQRES 13 B 314 ILE PRO ILE GLY ASP SER ALA GLY GLY ASN ALA THR ILE
SEQRES 14 B 314 VAL VAL SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL
SEQRES 15 B 314 PRO VAL VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER
SEQRES 16 B 314 ASP ALA VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU
SEQRES 17 B 314 GLY PHE VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP
SEQRES 18 B 314 THR ALA TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE
SEQRES 19 B 314 PRO ILE LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE
SEQRES 20 B 314 VAL ALA THR ALA SER LEU ASP PRO ILE ARG ASP SER GLY
SEQRES 21 B 314 ARG ASP TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP
SEQRES 22 B 314 VAL VAL TYR LEU GLU MET GLU GLY VAL THR HIS GLY PHE
SEQRES 23 B 314 THR ASN ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP
SEQRES 24 B 314 LEU GLU ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY
SEQRES 25 B 314 THR ALA
SEQRES 1 C 314 MET THR ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA
SEQRES 2 C 314 PHE LEU GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU
SEQRES 3 C 314 ALA GLU MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL
SEQRES 4 C 314 ALA LEU HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU
SEQRES 5 C 314 ALA VAL ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY
SEQRES 6 C 314 ASP ILE PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG
SEQRES 7 C 314 GLU ALA GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY
SEQRES 8 C 314 PHE VAL ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS
SEQRES 9 C 314 THR GLU ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA
SEQRES 10 C 314 VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA
SEQRES 11 C 314 ALA ILE GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA
SEQRES 12 C 314 SER SER PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL
SEQRES 13 C 314 ILE PRO ILE GLY ASP SER ALA GLY GLY ASN ALA THR ILE
SEQRES 14 C 314 VAL VAL SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL
SEQRES 15 C 314 PRO VAL VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER
SEQRES 16 C 314 ASP ALA VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU
SEQRES 17 C 314 GLY PHE VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP
SEQRES 18 C 314 THR ALA TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE
SEQRES 19 C 314 PRO ILE LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE
SEQRES 20 C 314 VAL ALA THR ALA SER LEU ASP PRO ILE ARG ASP SER GLY
SEQRES 21 C 314 ARG ASP TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP
SEQRES 22 C 314 VAL VAL TYR LEU GLU MET GLU GLY VAL THR HIS GLY PHE
SEQRES 23 C 314 THR ASN ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP
SEQRES 24 C 314 LEU GLU ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY
SEQRES 25 C 314 THR ALA
SEQRES 1 D 314 MET THR ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA
SEQRES 2 D 314 PHE LEU GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU
SEQRES 3 D 314 ALA GLU MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL
SEQRES 4 D 314 ALA LEU HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU
SEQRES 5 D 314 ALA VAL ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY
SEQRES 6 D 314 ASP ILE PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG
SEQRES 7 D 314 GLU ALA GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY
SEQRES 8 D 314 PHE VAL ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS
SEQRES 9 D 314 THR GLU ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA
SEQRES 10 D 314 VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA
SEQRES 11 D 314 ALA ILE GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA
SEQRES 12 D 314 SER SER PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL
SEQRES 13 D 314 ILE PRO ILE GLY ASP SER ALA GLY GLY ASN ALA THR ILE
SEQRES 14 D 314 VAL VAL SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL
SEQRES 15 D 314 PRO VAL VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER
SEQRES 16 D 314 ASP ALA VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU
SEQRES 17 D 314 GLY PHE VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP
SEQRES 18 D 314 THR ALA TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE
SEQRES 19 D 314 PRO ILE LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE
SEQRES 20 D 314 VAL ALA THR ALA SER LEU ASP PRO ILE ARG ASP SER GLY
SEQRES 21 D 314 ARG ASP TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP
SEQRES 22 D 314 VAL VAL TYR LEU GLU MET GLU GLY VAL THR HIS GLY PHE
SEQRES 23 D 314 THR ASN ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP
SEQRES 24 D 314 LEU GLU ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY
SEQRES 25 D 314 THR ALA
HET D8F A 401 17
HET SO4 A 402 5
HET EDO A 403 4
HET EDO A 404 4
HET EDO A 405 4
HET EDO A 406 4
HET EDO A 407 4
HET GOL A 408 6
HET GOL A 409 6
HET GOL A 410 6
HET GOL A 411 6
HET GOL A 412 6
HET 6NA A 413 8
HET D8F B 401 17
HET EDO B 402 4
HET EDO B 403 4
HET GOL B 404 6
HET GOL B 405 6
HET GOL B 406 6
HET D8F C 401 17
HET EDO C 402 4
HET EDO C 403 4
HET EDO C 404 4
HET GOL C 405 6
HET GOL C 406 6
HET GOL C 407 6
HET GOL C 408 6
HET 6NA C 409 8
HET PGE C 410 10
HET D8F D 401 17
HET SO4 D 402 5
HET EDO D 403 4
HET EDO D 404 4
HET EDO D 405 4
HET GOL D 406 6
HET GOL D 407 6
HET GOL D 408 6
HET GOL D 409 6
HET NPO D 410 10
HETNAM D8F (4-NITROPHENYL) HEXANOATE
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETNAM 6NA HEXANOIC ACID
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM NPO P-NITROPHENOL
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 D8F 4(C12 H15 N O4)
FORMUL 6 SO4 2(O4 S 2-)
FORMUL 7 EDO 13(C2 H6 O2)
FORMUL 12 GOL 16(C3 H8 O3)
FORMUL 17 6NA 2(C6 H12 O2)
FORMUL 33 PGE C6 H14 O4
FORMUL 43 NPO C6 H5 N O3
FORMUL 44 HOH *1409(H2 O)
HELIX 1 AA1 ARG A 8 ALA A 22 1 15
HELIX 2 AA2 THR A 25 MET A 29 5 5
HELIX 3 AA3 THR A 30 ASP A 46 1 17
HELIX 4 AA4 HIS A 100 ASP A 112 1 13
HELIX 5 AA5 PRO A 129 SER A 144 1 16
HELIX 6 AA6 SER A 145 GLY A 150 5 6
HELIX 7 AA7 SER A 162 LYS A 178 1 17
HELIX 8 AA8 SER A 200 PHE A 206 1 7
HELIX 9 AA9 THR A 213 LYS A 225 1 13
HELIX 10 AB1 PHE A 234 GLY A 238 5 5
HELIX 11 AB2 ILE A 256 ALA A 270 1 15
HELIX 12 AB3 GLY A 285 ILE A 289 5 5
HELIX 13 AB4 PRO A 294 GLY A 312 1 19
HELIX 14 AB5 ARG B 8 ALA B 22 1 15
HELIX 15 AB6 THR B 30 ASP B 46 1 17
HELIX 16 AB7 HIS B 100 ASP B 112 1 13
HELIX 17 AB8 PRO B 129 SER B 144 1 16
HELIX 18 AB9 SER B 145 GLY B 150 5 6
HELIX 19 AC1 SER B 162 LYS B 178 1 17
HELIX 20 AC2 SER B 200 PHE B 206 1 7
HELIX 21 AC3 THR B 213 LYS B 225 1 13
HELIX 22 AC4 PHE B 234 GLY B 238 5 5
HELIX 23 AC5 ILE B 256 ALA B 270 1 15
HELIX 24 AC6 GLY B 285 ILE B 289 5 5
HELIX 25 AC7 SER B 295 GLY B 312 1 18
HELIX 26 AC8 ARG C 8 ALA C 22 1 15
HELIX 27 AC9 THR C 30 ASP C 46 1 17
HELIX 28 AD1 HIS C 100 ASP C 112 1 13
HELIX 29 AD2 PRO C 129 SER C 144 1 16
HELIX 30 AD3 SER C 145 GLY C 150 5 6
HELIX 31 AD4 SER C 162 LYS C 178 1 17
HELIX 32 AD5 SER C 200 PHE C 206 1 7
HELIX 33 AD6 THR C 213 LYS C 225 1 13
HELIX 34 AD7 PHE C 234 GLY C 238 5 5
HELIX 35 AD8 ILE C 256 ALA C 270 1 15
HELIX 36 AD9 GLY C 285 ILE C 289 5 5
HELIX 37 AE1 SER C 295 GLY C 312 1 18
HELIX 38 AE2 ARG D 8 ALA D 22 1 15
HELIX 39 AE3 THR D 25 MET D 29 5 5
HELIX 40 AE4 THR D 30 ASP D 46 1 17
HELIX 41 AE5 HIS D 100 ASP D 112 1 13
HELIX 42 AE6 PRO D 129 SER D 144 1 16
HELIX 43 AE7 SER D 145 GLY D 150 5 6
HELIX 44 AE8 SER D 162 LYS D 178 1 17
HELIX 45 AE9 SER D 200 PHE D 206 1 7
HELIX 46 AF1 THR D 213 LYS D 225 1 13
HELIX 47 AF2 PHE D 234 GLY D 238 5 5
HELIX 48 AF3 ILE D 256 ALA D 270 1 15
HELIX 49 AF4 GLY D 285 ILE D 289 5 5
HELIX 50 AF5 PRO D 294 GLY D 312 1 19
SHEET 1 AA1 6 VAL A 54 CYS A 60 0
SHEET 2 AA1 6 ILE A 67 ASP A 73 -1 O LEU A 69 N LEU A 58
SHEET 3 AA1 6 VAL A 115 VAL A 118 -1 O ALA A 117 N ARG A 70
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 THR A 85
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 MET A 279 N THR A 250
SHEET 3 AA2 4 VAL B 274 MET B 279 -1 O TYR B 276 N VAL A 274
SHEET 4 AA2 4 THR B 246 ALA B 251 1 N VAL B 248 O VAL B 275
SHEET 1 AA3 6 VAL B 54 CYS B 60 0
SHEET 2 AA3 6 ILE B 67 ASP B 73 -1 O LEU B 71 N ARG B 56
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 CYS C 60 0
SHEET 2 AA4 6 ILE C 67 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 VAL C 275 N VAL C 248
SHEET 3 AA5 4 VAL D 274 MET D 279 -1 O VAL D 274 N TYR C 276
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 CYS D 60 0
SHEET 2 AA6 6 ILE D 67 ASP D 73 -1 O LEU D 71 N ARG D 56
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 THR D 85
SHEET 6 AA6 6 VAL D 188 ILE D 190 1 O ILE D 190 N GLY D 160
LINK OG SER A 162 CAN D8F A 401 1555 1555 1.39
LINK OG SER B 162 CAN D8F B 401 1555 1555 1.38
LINK OG SER C 162 CAN D8F C 401 1555 1555 1.39
LINK OG SER D 162 CAN D8F D 401 1555 1555 1.38
CISPEP 1 ALA A 123 PRO A 124 0 1.77
CISPEP 2 PHE A 128 PRO A 129 0 0.67
CISPEP 3 ALA B 123 PRO B 124 0 1.54
CISPEP 4 PHE B 128 PRO B 129 0 6.12
CISPEP 5 ALA C 123 PRO C 124 0 0.23
CISPEP 6 PHE C 128 PRO C 129 0 4.37
CISPEP 7 ALA D 123 PRO D 124 0 1.50
CISPEP 8 PHE D 128 PRO D 129 0 5.78
SITE 1 AC1 12 TYR A 38 GLY A 90 GLY A 91 SER A 162
SITE 2 AC1 12 ALA A 163 LEU A 193 LEU A 212 PHE A 220
SITE 3 AC1 12 HIS A 284 HOH A 501 HOH A 519 HOH A 538
SITE 1 AC2 4 PRO A 24 HOH A 538 HOH A 548 HOH A 573
SITE 1 AC3 2 PRO A 9 ASP A 10
SITE 1 AC4 3 GLU A 51 LEU A 52 HOH A 517
SITE 1 AC5 4 ARG A 302 HOH A 539 HOH A 734 MET B 309
SITE 1 AC6 3 LYS A 265 HOH A 574 GLU B 269
SITE 1 AC7 2 ASP A 112 HOH A 612
SITE 1 AC8 9 LEU A 193 ASP A 196 ALA A 197 VAL A 198
SITE 2 AC8 9 ASP A 221 ARG A 228 HOH A 502 HOH A 519
SITE 3 AC8 9 HOH A 561
SITE 1 AC9 7 ARG A 257 ARG A 261 GOL A 410 HOH A 564
SITE 2 AC9 7 HOH A 681 HOH B 513 HOH B 562
SITE 1 AD1 2 ARG A 257 GOL A 409
SITE 1 AD2 6 ARG A 140 PRO A 179 ALA A 180 ASP A 181
SITE 2 AD2 6 HOH A 552 HOH A 713
SITE 1 AD3 5 PRO A 124 THR A 222 ALA A 223 HOH A 513
SITE 2 AD3 5 HOH A 607
SITE 1 AD4 10 ASP A 96 ASP A 119 TYR A 120 ARG A 121
SITE 2 AD4 10 HOH A 525 HOH A 534 HOH A 547 HOH A 554
SITE 3 AD4 10 HOH A 679 HOH A 703
SITE 1 AD5 4 GLU B 79 ALA B 80 HOH B 501 HOH B 526
SITE 1 AD6 4 ARG B 8 PRO B 9 ASP B 10 HOH B 614
SITE 1 AD7 4 ALA B 201 ALA B 205 ARG B 257 GOL B 405
SITE 1 AD8 5 HOH A 532 ARG B 257 ARG B 261 GOL B 404
SITE 2 AD8 5 HOH B 519
SITE 1 AD9 8 ASP B 196 ALA B 197 VAL B 198 ILE B 217
SITE 2 AD9 8 ASP B 221 ARG B 228 HOH B 645 HOH B 662
SITE 1 AE1 4 ALA C 64 GLY C 65 ASP C 66 HOH C 624
SITE 1 AE2 3 ARG C 228 HOH C 683 HOH C 790
SITE 1 AE3 4 MET C 309 GLY C 312 HOH C 501 ALA D 305
SITE 1 AE4 10 LEU C 193 ASP C 196 ALA C 197 VAL C 198
SITE 2 AE4 10 ILE C 217 ASP C 221 ARG C 228 HOH C 511
SITE 3 AE4 10 HOH C 573 HOH C 632
SITE 1 AE5 5 ARG C 257 ARG C 261 GOL C 407 HOH C 503
SITE 2 AE5 5 HOH D 582
SITE 1 AE6 2 ARG C 257 GOL C 406
SITE 1 AE7 3 ARG C 75 GLU C 76 SER C 77
SITE 1 AE8 8 ASP C 96 ASP C 119 TYR C 120 ARG C 121
SITE 2 AE8 8 LEU C 122 HOH C 543 HOH C 578 HOH C 838
SITE 1 AE9 7 LYS C 265 ALA C 266 HOH C 597 HOH C 619
SITE 2 AE9 7 HOH C 708 LYS D 265 ALA D 266
SITE 1 AF1 1 ARG D 75
SITE 1 AF2 4 ARG D 8 PRO D 9 ASP D 10 SER D 295
SITE 1 AF3 4 LEU D 122 HIS D 126 EDO D 405 HOH D 703
SITE 1 AF4 5 ASP D 119 TYR D 120 EDO D 404 HOH D 503
SITE 2 AF4 5 HOH D 624
SITE 1 AF5 9 LEU D 193 ASP D 196 ALA D 197 VAL D 198
SITE 2 AF5 9 ILE D 217 ASP D 221 ARG D 228 HOH D 584
SITE 3 AF5 9 HOH D 592
SITE 1 AF6 7 HOH C 544 HOH C 588 ARG D 257 ARG D 261
SITE 2 AF6 7 GOL D 408 HOH D 508 HOH D 654
SITE 1 AF7 4 ALA D 201 ALA D 205 ARG D 257 GOL D 407
SITE 1 AF8 4 ALA D 74 ASP D 112 HOH D 553 HOH D 631
SITE 1 AF9 6 LYS D 12 LEU D 15 GLU D 16 GLY D 209
SITE 2 AF9 6 PHE D 210 HOH D 782
SITE 1 AG1 13 GLY B 90 GLY B 91 ASP B 161 ALA B 163
SITE 2 AG1 13 GLY B 164 GLY B 165 ASN B 166 ILE B 190
SITE 3 AG1 13 PHE B 191 PRO B 192 LEU B 212 HIS B 284
SITE 4 AG1 13 HOH B 645
SITE 1 AG2 15 TYR C 38 GLY C 90 GLY C 91 ASP C 161
SITE 2 AG2 15 ALA C 163 GLY C 164 GLY C 165 ASN C 166
SITE 3 AG2 15 ILE C 190 PHE C 191 PRO C 192 LEU C 212
SITE 4 AG2 15 PHE C 220 HIS C 284 HOH C 748
SITE 1 AG3 15 TYR D 38 GLY D 89 GLY D 90 GLY D 91
SITE 2 AG3 15 ASP D 161 ALA D 163 GLY D 164 GLY D 165
SITE 3 AG3 15 ASN D 166 ILE D 190 PHE D 191 LEU D 193
SITE 4 AG3 15 LEU D 212 HIS D 284 HOH D 584
CRYST1 70.657 129.715 219.464 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 0.014153 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007709 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004557 0.00000
TER 2272 GLY A 312
TER 4554 GLY B 312
TER 6834 GLY C 312
TER 9118 GLY D 312
MASTER 569 0 39 50 32 0 69 610785 4 266 100
END |