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HEADER HYDROLASE 06-JUL-19 6KF5
TITLE MICROBIAL HORMONE-SENSITIVE LIPASE E53 MUTANT I256L
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 X.YANG,Z.Y.LI,J.LI,X.W.XU
REVDAT 1 08-JUL-20 6KF5 0
JRNL AUTH X.YANG,H.YINGYI,Z.Y.LI,J.SHULING,R.ZHEN,W.ZHAO,H.XIAOJIAN,
JRNL AUTH 2 C.HENGLIN,J.LI,X.W.XU
JRNL TITL MICROBIAL HORMONE-SENSITIVE LIPASE E53 MUTANT I256L
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.09 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) : 2.09
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.50
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 119096
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930
REMARK 3 FREE R VALUE TEST SET COUNT : 5874
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 19.5000 - 6.4300 0.95 3857 203 0.2128 0.2150
REMARK 3 2 6.4300 - 5.1300 0.99 3927 179 0.2038 0.2344
REMARK 3 3 5.1300 - 4.4900 1.00 3854 192 0.1611 0.1798
REMARK 3 4 4.4900 - 4.0900 1.00 3845 192 0.1539 0.1742
REMARK 3 5 4.0900 - 3.8000 1.00 3824 197 0.1592 0.2057
REMARK 3 6 3.8000 - 3.5700 1.00 3798 210 0.1747 0.2002
REMARK 3 7 3.5700 - 3.4000 1.00 3772 203 0.1715 0.2160
REMARK 3 8 3.4000 - 3.2500 1.00 3803 209 0.1814 0.1815
REMARK 3 9 3.2500 - 3.1200 1.00 3831 177 0.1809 0.2283
REMARK 3 10 3.1200 - 3.0200 1.00 3791 171 0.1852 0.2278
REMARK 3 11 3.0200 - 2.9200 1.00 3800 189 0.1764 0.1961
REMARK 3 12 2.9200 - 2.8400 1.00 3764 199 0.1841 0.2367
REMARK 3 13 2.8400 - 2.7600 1.00 3804 194 0.1764 0.2092
REMARK 3 14 2.7600 - 2.7000 1.00 3781 189 0.1776 0.1940
REMARK 3 15 2.7000 - 2.6400 1.00 3713 224 0.1810 0.2192
REMARK 3 16 2.6400 - 2.5800 1.00 3790 198 0.1806 0.2088
REMARK 3 17 2.5800 - 2.5300 1.00 3776 164 0.1812 0.2185
REMARK 3 18 2.5300 - 2.4800 1.00 3794 184 0.1869 0.2521
REMARK 3 19 2.4800 - 2.4400 1.00 3720 197 0.1877 0.2164
REMARK 3 20 2.4400 - 2.4000 1.00 3770 214 0.1912 0.2316
REMARK 3 21 2.4000 - 2.3600 1.00 3701 195 0.1842 0.2050
REMARK 3 22 2.3600 - 2.3200 1.00 3805 186 0.1911 0.2291
REMARK 3 23 2.3200 - 2.2900 1.00 3704 210 0.1893 0.2446
REMARK 3 24 2.2900 - 2.2500 1.00 3754 200 0.1971 0.2560
REMARK 3 25 2.2500 - 2.2200 1.00 3702 219 0.2012 0.2620
REMARK 3 26 2.2200 - 2.2000 1.00 3742 194 0.2038 0.2447
REMARK 3 27 2.2000 - 2.1700 1.00 3740 181 0.2062 0.2493
REMARK 3 28 2.1700 - 2.1400 1.00 3708 197 0.2166 0.2354
REMARK 3 29 2.1400 - 2.1200 1.00 3751 202 0.2282 0.2656
REMARK 3 30 2.1200 - 2.0900 0.97 3601 205 0.2325 0.2792
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) : 0.204
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.399
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.23
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.79
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 9438
REMARK 3 ANGLE : 0.878 12853
REMARK 3 CHIRALITY : 0.053 1475
REMARK 3 PLANARITY : 0.006 1701
REMARK 3 DIHEDRAL : 5.624 5681
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 6KF5 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_1300012863.
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) : 0.97776
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 : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 119275
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.090
REMARK 200 RESOLUTION RANGE LOW (A) : 19.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 13.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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 (%): 68.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.88
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 35.38600
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 109.85350
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.38600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 109.85350
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 B 718 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 730 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 GLU D 79
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 79 CG CD OE1 OE2
REMARK 470 LYS A 178 CG CD CE NZ
REMARK 470 THR B 4 OG1 CG2
REMARK 470 GLU B 32 CG CD OE1 OE2
REMARK 470 GLU B 76 CG CD OE1 OE2
REMARK 470 LYS B 178 CG CD CE NZ
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 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 O HOH A 690 O HOH A 754 2.00
REMARK 500 O HOH A 623 O HOH A 650 2.06
REMARK 500 OE2 GLU D 16 O HOH D 501 2.06
REMARK 500 O HOH A 730 O HOH A 738 2.13
REMARK 500 O HOH C 619 O HOH C 701 2.14
REMARK 500 O HOH C 686 O HOH C 762 2.15
REMARK 500 O HOH C 616 O HOH C 721 2.15
REMARK 500 O HOH D 619 O HOH D 700 2.17
REMARK 500 O HOH B 673 O HOH B 679 2.17
REMARK 500 O HOH D 639 O HOH D 712 2.18
REMARK 500 OE2 GLU C 133 O HOH C 501 2.18
REMARK 500 O HOH A 778 O HOH C 761 2.18
REMARK 500 O HOH A 650 O HOH A 710 2.18
REMARK 500 O GLU B 33 O HOH B 501 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 1.89
REMARK 500 O HOH D 502 O HOH D 502 2754 1.93
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 -160.49 -164.37
REMARK 500 SER A 162 -117.02 68.17
REMARK 500 LEU A 186 142.41 -170.53
REMARK 500 PHE A 191 65.61 20.05
REMARK 500 VAL A 211 -70.25 69.21
REMARK 500 ASP B 96 -159.89 -164.14
REMARK 500 SER B 162 -113.96 61.96
REMARK 500 PHE B 191 66.86 19.40
REMARK 500 VAL B 211 -71.68 66.94
REMARK 500 HIS B 284 147.61 -39.22
REMARK 500 ALA C 22 -133.61 60.73
REMARK 500 ASP C 96 -161.77 -162.52
REMARK 500 PHE C 128 134.07 -39.53
REMARK 500 PRO C 129 31.62 -99.12
REMARK 500 SER C 162 -116.78 66.16
REMARK 500 LEU C 186 140.10 -174.67
REMARK 500 PHE C 191 63.08 21.90
REMARK 500 VAL C 211 -73.61 69.99
REMARK 500 HIS C 284 151.12 -42.78
REMARK 500 ASP D 96 -161.03 -166.60
REMARK 500 SER D 162 -111.92 65.62
REMARK 500 LEU D 186 139.46 -174.18
REMARK 500 PHE D 191 66.05 20.94
REMARK 500 VAL D 211 -68.55 69.68
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 788 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH A 789 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH A 790 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH A 791 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH B 736 DISTANCE = 7.16 ANGSTROMS
REMARK 525 HOH D 721 DISTANCE = 6.06 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 6NA 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 GOL A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 2FK A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue D8F B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue D8F C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue D8F D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 405
DBREF1 6KF5 A 1 314 UNP A0A074MDU6_ERYLO
DBREF2 6KF5 A A0A074MDU6 1 314
DBREF1 6KF5 B 1 314 UNP A0A074MDU6_ERYLO
DBREF2 6KF5 B A0A074MDU6 1 314
DBREF1 6KF5 C 1 314 UNP A0A074MDU6_ERYLO
DBREF2 6KF5 C A0A074MDU6 1 314
DBREF1 6KF5 D 1 314 UNP A0A074MDU6_ERYLO
DBREF2 6KF5 D A0A074MDU6 1 314
SEQADV 6KF5 LEU A 256 UNP A0A074MDU ILE 256 ENGINEERED MUTATION
SEQADV 6KF5 LEU B 256 UNP A0A074MDU ILE 256 ENGINEERED MUTATION
SEQADV 6KF5 LEU C 256 UNP A0A074MDU ILE 256 ENGINEERED MUTATION
SEQADV 6KF5 LEU D 256 UNP A0A074MDU ILE 256 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 LEU 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 SER 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 LEU 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 SER 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 LEU 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 SER 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 LEU 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 SER 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 6NA A 402 8
HET EDO A 403 4
HET EDO A 404 4
HET GOL A 405 6
HET GOL A 406 6
HET 2FK A 407 2
HET D8F B 401 17
HET GOL B 402 6
HET GOL B 403 6
HET D8F C 401 17
HET EDO C 402 4
HET D8F D 401 17
HET GOL D 402 6
HET GOL D 403 6
HET GOL D 404 6
HET GOL D 405 6
HETNAM D8F (4-NITROPHENYL) HEXANOATE
HETNAM 6NA HEXANOIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETNAM 2FK SUPEROXO ION
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 D8F 4(C12 H15 N O4)
FORMUL 6 6NA C6 H12 O2
FORMUL 7 EDO 3(C2 H6 O2)
FORMUL 9 GOL 8(C3 H8 O3)
FORMUL 11 2FK O2 1-
FORMUL 22 HOH *1042(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 LEU A 256 ALA A 270 1 15
HELIX 12 AB3 SER 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 LEU B 256 ALA B 270 1 15
HELIX 24 AC6 SER 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 LEU C 256 ALA C 270 1 15
HELIX 36 AD9 SER C 285 ILE C 289 5 5
HELIX 37 AE1 PRO C 294 GLY C 312 1 19
HELIX 38 AE2 ARG D 8 ALA D 22 1 15
HELIX 39 AE3 THR D 30 ASP D 46 1 17
HELIX 40 AE4 HIS D 100 ASP D 112 1 13
HELIX 41 AE5 PRO D 129 SER D 144 1 16
HELIX 42 AE6 SER D 145 GLY D 150 5 6
HELIX 43 AE7 SER D 162 LYS D 178 1 17
HELIX 44 AE8 SER D 200 PHE D 206 1 7
HELIX 45 AE9 THR D 213 LYS D 225 1 13
HELIX 46 AF1 PHE D 234 GLY D 238 5 5
HELIX 47 AF2 LEU D 256 ALA D 270 1 15
HELIX 48 AF3 SER D 285 ILE D 289 5 5
HELIX 49 AF4 PRO D 294 GLY D 312 1 19
SHEET 1 AA1 6 VAL A 54 GLY A 62 0
SHEET 2 AA1 6 GLY A 65 ASP A 73 -1 O LEU A 69 N LEU A 58
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 MET A 279 N THR A 250
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 THR B 250 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 GLY B 155 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 LEU C 69 N LEU C 58
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 THR D 250 O LEU D 277
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 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 0.86
CISPEP 2 PHE A 128 PRO A 129 0 3.57
CISPEP 3 ALA B 123 PRO B 124 0 -0.01
CISPEP 4 PHE B 128 PRO B 129 0 5.65
CISPEP 5 ALA C 123 PRO C 124 0 1.10
CISPEP 6 PHE C 128 PRO C 129 0 1.69
CISPEP 7 LEU C 311 GLY C 312 0 0.69
CISPEP 8 ALA D 123 PRO D 124 0 1.38
CISPEP 9 PHE D 128 PRO D 129 0 4.06
CISPEP 10 LEU D 311 GLY D 312 0 -13.18
SITE 1 AC1 14 TYR A 38 GLY A 90 GLY A 91 SER A 162
SITE 2 AC1 14 ALA A 163 LEU A 193 LEU A 212 ILE A 217
SITE 3 AC1 14 PHE A 220 HIS A 284 SER A 285 HOH A 529
SITE 4 AC1 14 HOH A 530 HOH A 637
SITE 1 AC2 5 GLU A 136 LEU A 174 ARG A 232 HOH A 760
SITE 2 AC2 5 PRO C 63
SITE 1 AC3 8 ARG A 35 TYR A 38 VAL A 39 GLY A 95
SITE 2 AC3 8 ASP A 96 THR A 99 HOH A 559 HOH A 654
SITE 1 AC4 4 GLU A 51 LEU A 52 ILE A 55 HOH A 522
SITE 1 AC5 6 ARG A 257 ARG A 261 GOL A 406 HOH A 581
SITE 2 AC5 6 HOH B 571 HOH B 623
SITE 1 AC6 3 ALA A 205 ARG A 257 GOL A 405
SITE 1 AC7 2 PRO A 24 HOH A 505
SITE 1 AC8 12 TYR B 38 GLY B 90 GLY B 91 SER B 162
SITE 2 AC8 12 ALA B 163 LEU B 193 LEU B 212 ILE B 217
SITE 3 AC8 12 PHE B 220 HIS B 284 SER B 285 HOH B 509
SITE 1 AC9 3 ARG B 257 ARG B 261 HOH B 511
SITE 1 AD1 8 LEU B 193 ASP B 196 ALA B 197 VAL B 198
SITE 2 AD1 8 ASP B 221 ARG B 228 PHE B 234 HOH B 509
SITE 1 AD2 9 TYR C 38 LEU C 41 GLY C 90 GLY C 91
SITE 2 AD2 9 SER C 162 ALA C 163 LEU C 212 HIS C 284
SITE 3 AD2 9 SER C 285
SITE 1 AD3 4 ASP C 119 TYR C 120 HOH C 506 HOH C 591
SITE 1 AD4 9 TYR D 38 GLY D 90 GLY D 91 SER D 162
SITE 2 AD4 9 ALA D 163 LEU D 212 PHE D 220 HIS D 284
SITE 3 AD4 9 SER D 285
SITE 1 AD5 3 ARG D 75 GLU D 76 SER D 77
SITE 1 AD6 4 HOH C 635 ARG D 257 ARG D 261 GOL D 404
SITE 1 AD7 4 ALA D 205 PHE D 206 ARG D 257 GOL D 403
SITE 1 AD8 7 LEU D 193 ASP D 196 ALA D 197 VAL D 198
SITE 2 AD8 7 ILE D 217 ASP D 221 ARG D 228
CRYST1 70.772 129.603 219.707 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 0.014130 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007716 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004552 0.00000
TER 2282 GLY A 312
TER 4560 GLY B 312
TER 6838 GLY C 312
TER 9115 GLY D 312
MASTER 443 0 17 49 32 0 31 610291 4 138 100
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