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HEADER HYDROLASE 05-JUL-19 6KF1
TITLE MICROBIAL HORMONE-SENSITIVE LIPASE- E53 MUTANT S162A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: LIPASE;
COMPND 8 CHAIN: D;
COMPND 9 ENGINEERED: YES;
COMPND 10 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;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: ERYTHROBACTER LONGUS;
SOURCE 9 ORGANISM_TAXID: 1044;
SOURCE 10 GENE: EH31_02760;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 12 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 6KF1 0
JRNL AUTH Y.XIAOCHEN,H.YINGYI,L.ZHENGYANG,J.SHULING,R.ZHEN,W.ZHAO,
JRNL AUTH 2 H.XIAOJIAN,C.HENGLIN,L.JIXI,X.XUEWEI
JRNL TITL FUNCTIONAL AND STRUCTURAL INSIGHTS INTO ENVIRONMENTAL
JRNL TITL 2 ADAPTATION OF A NOVEL HORMONE-SENSITIVE LIPASE, E53,
JRNL TITL 3 OBTAINED FROM ERYTHROBACTER LONGUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0253
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 136861
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.922
REMARK 3 FREE R VALUE TEST SET COUNT : 6777
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9485
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.12
REMARK 3 BIN R VALUE (WORKING SET) : 0.1940
REMARK 3 BIN FREE R VALUE SET COUNT : 472
REMARK 3 BIN FREE R VALUE : 0.2290
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9121
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 186
REMARK 3 SOLVENT ATOMS : 1429
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03500
REMARK 3 B22 (A**2) : -0.02900
REMARK 3 B33 (A**2) : -0.00600
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.113
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.110
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.071
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.525
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9505 ; 0.013 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 8977 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12953 ; 1.738 ; 1.643
REMARK 3 BOND ANGLES OTHERS (DEGREES): 20705 ; 1.461 ; 1.568
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1233 ; 6.613 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 431 ;24.575 ;20.812
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1378 ;12.399 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 72 ;23.875 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1286 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10795 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1973 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2143 ; 0.210 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 58 ; 0.176 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4871 ; 0.168 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1169 ; 0.202 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4954 ; 3.085 ; 3.181
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4949 ; 3.065 ; 3.179
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6178 ; 3.517 ; 4.746
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 6177 ; 3.519 ; 4.746
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4551 ; 3.829 ; 3.501
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4552 ; 3.829 ; 3.501
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6775 ; 5.140 ; 5.128
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6776 ; 5.140 ; 5.128
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 6KF1 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_1300012860.
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 136953
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.996
REMARK 200 RESOLUTION RANGE LOW (A) : 48.701
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 13.20
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 42.6330
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.35700
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: PHENIX
REMARK 200 STARTING MODEL: 4YPV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.30
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 35.19700
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 110.29100
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.19700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 110.29100
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 26.0 KCAL/MOL
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 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 PRO A 183 CG
REMARK 470 GLU A 204 CG CD OE1 OE2
REMARK 470 THR B 4 OG1 CG2
REMARK 470 GLU B 32 CG CD OE1 OE2
REMARK 470 GLU B 204 CG CD OE1 OE2
REMARK 470 THR C 4 OG1 CG2
REMARK 470 GLU C 51 CG CD OE1 OE2
REMARK 470 GLU C 76 CG CD OE1 OE2
REMARK 470 GLU C 79 CG CD OE1 OE2
REMARK 470 GLU C 204 CG CD OE1 OE2
REMARK 470 GLU D 204 CG CD OE1 OE2
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 686 O HOH A 829 1.70
REMARK 500 O HOH C 756 O HOH C 789 1.72
REMARK 500 O HOH D 712 O HOH D 771 1.79
REMARK 500 NH2 ARG A 228 O HOH A 501 1.80
REMARK 500 O HOH D 807 O HOH D 828 1.84
REMARK 500 O HOH C 728 O HOH C 833 1.93
REMARK 500 O HOH D 829 O HOH D 840 1.99
REMARK 500 O HOH D 666 O HOH D 752 2.04
REMARK 500 O HOH A 703 O HOH A 734 2.06
REMARK 500 OE1 GLU A 280 O HOH A 502 2.06
REMARK 500 OD1 ASP B 230 O HOH B 501 2.06
REMARK 500 O HOH C 748 O HOH C 755 2.08
REMARK 500 O HOH C 732 O HOH C 808 2.11
REMARK 500 O HOH D 809 O HOH D 828 2.13
REMARK 500 O HOH C 656 O HOH C 758 2.14
REMARK 500 CZ ARG A 228 O HOH A 501 2.14
REMARK 500 O HOH B 687 O HOH B 715 2.14
REMARK 500 O HOH C 615 O HOH C 833 2.15
REMARK 500 O HOH C 671 O HOH C 820 2.16
REMARK 500 O HOH B 683 O HOH B 707 2.16
REMARK 500 O HOH A 733 O HOH A 805 2.17
REMARK 500 O HOH A 638 O HOH A 726 2.18
REMARK 500 O HOH A 518 O HOH A 541 2.18
REMARK 500 O HOH D 550 O HOH D 720 2.19
REMARK 500 O HOH C 793 O HOH C 888 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 606 O HOH B 606 2755 1.10
REMARK 500 O HOH D 520 O HOH D 520 2556 1.34
REMARK 500 O HOH B 767 O HOH B 767 2755 1.60
REMARK 500 O HOH B 794 O HOH B 794 2755 1.79
REMARK 500 O HOH B 581 O HOH D 794 3565 2.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 133 CD GLU A 133 OE2 -0.090
REMARK 500 GLU B 76 CD GLU B 76 OE2 0.074
REMARK 500 GLU B 280 CD GLU B 280 OE2 0.070
REMARK 500 GLU C 133 CD GLU C 133 OE2 -0.112
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 257 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG C 151 CG - CD - NE ANGL. DEV. = 13.1 DEGREES
REMARK 500 ARG C 151 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG C 151 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG C 228 NE - CZ - NH1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG C 228 NE - CZ - NH2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG D 228 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
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 ALA A 80 130.88 -39.33
REMARK 500 ASP A 96 -165.77 -170.46
REMARK 500 PRO A 129 32.35 -97.97
REMARK 500 ALA A 162 -116.46 65.18
REMARK 500 PHE A 191 63.35 29.05
REMARK 500 VAL A 211 -73.19 73.40
REMARK 500 HIS A 284 144.78 -38.62
REMARK 500 ASP B 96 -156.26 -168.35
REMARK 500 ALA B 162 -114.78 66.93
REMARK 500 LEU B 186 140.03 -170.83
REMARK 500 PHE B 191 61.40 31.94
REMARK 500 VAL B 211 -68.69 72.79
REMARK 500 HIS B 284 142.04 -38.58
REMARK 500 SER B 285 7.88 82.79
REMARK 500 ASP C 96 -166.41 -167.98
REMARK 500 PRO C 129 32.20 -98.22
REMARK 500 ALA C 162 -118.30 64.49
REMARK 500 LEU C 186 139.70 -171.33
REMARK 500 PHE C 191 62.22 30.60
REMARK 500 VAL C 211 -72.11 73.32
REMARK 500 HIS C 284 144.36 -37.08
REMARK 500 ASP D 96 -162.79 -164.83
REMARK 500 PRO D 129 31.15 -98.55
REMARK 500 ALA D 162 -117.36 64.44
REMARK 500 PHE D 191 63.05 24.96
REMARK 500 VAL D 211 -71.31 71.62
REMARK 500 HIS D 284 136.32 -35.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR A 283 HIS A 284 149.26
REMARK 500 THR D 283 HIS D 284 149.57
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 871 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH A 872 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH A 873 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH D 841 DISTANCE = 6.76 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6NA A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6NA B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6NA C 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MES D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6NA D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6NA D 406
DBREF1 6KF1 A 4 312 UNP A0A074MDU6_ERYLO
DBREF2 6KF1 A A0A074MDU6 4 312
DBREF1 6KF1 B 4 312 UNP A0A074MDU6_ERYLO
DBREF2 6KF1 B A0A074MDU6 4 312
DBREF1 6KF1 C 4 312 UNP A0A074MDU6_ERYLO
DBREF2 6KF1 C A0A074MDU6 4 312
DBREF1 6KF1 D 3 312 UNP A0A074MDU6_ERYLO
DBREF2 6KF1 D A0A074MDU6 3 312
SEQADV 6KF1 ALA A 162 UNP A0A074MDU SER 162 ENGINEERED MUTATION
SEQADV 6KF1 ALA B 162 UNP A0A074MDU SER 162 ENGINEERED MUTATION
SEQADV 6KF1 ALA C 162 UNP A0A074MDU SER 162 ENGINEERED MUTATION
SEQADV 6KF1 ALA D 162 UNP A0A074MDU SER 162 ENGINEERED MUTATION
SEQRES 1 A 309 THR PRO PHE ILE ARG PRO ASP MET LYS ALA PHE LEU GLU
SEQRES 2 A 309 ALA ILE ALA ALA MET ALA GLY PRO THR LEU ALA GLU MET
SEQRES 3 A 309 THR LEU GLU GLU ALA ARG ALA SER TYR VAL ALA LEU HIS
SEQRES 4 A 309 GLY MET ALA ASP ARG PRO ALA ARG GLU LEU ALA VAL ILE
SEQRES 5 A 309 ARG ASN LEU SER CYS PRO GLY PRO ALA GLY ASP ILE PRO
SEQRES 6 A 309 LEU ARG LEU TYR ASP ALA ARG GLU SER ARG GLU ALA GLY
SEQRES 7 A 309 PRO VAL ILE THR PHE TYR HIS GLY GLY GLY PHE VAL ILE
SEQRES 8 A 309 GLY ASP LEU ASP THR HIS HIS ASN LEU CYS THR GLU ILE
SEQRES 9 A 309 ALA ALA LEU MET ASP LEU PRO VAL VAL ALA VAL ASP TYR
SEQRES 10 A 309 ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA ALA ILE GLU
SEQRES 11 A 309 ASP CYS GLU ALA ALA THR ARG TRP VAL ALA SER SER PRO
SEQRES 12 A 309 SER GLU LEU GLY ARG THR ALA SER GLY VAL ILE PRO ILE
SEQRES 13 A 309 GLY ASP ALA ALA GLY GLY ASN ALA THR ILE VAL VAL SER
SEQRES 14 A 309 GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL PRO VAL VAL
SEQRES 15 A 309 LEU GLN VAL PRO ILE PHE PRO LEU ALA SER ASP ALA VAL
SEQRES 16 A 309 GLY SER ALA SER LEU GLU ALA PHE ALA GLU GLY PHE VAL
SEQRES 17 A 309 LEU THR LYS ALA SER ILE GLU PHE PHE ASP THR ALA TYR
SEQRES 18 A 309 LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE PRO ILE LEU
SEQRES 19 A 309 GLY ASP HIS THR ALA ALA PRO PRO THR ILE VAL ALA THR
SEQRES 20 A 309 ALA SER LEU ASP PRO ILE ARG ASP SER GLY ARG ASP TYR
SEQRES 21 A 309 ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP VAL VAL TYR
SEQRES 22 A 309 LEU GLU MET GLU GLY VAL THR HIS SER PHE THR ASN ILE
SEQRES 23 A 309 ARG ALA ALA VAL PRO SER THR GLN GLY ASP LEU GLU ARG
SEQRES 24 A 309 ILE ILE ALA ALA MET LYS MET MET LEU GLY
SEQRES 1 B 309 THR PRO PHE ILE ARG PRO ASP MET LYS ALA PHE LEU GLU
SEQRES 2 B 309 ALA ILE ALA ALA MET ALA GLY PRO THR LEU ALA GLU MET
SEQRES 3 B 309 THR LEU GLU GLU ALA ARG ALA SER TYR VAL ALA LEU HIS
SEQRES 4 B 309 GLY MET ALA ASP ARG PRO ALA ARG GLU LEU ALA VAL ILE
SEQRES 5 B 309 ARG ASN LEU SER CYS PRO GLY PRO ALA GLY ASP ILE PRO
SEQRES 6 B 309 LEU ARG LEU TYR ASP ALA ARG GLU SER ARG GLU ALA GLY
SEQRES 7 B 309 PRO VAL ILE THR PHE TYR HIS GLY GLY GLY PHE VAL ILE
SEQRES 8 B 309 GLY ASP LEU ASP THR HIS HIS ASN LEU CYS THR GLU ILE
SEQRES 9 B 309 ALA ALA LEU MET ASP LEU PRO VAL VAL ALA VAL ASP TYR
SEQRES 10 B 309 ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA ALA ILE GLU
SEQRES 11 B 309 ASP CYS GLU ALA ALA THR ARG TRP VAL ALA SER SER PRO
SEQRES 12 B 309 SER GLU LEU GLY ARG THR ALA SER GLY VAL ILE PRO ILE
SEQRES 13 B 309 GLY ASP ALA ALA GLY GLY ASN ALA THR ILE VAL VAL SER
SEQRES 14 B 309 GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL PRO VAL VAL
SEQRES 15 B 309 LEU GLN VAL PRO ILE PHE PRO LEU ALA SER ASP ALA VAL
SEQRES 16 B 309 GLY SER ALA SER LEU GLU ALA PHE ALA GLU GLY PHE VAL
SEQRES 17 B 309 LEU THR LYS ALA SER ILE GLU PHE PHE ASP THR ALA TYR
SEQRES 18 B 309 LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE PRO ILE LEU
SEQRES 19 B 309 GLY ASP HIS THR ALA ALA PRO PRO THR ILE VAL ALA THR
SEQRES 20 B 309 ALA SER LEU ASP PRO ILE ARG ASP SER GLY ARG ASP TYR
SEQRES 21 B 309 ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP VAL VAL TYR
SEQRES 22 B 309 LEU GLU MET GLU GLY VAL THR HIS SER PHE THR ASN ILE
SEQRES 23 B 309 ARG ALA ALA VAL PRO SER THR GLN GLY ASP LEU GLU ARG
SEQRES 24 B 309 ILE ILE ALA ALA MET LYS MET MET LEU GLY
SEQRES 1 C 309 THR PRO PHE ILE ARG PRO ASP MET LYS ALA PHE LEU GLU
SEQRES 2 C 309 ALA ILE ALA ALA MET ALA GLY PRO THR LEU ALA GLU MET
SEQRES 3 C 309 THR LEU GLU GLU ALA ARG ALA SER TYR VAL ALA LEU HIS
SEQRES 4 C 309 GLY MET ALA ASP ARG PRO ALA ARG GLU LEU ALA VAL ILE
SEQRES 5 C 309 ARG ASN LEU SER CYS PRO GLY PRO ALA GLY ASP ILE PRO
SEQRES 6 C 309 LEU ARG LEU TYR ASP ALA ARG GLU SER ARG GLU ALA GLY
SEQRES 7 C 309 PRO VAL ILE THR PHE TYR HIS GLY GLY GLY PHE VAL ILE
SEQRES 8 C 309 GLY ASP LEU ASP THR HIS HIS ASN LEU CYS THR GLU ILE
SEQRES 9 C 309 ALA ALA LEU MET ASP LEU PRO VAL VAL ALA VAL ASP TYR
SEQRES 10 C 309 ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA ALA ILE GLU
SEQRES 11 C 309 ASP CYS GLU ALA ALA THR ARG TRP VAL ALA SER SER PRO
SEQRES 12 C 309 SER GLU LEU GLY ARG THR ALA SER GLY VAL ILE PRO ILE
SEQRES 13 C 309 GLY ASP ALA ALA GLY GLY ASN ALA THR ILE VAL VAL SER
SEQRES 14 C 309 GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL PRO VAL VAL
SEQRES 15 C 309 LEU GLN VAL PRO ILE PHE PRO LEU ALA SER ASP ALA VAL
SEQRES 16 C 309 GLY SER ALA SER LEU GLU ALA PHE ALA GLU GLY PHE VAL
SEQRES 17 C 309 LEU THR LYS ALA SER ILE GLU PHE PHE ASP THR ALA TYR
SEQRES 18 C 309 LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE PRO ILE LEU
SEQRES 19 C 309 GLY ASP HIS THR ALA ALA PRO PRO THR ILE VAL ALA THR
SEQRES 20 C 309 ALA SER LEU ASP PRO ILE ARG ASP SER GLY ARG ASP TYR
SEQRES 21 C 309 ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP VAL VAL TYR
SEQRES 22 C 309 LEU GLU MET GLU GLY VAL THR HIS SER PHE THR ASN ILE
SEQRES 23 C 309 ARG ALA ALA VAL PRO SER THR GLN GLY ASP LEU GLU ARG
SEQRES 24 C 309 ILE ILE ALA ALA MET LYS MET MET LEU GLY
SEQRES 1 D 310 ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA PHE LEU
SEQRES 2 D 310 GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU ALA GLU
SEQRES 3 D 310 MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL ALA LEU
SEQRES 4 D 310 HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU ALA VAL
SEQRES 5 D 310 ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY ASP ILE
SEQRES 6 D 310 PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG GLU ALA
SEQRES 7 D 310 GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY PHE VAL
SEQRES 8 D 310 ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS THR GLU
SEQRES 9 D 310 ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA VAL ASP
SEQRES 10 D 310 TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA ALA ILE
SEQRES 11 D 310 GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA SER SER
SEQRES 12 D 310 PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL ILE PRO
SEQRES 13 D 310 ILE GLY ASP ALA ALA GLY GLY ASN ALA THR ILE VAL VAL
SEQRES 14 D 310 SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL PRO VAL
SEQRES 15 D 310 VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER ASP ALA
SEQRES 16 D 310 VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU GLY PHE
SEQRES 17 D 310 VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP THR ALA
SEQRES 18 D 310 TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE PRO ILE
SEQRES 19 D 310 LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE VAL ALA
SEQRES 20 D 310 THR ALA SER LEU ASP PRO ILE ARG ASP SER GLY ARG ASP
SEQRES 21 D 310 TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP VAL VAL
SEQRES 22 D 310 TYR LEU GLU MET GLU GLY VAL THR HIS SER PHE THR ASN
SEQRES 23 D 310 ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP LEU GLU
SEQRES 24 D 310 ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY
HET NPO A 401 10
HET NPO A 402 10
HET NPO A 403 10
HET 6NA A 404 8
HET PGE A 405 10
HET NPO B 401 10
HET NPO B 402 10
HET NPO B 403 10
HET EDO B 404 4
HET 6NA B 405 8
HET NPO C 401 10
HET NPO C 402 10
HET NPO C 403 10
HET SO4 C 404 5
HET 6NA C 405 8
HET NPO D 401 10
HET NPO D 402 10
HET MES D 403 12
HET SO4 D 404 5
HET 6NA D 405 8
HET 6NA D 406 8
HETNAM NPO P-NITROPHENOL
HETNAM 6NA HEXANOIC ACID
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SO4 SULFATE ION
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 NPO 11(C6 H5 N O3)
FORMUL 8 6NA 5(C6 H12 O2)
FORMUL 9 PGE C6 H14 O4
FORMUL 13 EDO C2 H6 O2
FORMUL 18 SO4 2(O4 S 2-)
FORMUL 22 MES C6 H13 N O4 S
FORMUL 26 HOH *1429(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 ALA 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 SER A 285 ILE A 289 5 5
HELIX 13 AB4 SER A 295 GLY A 312 1 18
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 ALA 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 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 ALA 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 SER 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 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 ALA 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 ILE D 256 ALA D 270 1 15
HELIX 48 AF3 SER D 285 ILE D 289 5 5
HELIX 49 AF4 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 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 GLY B 62 0
SHEET 2 AA3 6 GLY B 65 ASP B 73 -1 O ILE B 67 N CYS B 60
SHEET 3 AA3 6 VAL B 115 VAL B 118 -1 O ALA B 117 N ARG B 70
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 GLY C 62 0
SHEET 2 AA4 6 GLY C 65 ASP C 73 -1 O LEU C 71 N ARG C 56
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 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 159 N THR D 85
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 -2.11
CISPEP 2 PHE A 128 PRO A 129 0 -1.43
CISPEP 3 ALA B 123 PRO B 124 0 0.24
CISPEP 4 PHE B 128 PRO B 129 0 4.48
CISPEP 5 ALA C 123 PRO C 124 0 -3.16
CISPEP 6 PHE C 128 PRO C 129 0 -0.67
CISPEP 7 ALA D 123 PRO D 124 0 -1.60
CISPEP 8 PHE D 128 PRO D 129 0 -0.59
SITE 1 AC1 9 GLY A 91 LEU A 193 ILE A 217 PHE A 220
SITE 2 AC1 9 ASP A 221 ILE A 256 NPO A 402 HOH A 555
SITE 3 AC1 9 HOH A 562
SITE 1 AC2 12 GLY A 91 PHE A 92 ALA A 163 ASN A 166
SITE 2 AC2 12 LEU A 193 ASP A 221 TYR A 224 ALA A 226
SITE 3 AC2 12 ARG A 228 PHE A 234 NPO A 401 HOH A 503
SITE 1 AC3 10 TYR A 38 LEU A 41 VAL A 211 PHE A 220
SITE 2 AC3 10 HIS A 284 SER A 285 HOH A 516 HOH A 540
SITE 3 AC3 10 HOH A 687 HOH A 688
SITE 1 AC4 3 ARG A 257 ARG A 261 HOH B 590
SITE 1 AC5 9 LYS A 265 ALA A 266 HOH A 618 HOH A 625
SITE 2 AC5 9 HOH A 715 LYS B 265 ALA B 266 GLU B 269
SITE 3 AC5 9 HOH B 561
SITE 1 AC6 11 GLY B 91 PHE B 92 ALA B 163 ASN B 166
SITE 2 AC6 11 LEU B 193 ASP B 221 ALA B 226 ARG B 228
SITE 3 AC6 11 PHE B 234 NPO B 402 HOH B 539
SITE 1 AC7 9 GLY B 91 LEU B 193 ILE B 217 PHE B 220
SITE 2 AC7 9 ASP B 221 ILE B 256 NPO B 401 HOH B 529
SITE 3 AC7 9 HOH B 596
SITE 1 AC8 6 LEU B 41 PHE B 220 HIS B 284 SER B 285
SITE 2 AC8 6 HOH B 513 HOH B 532
SITE 1 AC9 4 MET A 309 MET A 310 ARG B 302 HOH B 624
SITE 1 AD1 3 ARG B 257 ARG B 261 HOH B 626
SITE 1 AD2 11 GLY C 91 PHE C 92 ALA C 163 ASN C 166
SITE 2 AD2 11 LEU C 193 ASP C 221 TYR C 224 ALA C 226
SITE 3 AD2 11 PHE C 234 NPO C 402 HOH C 504
SITE 1 AD3 9 GLY C 91 LEU C 193 ILE C 217 PHE C 220
SITE 2 AD3 9 ASP C 221 ILE C 256 NPO C 401 HOH C 516
SITE 3 AD3 9 HOH C 558
SITE 1 AD4 6 VAL C 211 PHE C 220 HIS C 284 SER C 285
SITE 2 AD4 6 HOH C 647 HOH C 670
SITE 1 AD5 3 ARG C 272 HOH C 693 GLU D 280
SITE 1 AD6 4 ARG C 257 ARG C 261 HOH C 848 HOH D 595
SITE 1 AD7 9 GLY D 91 LEU D 193 ILE D 217 PHE D 220
SITE 2 AD7 9 ASP D 221 ILE D 256 NPO D 402 HOH D 583
SITE 3 AD7 9 HOH D 598
SITE 1 AD8 11 GLY D 91 PHE D 92 ALA D 163 ASN D 166
SITE 2 AD8 11 LEU D 193 ASP D 221 TYR D 224 ALA D 226
SITE 3 AD8 11 PHE D 234 NPO D 401 HOH D 529
SITE 1 AD9 13 SER B 145 PRO B 146 SER B 147 GLY B 150
SITE 2 AD9 13 ARG B 151 THR B 152 SER D 145 PRO D 146
SITE 3 AD9 13 GLY D 150 ARG D 151 THR D 152 HOH D 558
SITE 4 AD9 13 HOH D 572
SITE 1 AE1 1 ARG D 75
SITE 1 AE2 4 THR D 30 LEU D 31 GLU D 32 HOH D 662
SITE 1 AE3 6 ALA D 201 ARG D 257 ARG D 261 HOH D 679
SITE 2 AE3 6 HOH D 772 HOH D 816
CRYST1 70.394 129.786 220.582 90.00 90.00 90.00 P 21 2 21 12
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 0.014206 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007705 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004533 0.00000
TER 2276 GLY A 312
TER 4557 GLY B 312
TER 6830 GLY C 312
TER 9125 GLY D 312
MASTER 521 0 21 49 32 0 47 610736 4 186 96
END |