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HEADER HYDROLASE 08-DEC-21 7W8N
TITLE MICROBIAL HORMONE-SENSITIVE LIPASE E53 WILD TYPE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: LIPASE;
COMPND 7 CHAIN: C;
COMPND 8 ENGINEERED: 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 K-12;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 83333;
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 K-12;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 83333
KEYWDS ESTERASE, MICROBIAL HORMONE-SENSITIVE LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.YANG,Z.LI,X.XU,J.LI
REVDAT 1 23-FEB-22 7W8N 0
JRNL AUTH Y.DING,L.NIE,X.C.YANG,Y.LI,Y.Y.HUO,Z.LI,Y.GAO,H.L.CUI,J.LI,
JRNL AUTH 2 X.W.XU
JRNL TITL MECHANISM AND STRUCTURAL INSIGHTS INTO A NOVEL ESTERASE,
JRNL TITL 2 E53, ISOLATED FROM ERYTHROBACTER LONGUS .
JRNL REF FRONT MICROBIOL V. 12 98194 2021
JRNL REFN ESSN 1664-302X
JRNL PMID 35069500
JRNL DOI 10.3389/FMICB.2021.798194
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0257
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 203632
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) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.179
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 10276
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6344
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.43
REMARK 3 BIN R VALUE (WORKING SET) : 0.3174
REMARK 3 BIN FREE R VALUE SET COUNT : 322
REMARK 3 BIN FREE R VALUE : 0.3200
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9136
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 439
REMARK 3 SOLVENT ATOMS : 1431
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.03
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.13
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.186
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : FLAT BULK SOLVENT MODEL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.11
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7W8N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-DEC-21.
REMARK 100 THE DEPOSITION ID IS D_1300026206.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-SEP-16
REMARK 200 TEMPERATURE (KELVIN) : 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 : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 203632
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 48.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.1900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
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: PHENIX
REMARK 200 STARTING MODEL: 4YPV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES PH 6.5, PEG, AMMONIUM SULFATE,
REMARK 280 DIOXANE, PEG 1000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291.15K
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 35.28800
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 110.53950
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.28800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 110.53950
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 C1 NPO D 421 LIES ON A SPECIAL POSITION.
REMARK 375 C4 NPO D 421 LIES ON A SPECIAL POSITION.
REMARK 375 OH NPO D 421 LIES ON A SPECIAL POSITION.
REMARK 375 N1 NPO D 421 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 758 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 969 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D1655 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 76 CG CD OE1 OE2
REMARK 470 GLU A 79 CG CD OE1 OE2
REMARK 470 GLU A 204 CG CD OE1 OE2
REMARK 470 THR B 4 OG1 CG2
REMARK 470 THR C 4 OG1 CG2
REMARK 470 GLU C 79 CG CD OE1 OE2
REMARK 470 THR D 4 OG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O SER A 162 H GLY A 165 1.56
REMARK 500 O HOH B 702 O HOH B 971 1.88
REMARK 500 O HOH B 946 O HOH B 961 1.91
REMARK 500 O DMS A 414 O HOH A 501 1.92
REMARK 500 O HOH D 1719 O HOH D 1777 1.98
REMARK 500 O HOH C 917 O HOH C 988 2.02
REMARK 500 O HOH B 880 O HOH B 946 2.03
REMARK 500 O HOH C 972 O HOH C 1137 2.04
REMARK 500 O2 NPO B 620 O HOH B 701 2.06
REMARK 500 O HOH D 1708 O HOH D 1722 2.08
REMARK 500 O HOH A 502 O HOH A 792 2.08
REMARK 500 O1 EDO A 405 O HOH A 502 2.11
REMARK 500 O HOH A 625 O HOH C 1171 2.12
REMARK 500 OE1 GLU D 280 O HOH D 1501 2.14
REMARK 500 OE1 GLU C 280 O HOH C 901 2.15
REMARK 500 O HOH A 748 O HOH A 867 2.16
REMARK 500 O1 EDO A 412 O HOH A 503 2.17
REMARK 500 O HOH D 1505 O HOH D 1776 2.17
REMARK 500 O ARG A 151 O HOH A 504 2.17
REMARK 500 O HOH A 789 O HOH A 836 2.17
REMARK 500 O DMS C 819 O HOH C 902 2.18
REMARK 500 O HOH C 1090 O HOH C 1287 2.18
REMARK 500 O PRO A 63 O HOH A 505 2.19
REMARK 500 O HOH A 739 O HOH A 811 2.19
REMARK 500 O HOH D 1695 O HOH D 1779 2.19
REMARK 500 O HOH B 838 O HOH B 914 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 SD MET B 21 OH NPO B 621 2754 2.14
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 HIS A 284 CE1 HIS A 284 NE2 -0.074
REMARK 500 HIS B 284 CG HIS B 284 ND1 -0.090
REMARK 500 HIS B 284 ND1 HIS B 284 CE1 -0.120
REMARK 500 HIS C 284 CG HIS C 284 ND1 -0.101
REMARK 500 HIS C 284 ND1 HIS C 284 CE1 -0.129
REMARK 500 HIS C 284 NE2 HIS C 284 CD2 -0.075
REMARK 500 HIS D 284 CE1 HIS D 284 NE2 -0.142
REMARK 500 HIS D 284 NE2 HIS D 284 CD2 -0.068
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 SER A 162 CB - CA - C ANGL. DEV. = 11.4 DEGREES
REMARK 500 ALA A 163 CB - CA - C ANGL. DEV. = -10.3 DEGREES
REMARK 500 SER D 162 CB - CA - C ANGL. DEV. = 11.4 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 ASP A 96 -164.71 -164.60
REMARK 500 SER A 162 -121.11 56.85
REMARK 500 LEU A 186 137.30 -171.70
REMARK 500 PHE A 191 65.47 26.42
REMARK 500 VAL A 211 -55.55 68.72
REMARK 500 ASP B 96 -163.91 -167.29
REMARK 500 SER B 162 -122.24 60.27
REMARK 500 PHE B 191 66.79 23.38
REMARK 500 VAL B 211 -69.53 71.34
REMARK 500 ASP C 96 -164.68 -165.06
REMARK 500 PRO C 129 31.15 -99.43
REMARK 500 SER C 162 -118.47 61.37
REMARK 500 PHE C 191 61.46 28.14
REMARK 500 VAL C 211 -58.56 72.30
REMARK 500 SER D 162 -117.80 50.76
REMARK 500 LEU D 186 139.35 -171.66
REMARK 500 PHE D 191 66.25 24.23
REMARK 500 VAL D 211 -66.29 68.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 THR A 283 -10.70
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 899 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH B1022 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH B1023 DISTANCE = 7.46 ANGSTROMS
REMARK 525 HOH C1296 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH C1297 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH D1812 DISTANCE = 6.68 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 820 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C1008 O
REMARK 620 2 HOH C1109 O 106.2
REMARK 620 N 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7CIP RELATED DB: PDB
DBREF1 7W8N A 1 314 UNP A0A074MDU6_ERYLO
DBREF2 7W8N A A0A074MDU6 1 314
DBREF1 7W8N B 1 314 UNP A0A074MDU6_ERYLO
DBREF2 7W8N B A0A074MDU6 1 314
DBREF1 7W8N C 1 314 UNP A0A074MDU6_ERYLO
DBREF2 7W8N C A0A074MDU6 1 314
DBREF1 7W8N D 1 314 UNP A0A074MDU6_ERYLO
DBREF2 7W8N D A0A074MDU6 1 314
SEQADV 7W8N ALA C 204 UNP A0A074MDU GLU 204 CONFLICT
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 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 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 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 ALA 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 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 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 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 GOL A 401 9
HET EDO A 402 10
HET 6NA A 403 19
HET EDO A 404 10
HET EDO A 405 10
HET DMS A 406 10
HET DMS A 407 10
HET CCN A 408 6
HET CCN A 409 6
HET CCN A 410 6
HET CCN A 411 6
HET EDO A 412 10
HET CCN A 413 6
HET DMS A 414 10
HET DMS A 415 10
HET D8F A 416 32
HET 6NA A 417 19
HET CCN A 418 6
HET SO4 A 419 5
HET SO4 A 420 5
HET EDO B 601 10
HET EDO B 602 10
HET EDO B 603 10
HET DIO B 604 14
HET EDO B 605 10
HET EDO B 606 10
HET CCN B 607 6
HET EDO B 608 10
HET CCN B 609 6
HET CCN B 610 6
HET DMS B 611 10
HET DMS B 612 10
HET CCN B 613 6
HET CCN B 614 6
HET BUA B 615 13
HET DMS B 616 10
HET DMS B 617 10
HET CCN B 618 6
HET GOL B 619 9
HET NPO B 620 15
HET NPO B 621 15
HET DMS B 622 10
HET D8F B 623 32
HET EDO B 624 10
HET EDO C 801 10
HET GOL C 802 8
HET EDO C 803 10
HET EDO C 804 10
HET EDO C 805 10
HET EDO C 806 10
HET CCN C 807 6
HET CCN C 808 6
HET GOL C 809 8
HET 6NA C 810 19
HET CCN C 811 6
HET EDO C 812 10
HET GOL C 813 9
HET GOL C 814 9
HET EDO C 815 10
HET GOL C 816 9
HET D8F C 817 32
HET EDO C 818 10
HET DMS C 819 10
HET NA C 820 1
HET CCN C 821 6
HET DMS D 401 10
HET GOL D 402 9
HET EDO D 403 10
HET CCN D 404 6
HET EDO D 405 10
HET EDO D 406 10
HET EDO D 407 10
HET CCN D 408 6
HET DMS D 409 10
HET GOL D 410 8
HET CCN D 411 6
HET 6NA D 412 19
HET DMS D 413 10
HET EDO D 414 10
HET CCN D 415 6
HET CCN D 416 6
HET CCN D 417 6
HET 6NA D 418 19
HET CCN D 419 6
HET CCN D 420 6
HET NPO D 421 15
HET EDO D 422 10
HET D8F D 423 32
HETNAM GOL GLYCEROL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM 6NA HEXANOIC ACID
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM CCN ACETONITRILE
HETNAM D8F (4-NITROPHENYL) HEXANOATE
HETNAM SO4 SULFATE ION
HETNAM DIO 1,4-DIETHYLENE DIOXIDE
HETNAM BUA BUTANOIC ACID
HETNAM NPO P-NITROPHENOL
HETNAM NA SODIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 GOL 9(C3 H8 O3)
FORMUL 6 EDO 25(C2 H6 O2)
FORMUL 7 6NA 5(C6 H12 O2)
FORMUL 10 DMS 13(C2 H6 O S)
FORMUL 12 CCN 24(C2 H3 N)
FORMUL 20 D8F 4(C12 H15 N O4)
FORMUL 23 SO4 2(O4 S 2-)
FORMUL 28 DIO C4 H8 O2
FORMUL 39 BUA C4 H8 O2
FORMUL 44 NPO 3(C6 H5 N O3)
FORMUL 68 NA NA 1+
FORMUL 93 HOH *1431(H2 O)
HELIX 1 AA1 ARG A 8 ALA A 22 1 15
HELIX 2 AA2 THR A 30 ASP A 46 1 17
HELIX 3 AA3 HIS A 100 ASP A 112 1 13
HELIX 4 AA4 PRO A 129 SER A 144 1 16
HELIX 5 AA5 SER A 145 GLY A 150 5 6
HELIX 6 AA6 SER A 162 LYS A 178 1 17
HELIX 7 AA7 SER A 200 PHE A 206 1 7
HELIX 8 AA8 THR A 213 LYS A 225 1 13
HELIX 9 AA9 PHE A 234 GLY A 238 5 5
HELIX 10 AB1 ILE A 256 ALA A 270 1 15
HELIX 11 AB2 SER A 285 ILE A 289 5 5
HELIX 12 AB3 SER A 295 GLY A 312 1 18
HELIX 13 AB4 ARG B 8 ALA B 22 1 15
HELIX 14 AB5 THR B 30 ASP B 46 1 17
HELIX 15 AB6 HIS B 100 ASP B 112 1 13
HELIX 16 AB7 PRO B 129 SER B 144 1 16
HELIX 17 AB8 SER B 145 GLY B 150 5 6
HELIX 18 AB9 SER B 162 LYS B 178 1 17
HELIX 19 AC1 SER B 200 PHE B 206 1 7
HELIX 20 AC2 THR B 213 LYS B 225 1 13
HELIX 21 AC3 PHE B 234 GLY B 238 5 5
HELIX 22 AC4 ILE B 256 ALA B 270 1 15
HELIX 23 AC5 SER B 285 ILE B 289 5 5
HELIX 24 AC6 PRO B 294 GLY B 312 1 19
HELIX 25 AC7 ARG C 8 ALA C 22 1 15
HELIX 26 AC8 THR C 25 MET C 29 5 5
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 162 LYS C 178 1 17
HELIX 31 AD4 SER C 200 PHE C 206 1 7
HELIX 32 AD5 THR C 213 LYS C 225 1 13
HELIX 33 AD6 PHE C 234 GLY C 238 5 5
HELIX 34 AD7 ILE C 256 ALA C 270 1 15
HELIX 35 AD8 SER C 285 ILE C 289 5 5
HELIX 36 AD9 SER C 295 GLY C 312 1 18
HELIX 37 AE1 ARG D 8 ALA D 22 1 15
HELIX 38 AE2 THR D 30 ASP D 46 1 17
HELIX 39 AE3 HIS D 100 ASP D 112 1 13
HELIX 40 AE4 PRO D 129 SER D 144 1 16
HELIX 41 AE5 SER D 145 GLY D 150 5 6
HELIX 42 AE6 SER D 162 LYS D 178 1 17
HELIX 43 AE7 SER D 200 PHE D 206 1 7
HELIX 44 AE8 THR D 213 LYS D 225 1 13
HELIX 45 AE9 PHE D 234 GLY D 238 5 5
HELIX 46 AF1 ILE D 256 ALA D 270 1 15
HELIX 47 AF2 SER D 285 ILE D 289 5 5
HELIX 48 AF3 SER D 295 GLY D 312 1 18
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 71 N ARG A 56
SHEET 3 AA1 6 VAL A 115 VAL A 118 -1 O VAL A 115 N TYR A 72
SHEET 4 AA1 6 GLY A 81 TYR A 87 1 N ILE A 84 O VAL A 116
SHEET 5 AA1 6 ALA A 153 ASP A 161 1 O ILE A 157 N VAL A 83
SHEET 6 AA1 6 VAL A 188 ILE A 190 1 O ILE A 190 N GLY A 160
SHEET 1 AA2 4 THR A 246 ALA A 251 0
SHEET 2 AA2 4 VAL A 274 MET A 279 1 O VAL A 275 N VAL A 248
SHEET 3 AA2 4 VAL B 274 MET B 279 -1 O 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 GLY C 62 0
SHEET 2 AA4 6 GLY C 65 ASP C 73 -1 O ILE C 67 N CYS C 60
SHEET 3 AA4 6 VAL C 115 VAL C 118 -1 O VAL C 115 N TYR C 72
SHEET 4 AA4 6 GLY C 81 TYR C 87 1 N ILE C 84 O VAL C 116
SHEET 5 AA4 6 ALA C 153 ASP C 161 1 O ILE C 157 N VAL C 83
SHEET 6 AA4 6 VAL C 188 ILE C 190 1 O ILE C 190 N GLY C 160
SHEET 1 AA5 4 THR C 246 ALA C 251 0
SHEET 2 AA5 4 VAL C 274 MET C 279 1 O MET C 279 N THR C 250
SHEET 3 AA5 4 VAL D 274 MET D 279 -1 O TYR D 276 N VAL C 274
SHEET 4 AA5 4 THR D 246 ALA D 251 1 N VAL D 248 O VAL D 275
SHEET 1 AA6 6 VAL D 54 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 157 N VAL D 83
SHEET 6 AA6 6 VAL D 188 ILE D 190 1 O ILE D 190 N GLY D 160
LINK N1 NPO B 620 O2 NPO B 621 1555 2754 1.31
LINK NA NA C 820 O HOH C1008 1555 1555 3.16
LINK NA NA C 820 O HOH C1109 1555 1555 2.69
CISPEP 1 ALA A 123 PRO A 124 0 1.91
CISPEP 2 PHE A 128 PRO A 129 0 3.78
CISPEP 3 ALA B 123 PRO B 124 0 0.02
CISPEP 4 PHE B 128 PRO B 129 0 4.75
CISPEP 5 ALA C 123 PRO C 124 0 0.64
CISPEP 6 PHE C 128 PRO C 129 0 1.50
CISPEP 7 ALA D 123 PRO D 124 0 -0.63
CISPEP 8 PHE D 128 PRO D 129 0 6.26
CRYST1 70.576 129.838 221.079 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 0.014169 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007702 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004523 0.00000
TER 4535 GLY A 312
TER 9095 GLY B 312
TER 13641 GLY C 312
TER 18201 GLY D 312
MASTER 471 0 88 48 32 0 0 611006 4 910 100
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