| content |
HEADER HYDROLASE 04-JAN-16 5HC4
TITLE STRUCTURE OF ESTERASE EST22
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPOLYTIC ENZYME;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ESTERASE, EST22, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LI,J.HUANG
REVDAT 1 18-JAN-17 5HC4 0
JRNL AUTH J.HUANG,Y.Y.HUO,R.JI,S.KUANG,C.JI,X.W.XU,J.LI
JRNL TITL STRUCTURAL INSIGHTS OF A HORMONE SENSITIVE LIPASE HOMOLOGUE
JRNL TITL 2 EST22.
JRNL REF SCI REP V. 6 28550 2016
JRNL REFN ESSN 2045-2322
JRNL PMID 27328716
JRNL DOI 10.1038/SREP28550
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 91396
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4786
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
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) : 5334
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.2320
REMARK 3 BIN FREE R VALUE SET COUNT : 280
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10183
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 1131
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.15000
REMARK 3 B22 (A**2) : 1.18000
REMARK 3 B33 (A**2) : -1.03000
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): 0.179
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.170
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.127
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.781
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10408 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14123 ; 1.918 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1361 ; 6.797 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 455 ;37.792 ;24.549
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1619 ;15.547 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 64 ;19.741 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1544 ; 0.128 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8024 ; 0.010 ; 0.021
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): 5454 ; 2.932 ; 3.096
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6808 ; 3.945 ; 4.620
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4954 ; 4.219 ; 3.289
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): 17703 ; 7.975 ;26.971
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 : MASK
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 USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES
REMARK 4
REMARK 4 5HC4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000216808.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAY-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 0.9785
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-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 101542
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.50
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES SODIUM, PH7.5, 1.5M LI2SO4,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 40.62150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.26100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.90550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.26100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.62150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 60.90550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 ASN A 3
REMARK 465 MET B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ASN B 3
REMARK 465 MET C -20
REMARK 465 GLY C -19
REMARK 465 SER C -18
REMARK 465 SER C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 GLY C 25
REMARK 465 GLY C 26
REMARK 465 MET D -20
REMARK 465 GLY D -19
REMARK 465 SER D -18
REMARK 465 SER D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 THR D 2
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 GLU A 43 CG CD OE1 OE2
REMARK 470 GLU B 44 CG CD OE1 OE2
REMARK 470 ASN C 3 CG OD1 ND2
REMARK 470 LYS C 4 CG CD CE NZ
REMARK 470 GLU C 7 CG CD OE1 OE2
REMARK 470 ASP C 23 CG OD1 OD2
REMARK 470 LEU C 24 CG CD1 CD2
REMARK 470 GLU C 31 CG CD OE1 OE2
REMARK 470 ASN D 3 CG OD1 ND2
REMARK 470 SER D 41 OG
REMARK 470 GLU D 43 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 B 600 O HOH B 632 1.91
REMARK 500 NH1 ARG D 331 O HOH D 401 1.94
REMARK 500 O HOH C 610 O HOH C 626 2.03
REMARK 500 SD MET C 258 O HOH C 601 2.08
REMARK 500 OE1 GLU D 204 O HOH D 402 2.11
REMARK 500 O HOH C 615 O HOH C 657 2.11
REMARK 500 O GLY D 109 O HOH D 403 2.12
REMARK 500 O HOH A 623 O HOH A 763 2.13
REMARK 500 NH1 ARG A 121 O HOH A 501 2.13
REMARK 500 OE1 GLU A 204 O HOH A 502 2.16
REMARK 500 O HOH C 615 O HOH C 622 2.16
REMARK 500 OE1 GLU C 204 O HOH C 401 2.18
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 D 258 O HOH A 747 3545 2.08
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 A 181 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 200 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ASP B 241 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG C 200 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG C 200 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP C 241 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG C 290 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 GLY D 26 N - CA - C ANGL. DEV. = -17.4 DEGREES
REMARK 500 VAL D 137 CB - CA - C ANGL. DEV. = -15.2 DEGREES
REMARK 500 ARG D 181 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ASP D 228 CB - CG - OD1 ANGL. DEV. = 6.2 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 SER A 42 153.45 -46.70
REMARK 500 LEU A 113 -179.99 81.95
REMARK 500 LEU A 143 -54.40 -135.82
REMARK 500 SER A 146 -149.93 -87.93
REMARK 500 SER A 188 -115.02 62.78
REMARK 500 CYS A 217 56.14 22.90
REMARK 500 LEU A 239 -54.05 71.22
REMARK 500 CYS A 286 42.06 -98.02
REMARK 500 SER A 306 102.52 -58.60
REMARK 500 PHE A 322 70.78 -119.26
REMARK 500 LEU B 24 88.77 -61.81
REMARK 500 SER B 95 -179.85 -176.56
REMARK 500 LEU B 113 177.59 71.01
REMARK 500 LEU B 143 -61.68 -131.99
REMARK 500 SER B 146 -149.94 -101.87
REMARK 500 SER B 188 -124.79 66.09
REMARK 500 CYS B 217 53.26 30.94
REMARK 500 LEU B 239 -55.47 74.58
REMARK 500 CYS B 286 46.32 -100.97
REMARK 500 PHE B 322 69.64 -117.90
REMARK 500 LEU C 113 178.77 83.72
REMARK 500 LEU C 143 -62.17 -127.28
REMARK 500 SER C 146 -151.16 -74.10
REMARK 500 SER C 188 -116.67 61.32
REMARK 500 CYS C 217 57.29 24.97
REMARK 500 THR C 233 -61.45 -96.00
REMARK 500 LEU C 239 -55.42 64.34
REMARK 500 CYS C 286 47.32 -98.97
REMARK 500 ILE D 5 -69.59 123.71
REMARK 500 LEU D 113 176.46 77.11
REMARK 500 LEU D 143 -62.07 -127.31
REMARK 500 SER D 146 -153.78 -83.64
REMARK 500 SER D 188 -117.88 59.60
REMARK 500 ASP D 208 -45.19 -17.44
REMARK 500 CYS D 217 57.63 22.97
REMARK 500 LEU D 239 -42.95 68.26
REMARK 500 CYS D 286 52.42 -100.28
REMARK 500 PHE D 322 70.04 -111.48
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 GLY B 26 GLY B 27 -145.57
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 C 682 DISTANCE = 5.81 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5HC0 RELATED DB: PDB
REMARK 900 5HC0 CONTAINS THE SAME PROTEIN COMPLEXED WITH THE LIGAND P-
REMARK 900 NITROPHENOL.
REMARK 900 RELATED ID: 5HC2 RELATED DB: PDB
REMARK 900 5HC2 CONTAINS THE SAME PROTEIN COMPLEXED WITH THE LIGAND P-
REMARK 900 NITROPHENOL. AT THE SAME TIME, IT HAVE A MUTATION SER188ALA.
REMARK 900 RELATED ID: 5HC3 RELATED DB: PDB
REMARK 900 5HC3 CONTAINS THE SAME PROTEIN AND HAVE A MUTATION SER170ALA.
REMARK 900 RELATED ID: 5HC5 RELATED DB: PDB
DBREF 5HC4 A 1 344 UNP H6BDX1 H6BDX1_9BACT 1 344
DBREF 5HC4 B 1 344 UNP H6BDX1 H6BDX1_9BACT 1 344
DBREF 5HC4 C 1 344 UNP H6BDX1 H6BDX1_9BACT 1 344
DBREF 5HC4 D 1 344 UNP H6BDX1 H6BDX1_9BACT 1 344
SEQADV 5HC4 MET A -20 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 GLY A -19 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 SER A -18 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 SER A -17 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS A -16 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS A -15 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS A -14 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS A -13 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS A -12 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS A -11 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS A -10 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 SER A -9 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 SER A -8 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 GLY A -7 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 LEU A -6 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 VAL A -5 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 PRO A -4 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 ARG A -3 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 GLY A -2 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 SER A -1 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS A 0 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 MET B -20 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 GLY B -19 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 SER B -18 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 SER B -17 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS B -16 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS B -15 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS B -14 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS B -13 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS B -12 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS B -11 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS B -10 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 SER B -9 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 SER B -8 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 GLY B -7 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 LEU B -6 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 VAL B -5 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 PRO B -4 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 ARG B -3 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 GLY B -2 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 SER B -1 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS B 0 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 MET C -20 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 GLY C -19 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 SER C -18 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 SER C -17 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS C -16 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS C -15 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS C -14 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS C -13 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS C -12 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS C -11 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS C -10 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 SER C -9 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 SER C -8 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 GLY C -7 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 LEU C -6 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 VAL C -5 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 PRO C -4 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 ARG C -3 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 GLY C -2 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 SER C -1 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS C 0 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 MET D -20 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 GLY D -19 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 SER D -18 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 SER D -17 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS D -16 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS D -15 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS D -14 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS D -13 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS D -12 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS D -11 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS D -10 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 SER D -9 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 SER D -8 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 GLY D -7 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 LEU D -6 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 VAL D -5 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 PRO D -4 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 ARG D -3 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 GLY D -2 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 SER D -1 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC4 HIS D 0 UNP H6BDX1 EXPRESSION TAG
SEQRES 1 A 365 MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS SER SER
SEQRES 2 A 365 GLY LEU VAL PRO ARG GLY SER HIS MET THR ASN LYS ILE
SEQRES 3 A 365 ALA GLU ASP PRO ARG ILE ASP PRO ARG ILE LYS ALA ILE
SEQRES 4 A 365 PHE SER GLY MET ASP LEU GLY GLY GLY GLY ASP VAL GLU
SEQRES 5 A 365 SER ARG GLU ALA MET LEU GLU ALA ALA SER SER GLU GLU
SEQRES 6 A 365 ALA THR ALA VAL ARG ASP GLY LEU ARG VAL PHE LEU ASP
SEQRES 7 A 365 ALA CYS ASP ASN GLU GLU ILE ALA PRO SER ALA GLY LEU
SEQRES 8 A 365 LYS ILE GLU ASP TYR GLU PHE THR SER GLU PRO ASP GLY
SEQRES 9 A 365 ASN ILE ALA LYS ILE GLN TYR ILE ARG PRO ASP SER THR
SEQRES 10 A 365 ASP LYS LEU PRO CYS VAL TYR TYR ILE HIS GLY GLY GLY
SEQRES 11 A 365 MET GLN SER LEU SER CYS TYR TYR GLY ASN TYR ARG ALA
SEQRES 12 A 365 TRP GLY LYS ILE ILE ALA SER ASN GLY VAL ALA VAL ALA
SEQRES 13 A 365 MET VAL GLU PHE ARG ASN ALA LEU VAL PRO SER ALA LEU
SEQRES 14 A 365 PRO GLU VAL ALA PRO TYR PRO ALA GLY LEU ASN ASP CYS
SEQRES 15 A 365 VAL SER GLY VAL LYS TRP VAL ALA SER HIS ALA ASP GLU
SEQRES 16 A 365 LEU GLY ILE ASP ALA SER ARG ILE ILE ILE ALA GLY GLU
SEQRES 17 A 365 SER GLY GLY GLY ASN LEU THR LEU ALA ALA GLY LEU ARG
SEQRES 18 A 365 LEU LYS GLN GLU GLY SER GLN ASP LEU ILE GLN GLY LEU
SEQRES 19 A 365 TYR ALA LEU CYS PRO TYR ILE ALA GLY SER TRP PRO SER
SEQRES 20 A 365 GLU ASP SER PRO SER SER THR GLU ASN ASN GLY ILE LEU
SEQRES 21 A 365 LEU ASP LEU HIS ASN ASN GLN GLY ALA MET GLY TYR GLY
SEQRES 22 A 365 ILE GLU ALA TYR GLU MET ARG ASP PRO LEU ALA TRP PRO
SEQRES 23 A 365 GLY PHE ALA THR GLU GLU ASP VAL SER GLY LEU VAL PRO
SEQRES 24 A 365 THR PHE ILE SER VAL ASN GLU CYS ASP PRO LEU ARG ASP
SEQRES 25 A 365 GLU GLY ILE ASN PHE TYR ARG LEU LEU LEU ARG ALA GLY
SEQRES 26 A 365 VAL SER ALA LYS CYS ARG GLN VAL MET GLY THR ILE HIS
SEQRES 27 A 365 GLY THR GLU ILE PHE PRO ILE ALA CYS PRO ASP VAL SER
SEQRES 28 A 365 ARG ASP THR ALA ALA SER ILE ALA ASN PHE CYS LYS GLY
SEQRES 29 A 365 GLY
SEQRES 1 B 365 MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS SER SER
SEQRES 2 B 365 GLY LEU VAL PRO ARG GLY SER HIS MET THR ASN LYS ILE
SEQRES 3 B 365 ALA GLU ASP PRO ARG ILE ASP PRO ARG ILE LYS ALA ILE
SEQRES 4 B 365 PHE SER GLY MET ASP LEU GLY GLY GLY GLY ASP VAL GLU
SEQRES 5 B 365 SER ARG GLU ALA MET LEU GLU ALA ALA SER SER GLU GLU
SEQRES 6 B 365 ALA THR ALA VAL ARG ASP GLY LEU ARG VAL PHE LEU ASP
SEQRES 7 B 365 ALA CYS ASP ASN GLU GLU ILE ALA PRO SER ALA GLY LEU
SEQRES 8 B 365 LYS ILE GLU ASP TYR GLU PHE THR SER GLU PRO ASP GLY
SEQRES 9 B 365 ASN ILE ALA LYS ILE GLN TYR ILE ARG PRO ASP SER THR
SEQRES 10 B 365 ASP LYS LEU PRO CYS VAL TYR TYR ILE HIS GLY GLY GLY
SEQRES 11 B 365 MET GLN SER LEU SER CYS TYR TYR GLY ASN TYR ARG ALA
SEQRES 12 B 365 TRP GLY LYS ILE ILE ALA SER ASN GLY VAL ALA VAL ALA
SEQRES 13 B 365 MET VAL GLU PHE ARG ASN ALA LEU VAL PRO SER ALA LEU
SEQRES 14 B 365 PRO GLU VAL ALA PRO TYR PRO ALA GLY LEU ASN ASP CYS
SEQRES 15 B 365 VAL SER GLY VAL LYS TRP VAL ALA SER HIS ALA ASP GLU
SEQRES 16 B 365 LEU GLY ILE ASP ALA SER ARG ILE ILE ILE ALA GLY GLU
SEQRES 17 B 365 SER GLY GLY GLY ASN LEU THR LEU ALA ALA GLY LEU ARG
SEQRES 18 B 365 LEU LYS GLN GLU GLY SER GLN ASP LEU ILE GLN GLY LEU
SEQRES 19 B 365 TYR ALA LEU CYS PRO TYR ILE ALA GLY SER TRP PRO SER
SEQRES 20 B 365 GLU ASP SER PRO SER SER THR GLU ASN ASN GLY ILE LEU
SEQRES 21 B 365 LEU ASP LEU HIS ASN ASN GLN GLY ALA MET GLY TYR GLY
SEQRES 22 B 365 ILE GLU ALA TYR GLU MET ARG ASP PRO LEU ALA TRP PRO
SEQRES 23 B 365 GLY PHE ALA THR GLU GLU ASP VAL SER GLY LEU VAL PRO
SEQRES 24 B 365 THR PHE ILE SER VAL ASN GLU CYS ASP PRO LEU ARG ASP
SEQRES 25 B 365 GLU GLY ILE ASN PHE TYR ARG LEU LEU LEU ARG ALA GLY
SEQRES 26 B 365 VAL SER ALA LYS CYS ARG GLN VAL MET GLY THR ILE HIS
SEQRES 27 B 365 GLY THR GLU ILE PHE PRO ILE ALA CYS PRO ASP VAL SER
SEQRES 28 B 365 ARG ASP THR ALA ALA SER ILE ALA ASN PHE CYS LYS GLY
SEQRES 29 B 365 GLY
SEQRES 1 C 365 MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS SER SER
SEQRES 2 C 365 GLY LEU VAL PRO ARG GLY SER HIS MET THR ASN LYS ILE
SEQRES 3 C 365 ALA GLU ASP PRO ARG ILE ASP PRO ARG ILE LYS ALA ILE
SEQRES 4 C 365 PHE SER GLY MET ASP LEU GLY GLY GLY GLY ASP VAL GLU
SEQRES 5 C 365 SER ARG GLU ALA MET LEU GLU ALA ALA SER SER GLU GLU
SEQRES 6 C 365 ALA THR ALA VAL ARG ASP GLY LEU ARG VAL PHE LEU ASP
SEQRES 7 C 365 ALA CYS ASP ASN GLU GLU ILE ALA PRO SER ALA GLY LEU
SEQRES 8 C 365 LYS ILE GLU ASP TYR GLU PHE THR SER GLU PRO ASP GLY
SEQRES 9 C 365 ASN ILE ALA LYS ILE GLN TYR ILE ARG PRO ASP SER THR
SEQRES 10 C 365 ASP LYS LEU PRO CYS VAL TYR TYR ILE HIS GLY GLY GLY
SEQRES 11 C 365 MET GLN SER LEU SER CYS TYR TYR GLY ASN TYR ARG ALA
SEQRES 12 C 365 TRP GLY LYS ILE ILE ALA SER ASN GLY VAL ALA VAL ALA
SEQRES 13 C 365 MET VAL GLU PHE ARG ASN ALA LEU VAL PRO SER ALA LEU
SEQRES 14 C 365 PRO GLU VAL ALA PRO TYR PRO ALA GLY LEU ASN ASP CYS
SEQRES 15 C 365 VAL SER GLY VAL LYS TRP VAL ALA SER HIS ALA ASP GLU
SEQRES 16 C 365 LEU GLY ILE ASP ALA SER ARG ILE ILE ILE ALA GLY GLU
SEQRES 17 C 365 SER GLY GLY GLY ASN LEU THR LEU ALA ALA GLY LEU ARG
SEQRES 18 C 365 LEU LYS GLN GLU GLY SER GLN ASP LEU ILE GLN GLY LEU
SEQRES 19 C 365 TYR ALA LEU CYS PRO TYR ILE ALA GLY SER TRP PRO SER
SEQRES 20 C 365 GLU ASP SER PRO SER SER THR GLU ASN ASN GLY ILE LEU
SEQRES 21 C 365 LEU ASP LEU HIS ASN ASN GLN GLY ALA MET GLY TYR GLY
SEQRES 22 C 365 ILE GLU ALA TYR GLU MET ARG ASP PRO LEU ALA TRP PRO
SEQRES 23 C 365 GLY PHE ALA THR GLU GLU ASP VAL SER GLY LEU VAL PRO
SEQRES 24 C 365 THR PHE ILE SER VAL ASN GLU CYS ASP PRO LEU ARG ASP
SEQRES 25 C 365 GLU GLY ILE ASN PHE TYR ARG LEU LEU LEU ARG ALA GLY
SEQRES 26 C 365 VAL SER ALA LYS CYS ARG GLN VAL MET GLY THR ILE HIS
SEQRES 27 C 365 GLY THR GLU ILE PHE PRO ILE ALA CYS PRO ASP VAL SER
SEQRES 28 C 365 ARG ASP THR ALA ALA SER ILE ALA ASN PHE CYS LYS GLY
SEQRES 29 C 365 GLY
SEQRES 1 D 365 MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS SER SER
SEQRES 2 D 365 GLY LEU VAL PRO ARG GLY SER HIS MET THR ASN LYS ILE
SEQRES 3 D 365 ALA GLU ASP PRO ARG ILE ASP PRO ARG ILE LYS ALA ILE
SEQRES 4 D 365 PHE SER GLY MET ASP LEU GLY GLY GLY GLY ASP VAL GLU
SEQRES 5 D 365 SER ARG GLU ALA MET LEU GLU ALA ALA SER SER GLU GLU
SEQRES 6 D 365 ALA THR ALA VAL ARG ASP GLY LEU ARG VAL PHE LEU ASP
SEQRES 7 D 365 ALA CYS ASP ASN GLU GLU ILE ALA PRO SER ALA GLY LEU
SEQRES 8 D 365 LYS ILE GLU ASP TYR GLU PHE THR SER GLU PRO ASP GLY
SEQRES 9 D 365 ASN ILE ALA LYS ILE GLN TYR ILE ARG PRO ASP SER THR
SEQRES 10 D 365 ASP LYS LEU PRO CYS VAL TYR TYR ILE HIS GLY GLY GLY
SEQRES 11 D 365 MET GLN SER LEU SER CYS TYR TYR GLY ASN TYR ARG ALA
SEQRES 12 D 365 TRP GLY LYS ILE ILE ALA SER ASN GLY VAL ALA VAL ALA
SEQRES 13 D 365 MET VAL GLU PHE ARG ASN ALA LEU VAL PRO SER ALA LEU
SEQRES 14 D 365 PRO GLU VAL ALA PRO TYR PRO ALA GLY LEU ASN ASP CYS
SEQRES 15 D 365 VAL SER GLY VAL LYS TRP VAL ALA SER HIS ALA ASP GLU
SEQRES 16 D 365 LEU GLY ILE ASP ALA SER ARG ILE ILE ILE ALA GLY GLU
SEQRES 17 D 365 SER GLY GLY GLY ASN LEU THR LEU ALA ALA GLY LEU ARG
SEQRES 18 D 365 LEU LYS GLN GLU GLY SER GLN ASP LEU ILE GLN GLY LEU
SEQRES 19 D 365 TYR ALA LEU CYS PRO TYR ILE ALA GLY SER TRP PRO SER
SEQRES 20 D 365 GLU ASP SER PRO SER SER THR GLU ASN ASN GLY ILE LEU
SEQRES 21 D 365 LEU ASP LEU HIS ASN ASN GLN GLY ALA MET GLY TYR GLY
SEQRES 22 D 365 ILE GLU ALA TYR GLU MET ARG ASP PRO LEU ALA TRP PRO
SEQRES 23 D 365 GLY PHE ALA THR GLU GLU ASP VAL SER GLY LEU VAL PRO
SEQRES 24 D 365 THR PHE ILE SER VAL ASN GLU CYS ASP PRO LEU ARG ASP
SEQRES 25 D 365 GLU GLY ILE ASN PHE TYR ARG LEU LEU LEU ARG ALA GLY
SEQRES 26 D 365 VAL SER ALA LYS CYS ARG GLN VAL MET GLY THR ILE HIS
SEQRES 27 D 365 GLY THR GLU ILE PHE PRO ILE ALA CYS PRO ASP VAL SER
SEQRES 28 D 365 ARG ASP THR ALA ALA SER ILE ALA ASN PHE CYS LYS GLY
SEQRES 29 D 365 GLY
HET GOL A 401 6
HET TRS A 402 8
HETNAM GOL GLYCEROL
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN TRS TRIS BUFFER
FORMUL 5 GOL C3 H8 O3
FORMUL 6 TRS C4 H12 N O3 1+
FORMUL 7 HOH *1131(H2 O)
HELIX 1 AA1 ASP A 12 SER A 20 1 9
HELIX 2 AA2 SER A 32 SER A 41 1 10
HELIX 3 AA3 SER A 42 ALA A 58 1 17
HELIX 4 AA4 TYR A 117 SER A 129 1 13
HELIX 5 AA5 PRO A 155 HIS A 171 1 17
HELIX 6 AA6 HIS A 171 GLY A 176 1 6
HELIX 7 AA7 SER A 188 GLY A 205 1 18
HELIX 8 AA8 SER A 206 ILE A 210 5 5
HELIX 9 AA9 PRO A 230 ASN A 235 1 6
HELIX 10 AB1 ASN A 245 MET A 258 1 14
HELIX 11 AB2 TRP A 264 ALA A 268 5 5
HELIX 12 AB3 THR A 269 SER A 274 1 6
HELIX 13 AB4 LEU A 289 ALA A 303 1 15
HELIX 14 AB5 GLY A 318 PHE A 322 5 5
HELIX 15 AB6 CYS A 326 GLY A 344 1 19
HELIX 16 AB7 LYS B 4 ASP B 8 5 5
HELIX 17 AB8 ASP B 12 SER B 20 1 9
HELIX 18 AB9 SER B 32 SER B 41 1 10
HELIX 19 AC1 SER B 42 CYS B 59 1 18
HELIX 20 AC2 TYR B 117 SER B 129 1 13
HELIX 21 AC3 PRO B 155 HIS B 171 1 17
HELIX 22 AC4 HIS B 171 GLY B 176 1 6
HELIX 23 AC5 SER B 188 GLU B 204 1 17
HELIX 24 AC6 SER B 206 ILE B 210 5 5
HELIX 25 AC7 SER B 229 ASN B 235 1 7
HELIX 26 AC8 ASN B 245 MET B 258 1 14
HELIX 27 AC9 TRP B 264 ALA B 268 5 5
HELIX 28 AD1 THR B 269 SER B 274 1 6
HELIX 29 AD2 LEU B 289 GLY B 304 1 16
HELIX 30 AD3 GLY B 318 PHE B 322 5 5
HELIX 31 AD4 CYS B 326 GLY B 343 1 18
HELIX 32 AD5 LYS C 4 ASP C 8 1 5
HELIX 33 AD6 ASP C 12 SER C 20 1 9
HELIX 34 AD7 SER C 32 SER C 41 1 10
HELIX 35 AD8 SER C 42 ALA C 58 1 17
HELIX 36 AD9 TYR C 117 SER C 129 1 13
HELIX 37 AE1 PRO C 155 HIS C 171 1 17
HELIX 38 AE2 HIS C 171 GLY C 176 1 6
HELIX 39 AE3 SER C 188 GLU C 204 1 17
HELIX 40 AE4 SER C 206 ILE C 210 5 5
HELIX 41 AE5 SER C 229 ASN C 235 1 7
HELIX 42 AE6 ASN C 245 MET C 258 1 14
HELIX 43 AE7 TRP C 264 ALA C 268 5 5
HELIX 44 AE8 THR C 269 SER C 274 1 6
HELIX 45 AE9 LEU C 289 ALA C 303 1 15
HELIX 46 AF1 GLY C 318 PHE C 322 5 5
HELIX 47 AF2 CYS C 326 GLY C 343 1 18
HELIX 48 AF3 ASP D 12 SER D 20 1 9
HELIX 49 AF4 SER D 32 SER D 42 1 11
HELIX 50 AF5 SER D 42 CYS D 59 1 18
HELIX 51 AF6 TYR D 117 SER D 129 1 13
HELIX 52 AF7 PRO D 155 HIS D 171 1 17
HELIX 53 AF8 SER D 188 GLU D 204 1 17
HELIX 54 AF9 SER D 206 ILE D 210 5 5
HELIX 55 AG1 PRO D 230 ASN D 235 1 6
HELIX 56 AG2 ASN D 245 MET D 258 1 14
HELIX 57 AG3 TRP D 264 ALA D 268 5 5
HELIX 58 AG4 THR D 269 SER D 274 1 6
HELIX 59 AG5 LEU D 289 ALA D 303 1 15
HELIX 60 AG6 GLY D 318 PHE D 322 5 5
HELIX 61 AG7 CYS D 326 GLY D 344 1 19
SHEET 1 AA116 LEU A 70 THR A 78 0
SHEET 2 AA116 ILE A 85 PRO A 93 -1 O TYR A 90 N GLU A 73
SHEET 3 AA116 ALA A 133 GLU A 138 -1 O MET A 136 N GLN A 89
SHEET 4 AA116 LEU A 99 ILE A 105 1 N VAL A 102 O ALA A 133
SHEET 5 AA116 ILE A 177 GLU A 187 1 O ILE A 183 N TYR A 103
SHEET 6 AA116 GLY A 212 LEU A 216 1 O LEU A 216 N GLY A 186
SHEET 7 AA116 THR A 279 ASN A 284 1 O PHE A 280 N LEU A 213
SHEET 8 AA116 ALA A 307 MET A 313 1 O VAL A 312 N VAL A 283
SHEET 9 AA116 ALA B 307 VAL B 312 -1 O GLN B 311 N GLN A 311
SHEET 10 AA116 THR B 279 ASN B 284 1 N VAL B 283 O VAL B 312
SHEET 11 AA116 GLY B 212 LEU B 216 1 N LEU B 213 O PHE B 280
SHEET 12 AA116 ILE B 177 GLU B 187 1 N ILE B 184 O TYR B 214
SHEET 13 AA116 LEU B 99 ILE B 105 1 N TYR B 103 O ILE B 183
SHEET 14 AA116 ALA B 133 GLU B 138 1 O ALA B 133 N VAL B 102
SHEET 15 AA116 ILE B 85 PRO B 93 -1 N LYS B 87 O GLU B 138
SHEET 16 AA116 LEU B 70 THR B 78 -1 N GLU B 73 O TYR B 90
SHEET 1 AA216 LEU C 70 THR C 78 0
SHEET 2 AA216 ILE C 85 PRO C 93 -1 O ALA C 86 N PHE C 77
SHEET 3 AA216 ALA C 133 GLU C 138 -1 O VAL C 134 N ILE C 91
SHEET 4 AA216 LEU C 99 ILE C 105 1 N VAL C 102 O ALA C 133
SHEET 5 AA216 ILE C 177 GLU C 187 1 O ALA C 185 N TYR C 103
SHEET 6 AA216 GLY C 212 LEU C 216 1 O LEU C 216 N GLY C 186
SHEET 7 AA216 THR C 279 CYS C 286 1 O PHE C 280 N LEU C 213
SHEET 8 AA216 ALA C 307 ILE C 316 1 O VAL C 312 N VAL C 283
SHEET 9 AA216 ALA D 307 ILE D 316 -1 O GLN D 311 N GLN C 311
SHEET 10 AA216 THR D 279 CYS D 286 1 N VAL D 283 O VAL D 312
SHEET 11 AA216 GLY D 212 LEU D 216 1 N LEU D 213 O PHE D 280
SHEET 12 AA216 ILE D 177 GLU D 187 1 N GLY D 186 O LEU D 216
SHEET 13 AA216 LEU D 99 ILE D 105 1 N TYR D 103 O ILE D 183
SHEET 14 AA216 ALA D 133 GLU D 138 1 O ALA D 133 N VAL D 102
SHEET 15 AA216 ILE D 85 PRO D 93 -1 N LYS D 87 O GLU D 138
SHEET 16 AA216 LEU D 70 THR D 78 -1 N PHE D 77 O ALA D 86
CISPEP 1 GLU A 80 PRO A 81 0 13.05
CISPEP 2 TYR A 154 PRO A 155 0 7.11
CISPEP 3 TRP A 224 PRO A 225 0 -0.87
CISPEP 4 GLY A 343 GLY A 344 0 -3.28
CISPEP 5 GLU B 80 PRO B 81 0 0.59
CISPEP 6 TYR B 154 PRO B 155 0 7.82
CISPEP 7 TRP B 224 PRO B 225 0 3.28
CISPEP 8 GLU C 80 PRO C 81 0 4.54
CISPEP 9 TYR C 154 PRO C 155 0 4.42
CISPEP 10 TRP C 224 PRO C 225 0 -2.98
CISPEP 11 GLY C 343 GLY C 344 0 -12.12
CISPEP 12 GLY D 25 GLY D 26 0 -6.94
CISPEP 13 GLU D 80 PRO D 81 0 3.09
CISPEP 14 TYR D 154 PRO D 155 0 7.65
CISPEP 15 TRP D 224 PRO D 225 0 -1.77
SITE 1 AC1 7 ARG A 49 LEU A 52 ARG A 53 SER A 112
SITE 2 AC1 7 LEU A 113 TYR A 117 VAL A 144
SITE 1 AC2 9 GLY A 108 GLY A 109 TYR A 120 GLU A 187
SITE 2 AC2 9 SER A 188 GLY A 189 HIS A 317 ILE A 321
SITE 3 AC2 9 HOH A 660
CRYST1 81.243 121.811 150.522 90.00 90.00 90.00 P 21 21 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 0.012309 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008209 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006644 0.00000
TER 2550 GLY A 344
TER 5100 GLY B 344
TER 7638 GLY C 344
TER 10192 GLY D 344
MASTER 529 0 2 61 32 0 5 611328 4 14 116
END |