| 5hc3-pdb | HEADER HYDROLASE 04-JAN-16 5HC3
TITLE THE 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;
COMPND 6 MUTATION: 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 5HC3 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. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 55582
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) : 0.140
REMARK 3 R VALUE (WORKING SET) : 0.137
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2942
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.47
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3885
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.1800
REMARK 3 BIN FREE R VALUE SET COUNT : 223
REMARK 3 BIN FREE R VALUE : 0.2610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10144
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 561
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.42000
REMARK 3 B22 (A**2) : 1.21000
REMARK 3 B33 (A**2) : -3.63000
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): 0.320
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.211
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.152
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.685
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10551 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 9796 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14357 ; 1.638 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): 22651 ; 1.017 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1403 ; 6.448 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 458 ;35.856 ;24.585
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1647 ;13.769 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 64 ;17.161 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1568 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12300 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2288 ; 0.002 ; 0.020
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): 5516 ; 2.550 ; 3.601
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5515 ; 2.548 ; 3.601
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6918 ; 3.823 ; 5.387
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 6919 ; 3.823 ; 5.388
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5035 ; 3.304 ; 3.872
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 5035 ; 3.301 ; 3.872
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 7429 ; 5.015 ; 5.678
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 12290 ; 6.425 ;28.743
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 12058 ; 6.334 ;28.569
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 ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5HC3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000216811.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.3
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 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58728
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
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 : 13.20
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5HC4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM TARTRATE DIHYDRATE, PH7.3,
REMARK 280 20% PEG 3350, 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 40.58000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.24500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.83950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.24500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.58000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 60.83950
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 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 GLY B 21
REMARK 465 MET B 22
REMARK 465 ASP B 23
REMARK 465 LEU B 24
REMARK 465 GLY B 25
REMARK 465 GLY B 26
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 ASN C 3
REMARK 465 MET C 22
REMARK 465 ASP C 23
REMARK 465 LEU C 24
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 465 ASP D 23
REMARK 465 LEU D 24
REMARK 465 GLY D 25
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 MET A 1 CG SD CE
REMARK 470 LEU A 24 CG CD1 CD2
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 D 525 O HOH D 613 1.76
REMARK 500 O HOH D 614 O HOH D 636 1.83
REMARK 500 O HOH B 608 O HOH B 661 1.93
REMARK 500 O HOH D 516 O HOH D 613 2.02
REMARK 500 O3 GOL B 402 O HOH B 501 2.04
REMARK 500 O1 GOL D 401 O HOH D 501 2.04
REMARK 500 O1 GOL B 401 O HOH B 502 2.07
REMARK 500 O HOH B 527 O HOH B 639 2.10
REMARK 500 O HOH A 487 O HOH A 502 2.12
REMARK 500 O HOH D 513 O HOH D 575 2.12
REMARK 500 O HOH C 512 O HOH C 528 2.13
REMARK 500 O3 GOL B 403 O HOH B 503 2.14
REMARK 500 O HOH B 612 O HOH B 658 2.16
REMARK 500 O HOH D 575 O HOH D 630 2.19
REMARK 500 O HOH C 516 O HOH C 522 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 A 498 O HOH C 502 4455 2.06
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 290 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 290 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG B 181 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 200 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 MET C 249 CG - SD - CE ANGL. DEV. = -10.1 DEGREES
REMARK 500 ARG D 331 NE - CZ - NH2 ANGL. DEV. = -3.0 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 23 -66.60 -106.68
REMARK 500 LEU A 24 70.94 22.93
REMARK 500 LEU A 113 179.99 78.17
REMARK 500 LEU A 143 -57.58 -127.92
REMARK 500 SER A 146 -156.28 -93.92
REMARK 500 ARG A 181 58.88 -144.40
REMARK 500 SER A 188 -119.87 62.14
REMARK 500 CYS A 217 59.57 31.15
REMARK 500 LEU A 239 -51.97 83.94
REMARK 500 CYS A 286 54.01 -100.57
REMARK 500 PHE A 322 72.40 -118.02
REMARK 500 MET B 110 0.56 59.59
REMARK 500 LEU B 113 178.46 75.45
REMARK 500 LEU B 143 -54.09 -124.08
REMARK 500 SER B 146 -152.63 -91.51
REMARK 500 SER B 188 -122.12 66.62
REMARK 500 CYS B 217 60.50 33.00
REMARK 500 LEU B 239 -53.74 71.70
REMARK 500 CYS B 286 32.03 -95.66
REMARK 500 MET C 110 0.14 59.95
REMARK 500 LEU C 113 179.66 77.92
REMARK 500 LEU C 143 -61.24 -130.36
REMARK 500 SER C 146 -153.90 -93.74
REMARK 500 SER C 188 -116.72 59.73
REMARK 500 CYS C 217 58.06 28.61
REMARK 500 LEU C 239 -47.67 62.10
REMARK 500 PRO C 265 -8.49 -59.66
REMARK 500 CYS C 286 39.60 -97.75
REMARK 500 PHE C 322 74.26 -107.37
REMARK 500 LYS D 4 -80.18 79.11
REMARK 500 PHE D 19 37.49 -98.51
REMARK 500 MET D 110 7.89 59.25
REMARK 500 LEU D 113 176.61 83.38
REMARK 500 SER D 129 -9.73 -59.04
REMARK 500 LEU D 143 -57.16 -129.86
REMARK 500 SER D 146 -152.36 -78.91
REMARK 500 SER D 188 -122.07 62.57
REMARK 500 CYS D 217 62.19 21.66
REMARK 500 LEU D 239 -55.71 71.21
REMARK 500 PHE D 322 70.52 -116.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5HC0 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT MUTATION
REMARK 900 RELATED ID: 5HC2 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH ANOTHER MUTATION SER188ALA
REMARK 900 RELATED ID: 5HC4 RELATED DB: PDB
REMARK 900 RELATED ID: 5HC5 RELATED DB: PDB
DBREF 5HC3 A 1 344 UNP H6BDX1 H6BDX1_9BACT 1 344
DBREF 5HC3 B 1 344 UNP H6BDX1 H6BDX1_9BACT 1 344
DBREF 5HC3 C 1 344 UNP H6BDX1 H6BDX1_9BACT 1 344
DBREF 5HC3 D 1 344 UNP H6BDX1 H6BDX1_9BACT 1 344
SEQADV 5HC3 MET A -20 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 GLY A -19 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 SER A -18 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 SER A -17 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS A -16 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS A -15 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS A -14 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS A -13 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS A -12 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS A -11 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS A -10 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 SER A -9 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 SER A -8 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 GLY A -7 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 LEU A -6 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 VAL A -5 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 PRO A -4 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 ARG A -3 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 GLY A -2 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 SER A -1 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS A 0 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 ALA A 170 UNP H6BDX1 SER 170 ENGINEERED MUTATION
SEQADV 5HC3 MET B -20 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 GLY B -19 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 SER B -18 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 SER B -17 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS B -16 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS B -15 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS B -14 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS B -13 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS B -12 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS B -11 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS B -10 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 SER B -9 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 SER B -8 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 GLY B -7 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 LEU B -6 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 VAL B -5 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 PRO B -4 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 ARG B -3 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 GLY B -2 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 SER B -1 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS B 0 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 ALA B 170 UNP H6BDX1 SER 170 ENGINEERED MUTATION
SEQADV 5HC3 MET C -20 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 GLY C -19 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 SER C -18 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 SER C -17 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS C -16 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS C -15 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS C -14 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS C -13 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS C -12 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS C -11 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS C -10 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 SER C -9 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 SER C -8 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 GLY C -7 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 LEU C -6 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 VAL C -5 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 PRO C -4 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 ARG C -3 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 GLY C -2 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 SER C -1 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS C 0 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 ALA C 170 UNP H6BDX1 SER 170 ENGINEERED MUTATION
SEQADV 5HC3 MET D -20 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 GLY D -19 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 SER D -18 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 SER D -17 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS D -16 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS D -15 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS D -14 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS D -13 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS D -12 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS D -11 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS D -10 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 SER D -9 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 SER D -8 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 GLY D -7 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 LEU D -6 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 VAL D -5 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 PRO D -4 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 ARG D -3 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 GLY D -2 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 SER D -1 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 HIS D 0 UNP H6BDX1 EXPRESSION TAG
SEQADV 5HC3 ALA D 170 UNP H6BDX1 SER 170 ENGINEERED MUTATION
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 ALA 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 ALA 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 ALA 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 ALA 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 B 401 6
HET GOL B 402 6
HET GOL B 403 6
HET GOL D 401 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 4(C3 H8 O3)
FORMUL 9 HOH *561(H2 O)
HELIX 1 AA1 ASP A 12 SER A 20 1 9
HELIX 2 AA2 SER A 32 SER A 42 1 11
HELIX 3 AA3 SER A 42 CYS A 59 1 18
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 GLU A 204 1 17
HELIX 8 AA8 SER A 206 ILE A 210 5 5
HELIX 9 AA9 SER A 229 ASN A 235 1 7
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 GLY A 304 1 16
HELIX 14 AB5 GLY A 318 PHE A 322 5 5
HELIX 15 AB6 CYS A 326 GLY A 343 1 18
HELIX 16 AB7 ASP B 12 PHE B 19 1 8
HELIX 17 AB8 SER B 32 SER B 42 1 11
HELIX 18 AB9 SER B 42 ALA B 58 1 17
HELIX 19 AC1 TYR B 117 SER B 129 1 13
HELIX 20 AC2 PRO B 155 HIS B 171 1 17
HELIX 21 AC3 HIS B 171 GLY B 176 1 6
HELIX 22 AC4 SER B 188 GLU B 204 1 17
HELIX 23 AC5 SER B 206 ILE B 210 5 5
HELIX 24 AC6 PRO B 230 ASN B 235 1 6
HELIX 25 AC7 ASN B 245 MET B 258 1 14
HELIX 26 AC8 TRP B 264 ALA B 268 5 5
HELIX 27 AC9 THR B 269 SER B 274 1 6
HELIX 28 AD1 LEU B 289 ALA B 303 1 15
HELIX 29 AD2 GLY B 318 PHE B 322 5 5
HELIX 30 AD3 CYS B 326 GLY B 343 1 18
HELIX 31 AD4 ASP C 12 SER C 20 1 9
HELIX 32 AD5 SER C 32 SER C 41 1 10
HELIX 33 AD6 SER C 42 CYS C 59 1 18
HELIX 34 AD7 TYR C 117 SER C 129 1 13
HELIX 35 AD8 PRO C 155 HIS C 171 1 17
HELIX 36 AD9 HIS C 171 GLY C 176 1 6
HELIX 37 AE1 SER C 188 GLU C 204 1 17
HELIX 38 AE2 SER C 206 ILE C 210 5 5
HELIX 39 AE3 PRO C 230 ASN C 235 1 6
HELIX 40 AE4 ASN C 245 MET C 258 1 14
HELIX 41 AE5 TRP C 264 ALA C 268 5 5
HELIX 42 AE6 THR C 269 SER C 274 1 6
HELIX 43 AE7 LEU C 289 ALA C 303 1 15
HELIX 44 AE8 GLY C 318 PHE C 322 5 5
HELIX 45 AE9 CYS C 326 GLY C 343 1 18
HELIX 46 AF1 ASP D 12 PHE D 19 1 8
HELIX 47 AF2 SER D 32 SER D 41 1 10
HELIX 48 AF3 SER D 42 ALA D 58 1 17
HELIX 49 AF4 TYR D 117 SER D 129 1 13
HELIX 50 AF5 PRO D 155 HIS D 171 1 17
HELIX 51 AF6 HIS D 171 GLY D 176 1 6
HELIX 52 AF7 SER D 188 GLU D 204 1 17
HELIX 53 AF8 SER D 206 ILE D 210 5 5
HELIX 54 AF9 SER D 229 ASN D 235 1 7
HELIX 55 AG1 ASN D 245 MET D 258 1 14
HELIX 56 AG2 TRP D 264 ALA D 268 5 5
HELIX 57 AG3 THR D 269 SER D 274 1 6
HELIX 58 AG4 LEU D 289 ALA D 303 1 15
HELIX 59 AG5 GLY D 318 PHE D 322 5 5
HELIX 60 AG6 CYS D 326 GLY D 343 1 18
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 ALA A 185 N ILE A 105
SHEET 6 AA116 GLY A 212 LEU A 216 1 O LEU A 216 N GLY A 186
SHEET 7 AA116 THR A 279 CYS A 286 1 O PHE A 280 N LEU A 213
SHEET 8 AA116 ALA A 307 ILE A 316 1 O LYS A 308 N ILE A 281
SHEET 9 AA116 ALA B 307 VAL B 312 -1 O CYS B 309 N MET A 313
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 GLY B 186 O LEU B 216
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 ILE B 91 O VAL B 134
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 MET C 136 N GLN C 89
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 ASN C 284 1 O PHE C 280 N LEU C 213
SHEET 8 AA216 ALA C 307 VAL C 312 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 PRO D 100
SHEET 15 AA216 ILE D 85 PRO D 93 -1 N GLN D 89 O MET D 136
SHEET 16 AA216 LEU D 70 THR D 78 -1 N GLU D 73 O TYR D 90
CISPEP 1 GLU A 80 PRO A 81 0 4.15
CISPEP 2 TYR A 154 PRO A 155 0 9.70
CISPEP 3 TRP A 224 PRO A 225 0 7.31
CISPEP 4 GLU B 80 PRO B 81 0 -2.54
CISPEP 5 TYR B 154 PRO B 155 0 13.83
CISPEP 6 TRP B 224 PRO B 225 0 -3.55
CISPEP 7 GLU C 80 PRO C 81 0 2.75
CISPEP 8 TYR C 154 PRO C 155 0 8.91
CISPEP 9 TRP C 224 PRO C 225 0 -1.81
CISPEP 10 GLU D 80 PRO D 81 0 8.48
CISPEP 11 TYR D 154 PRO D 155 0 6.37
CISPEP 12 TRP D 224 PRO D 225 0 -4.41
SITE 1 AC1 6 GLY B 108 GLY B 109 SER B 188 GLY B 189
SITE 2 AC1 6 HIS B 317 HOH B 502
SITE 1 AC2 7 HOH A 413 ASP B 291 ARG B 298 HOH B 501
SITE 2 AC2 7 HOH B 546 HOH B 576 MET C 258
SITE 1 AC3 7 ILE B 183 GLN B 211 PHE B 340 GLY B 343
SITE 2 AC3 7 GLY B 344 HOH B 503 HOH B 524
SITE 1 AC4 7 GLY D 108 GLY D 109 SER D 188 GLY D 189
SITE 2 AC4 7 HIS D 317 HOH D 501 HOH D 503
CRYST1 81.160 121.679 150.490 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 0.012321 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008218 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006645 0.00000
TER 2604 GLY A 344
TER 5166 GLY B 344
TER 7716 GLY C 344
TER 10298 GLY D 344
MASTER 511 0 4 60 32 0 8 610729 4 24 116
END
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