HEADER ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE)06-APR-92 3XIN
TITLE PROTEIN ENGINEERING OF XYLOSE (GLUCOSE) ISOMERASE FROM ACTINOPLANES
TITLE 2 MISSOURIENSIS. 1. CRYSTALLOGRAPHY AND SITE-DIRECTED MUTAGENESIS OF
TITLE 3 METAL BINDING SITES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D-XYLOSE ISOMERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 5.3.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACTINOPLANES MISSOURIENSIS;
SOURCE 3 ORGANISM_TAXID: 1866
KEYWDS ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR J.JANIN
REVDAT 4 28-FEB-24 3XIN 1 SEQADV
REVDAT 3 24-FEB-09 3XIN 1 VERSN
REVDAT 2 01-APR-03 3XIN 1 JRNL
REVDAT 1 15-JUL-93 3XIN 0
JRNL AUTH J.JENKINS,J.JANIN,F.REY,M.CHIADMI,H.VAN TILBEURGH,I.LASTERS,
JRNL AUTH 2 M.DE MAEYER,D.VAN BELLE,S.J.WODAK,M.LAUWEREYS,P.STANSSENS,
JRNL AUTH 3 G.MATTHYSSENS,A.M.LAMBEIR
JRNL TITL PROTEIN ENGINEERING OF XYLOSE (GLUCOSE) ISOMERASE FROM
JRNL TITL 2 ACTINOPLANES MISSOURIENSIS. 1. CRYSTALLOGRAPHY AND
JRNL TITL 3 SITE-DIRECTED MUTAGENESIS OF METAL BINDING SITES.
JRNL REF BIOCHEMISTRY V. 31 5449 1992
JRNL REFN ISSN 0006-2960
JRNL PMID 1610791
JRNL DOI 10.1021/BI00139A005
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.-M.LAMBEIR,M.LAUWEREYS,P.STANSSENS,N.T.MRABET,J.SNAUWAERT,
REMARK 1 AUTH 2 H.VANTILBEURGH,G.MATTHYSSENS,I.LASTERS,M.DEMAEYER,S.J.WODAK,
REMARK 1 AUTH 3 J.JENKINS,M.CHIADMI,J.JANIN
REMARK 1 TITL PROTEIN ENGINEERING OF XYLOSE (GLUCOSE) ISOMERASE FROM
REMARK 1 TITL 2 ACTINOPLANES MISSOURIENSIS. 2. SITE-DIRECTED MUTAGENESIS OF
REMARK 1 TITL 3 THE XYLOSE BINDING SITE
REMARK 1 REF BIOCHEMISTRY V. 31 5459 1992
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH H.VANTILBEURGH,J.JENKINS,M.CHIADMI,J.JANIN S.J.WODAK,
REMARK 1 AUTH 2 N.T.MRABET,A.-M.LAMBEIR
REMARK 1 TITL PROTEIN ENGINEERING OF XYLOSE (GLUCOSE) ISOMERASE FROM
REMARK 1 TITL 2 ACTINOPLANES MISSOURIENSIS. 3. CHANGING METAL SPECIFICITY
REMARK 1 TITL 3 AND THE PH PROFILE BY SITE-DIRECTED MUTAGENESIS
REMARK 1 REF BIOCHEMISTRY V. 31 5467 1992
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH N.T.MRABET,A.VAN DENBROEK,I.VAN DEN BRANDE,P.STANSSENS,
REMARK 1 AUTH 2 Y.LAROCHE,A.-M.LAMBEIR,G.MATTHIJSSENS,J.JENKINS,M.CHIADMI,
REMARK 1 AUTH 3 H.VANTILBEURGH,F.REY,J.JANIN,W.J.QUAX,I.LASTERS,M.DEMAEYER,
REMARK 1 AUTH 4 S.J.WODAK
REMARK 1 TITL ARGININE RESIDUES AS STABILIZING ELEMENTS IN PROTEINS
REMARK 1 REF BIOCHEMISTRY V. 31 2239 1992
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 4
REMARK 1 AUTH F.REY,J.JENKINS,J.JANIN,I.LASTERS,P.ALARD,M.CLAESSENS,
REMARK 1 AUTH 2 G.MATTHYSSENS,S.WODAK
REMARK 1 TITL STRUCTURAL ANALYSIS OF THE 2.8 ANGSTROMS MODEL OF XYLOSE
REMARK 1 TITL 2 ISOMERASE FROM ACTINOPLANES MISSOURIENSIS
REMARK 1 REF PROTEINS V. 4 165 1988
REMARK 1 REFN ISSN 0887-3585
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 107427
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12212
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 904
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.011 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.038 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.036 ; 0.040
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.010 ; 0.010
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.127 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : 0.267 ; 0.500
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3XIN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000179194.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 154.33333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 77.16667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 77.16667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 154.33333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 31600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -114.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 SER A 2
REMARK 465 SER B 2
REMARK 465 SER C 2
REMARK 465 SER 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 GLN A 4 CG CD OE1 NE2
REMARK 470 GLN A 66 CG CD OE1 NE2
REMARK 470 ASP A 280 CG OD1 OD2
REMARK 470 GLN B 4 CG CD OE1 NE2
REMARK 470 GLN B 66 CG CD OE1 NE2
REMARK 470 ASP B 280 CG OD1 OD2
REMARK 470 GLN C 4 CG CD OE1 NE2
REMARK 470 GLN C 66 CG CD OE1 NE2
REMARK 470 ASP C 280 CG OD1 OD2
REMARK 470 GLN D 4 CG CD OE1 NE2
REMARK 470 GLN D 66 CG CD OE1 NE2
REMARK 470 ASP D 280 CG OD1 OD2
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 OE1 GLN B 204 OE1 GLN D 204 1.59
REMARK 500 OE1 GLN A 204 OE1 GLN C 204 1.61
REMARK 500 O HOH C 623 O HOH C 624 2.16
REMARK 500 NH1 ARG D 394 O HOH D 601 2.16
REMARK 500 O HOH B 402 O HOH B 504 2.18
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 7 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ASP A 55 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 57 CB - CG - OD1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ASP A 80 CA - CB - CG ANGL. DEV. = -15.9 DEGREES
REMARK 500 ASP A 80 CB - CG - OD1 ANGL. DEV. = -9.5 DEGREES
REMARK 500 ARG A 109 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG A 113 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 113 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 117 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG A 117 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG A 121 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ASP A 124 CB - CG - OD1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 ASP A 146 CB - CG - OD1 ANGL. DEV. = 8.7 DEGREES
REMARK 500 ASP A 150 CB - CG - OD1 ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG A 157 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 TYR A 158 CB - CG - CD2 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 159 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ASP A 171 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 172 CD - NE - CZ ANGL. DEV. = 11.8 DEGREES
REMARK 500 ARG A 172 NE - CZ - NH1 ANGL. DEV. = 8.2 DEGREES
REMARK 500 ARG A 172 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG A 188 CD - NE - CZ ANGL. DEV. = 11.8 DEGREES
REMARK 500 ARG A 188 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 GLU A 205 OE1 - CD - OE2 ANGL. DEV. = -9.8 DEGREES
REMARK 500 GLU A 207 CA - CB - CG ANGL. DEV. = 13.6 DEGREES
REMARK 500 ASP A 273 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 GLU A 299 OE1 - CD - OE2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 ASP A 300 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 300 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG A 313 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 321 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 326 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ASP A 328 CB - CG - OD2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ARG A 361 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 361 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP A 368 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP A 368 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG A 394 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 ARG A 394 NH1 - CZ - NH2 ANGL. DEV. = 10.4 DEGREES
REMARK 500 ARG A 394 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG A 394 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG B 23 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 31 NE - CZ - NH2 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 68 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG B 68 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP B 80 CB - CG - OD1 ANGL. DEV. = -7.7 DEGREES
REMARK 500 ARG B 109 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 113 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 117 NE - CZ - NH1 ANGL. DEV. = 8.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 128 ANGLE DEVIATIONS.
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 THR A 17 -75.28 -82.99
REMARK 500 ASP A 24 -166.42 -101.25
REMARK 500 PHE A 94 -31.25 -138.01
REMARK 500 GLU A 186 107.16 74.92
REMARK 500 LYS A 239 37.18 71.50
REMARK 500 ASN A 247 -175.07 -171.06
REMARK 500 HIS A 250 73.10 -112.84
REMARK 500 PRO A 252 96.80 -69.97
REMARK 500 PHE A 364 -72.22 -160.64
REMARK 500 THR B 17 -75.21 -78.95
REMARK 500 ALA B 22 37.12 75.80
REMARK 500 GLU B 186 107.32 70.50
REMARK 500 LEU B 193 61.35 66.36
REMARK 500 HIS B 250 74.19 -115.31
REMARK 500 PRO B 252 97.67 -66.08
REMARK 500 ASP B 280 47.38 71.14
REMARK 500 PHE B 364 -75.69 -155.77
REMARK 500 THR C 17 -71.91 -82.76
REMARK 500 GLU C 186 110.76 74.62
REMARK 500 LEU C 193 63.80 61.77
REMARK 500 ASN C 247 -171.20 -170.42
REMARK 500 HIS C 250 76.26 -111.77
REMARK 500 PRO C 279 -74.19 -25.51
REMARK 500 ASP C 280 -91.87 -66.00
REMARK 500 ASP C 300 -167.56 -102.21
REMARK 500 PHE C 364 -67.50 -164.99
REMARK 500 THR D 17 -76.19 -83.53
REMARK 500 ALA D 22 39.15 70.09
REMARK 500 ASP D 24 -165.46 -103.29
REMARK 500 PHE D 94 -24.16 -140.48
REMARK 500 GLU D 186 105.01 78.38
REMARK 500 LEU D 193 62.61 60.54
REMARK 500 HIS D 250 75.78 -110.21
REMARK 500 PHE D 254 160.30 -49.18
REMARK 500 ASN D 277 57.63 -99.16
REMARK 500 ASP D 280 36.42 85.21
REMARK 500 PRO D 346 150.03 -48.06
REMARK 500 PHE D 364 -69.20 -160.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG B 172 0.12 SIDE CHAIN
REMARK 500 ARG C 172 0.11 SIDE CHAIN
REMARK 500 ARG D 208 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE E181Q MUTATION AFFECTS METAL BINDING. CRYSTALS WERE
REMARK 600 SOAKED IN XYLOSE AND MG++. NO LIGAND OR METAL BINDING WAS
REMARK 600 OBSERVED.
DBREF 3XIN A 2 394 UNP P12851 XYLA_ACTMI 1 393
DBREF 3XIN B 2 394 UNP P12851 XYLA_ACTMI 1 393
DBREF 3XIN C 2 394 UNP P12851 XYLA_ACTMI 1 393
DBREF 3XIN D 2 394 UNP P12851 XYLA_ACTMI 1 393
SEQADV 3XIN GLN A 181 UNP P12851 GLU 180 CONFLICT
SEQADV 3XIN GLN B 181 UNP P12851 GLU 180 CONFLICT
SEQADV 3XIN GLN C 181 UNP P12851 GLU 180 CONFLICT
SEQADV 3XIN GLN D 181 UNP P12851 GLU 180 CONFLICT
SEQRES 1 A 393 SER VAL GLN ALA THR ARG GLU ASP LYS PHE SER PHE GLY
SEQRES 2 A 393 LEU TRP THR VAL GLY TRP GLN ALA ARG ASP ALA PHE GLY
SEQRES 3 A 393 ASP ALA THR ARG THR ALA LEU ASP PRO VAL GLU ALA VAL
SEQRES 4 A 393 HIS LYS LEU ALA GLU ILE GLY ALA TYR GLY ILE THR PHE
SEQRES 5 A 393 HIS ASP ASP ASP LEU VAL PRO PHE GLY SER ASP ALA GLN
SEQRES 6 A 393 THR ARG ASP GLY ILE ILE ALA GLY PHE LYS LYS ALA LEU
SEQRES 7 A 393 ASP GLU THR GLY LEU ILE VAL PRO MET VAL THR THR ASN
SEQRES 8 A 393 LEU PHE THR HIS PRO VAL PHE LYS ASP GLY GLY PHE THR
SEQRES 9 A 393 SER ASN ASP ARG SER VAL ARG ARG TYR ALA ILE ARG LYS
SEQRES 10 A 393 VAL LEU ARG GLN MET ASP LEU GLY ALA GLU LEU GLY ALA
SEQRES 11 A 393 LYS THR LEU VAL LEU TRP GLY GLY ARG GLU GLY ALA GLU
SEQRES 12 A 393 TYR ASP SER ALA LYS ASP VAL SER ALA ALA LEU ASP ARG
SEQRES 13 A 393 TYR ARG GLU ALA LEU ASN LEU LEU ALA GLN TYR SER GLU
SEQRES 14 A 393 ASP ARG GLY TYR GLY LEU ARG PHE ALA ILE GLN PRO LYS
SEQRES 15 A 393 PRO ASN GLU PRO ARG GLY ASP ILE LEU LEU PRO THR ALA
SEQRES 16 A 393 GLY HIS ALA ILE ALA PHE VAL GLN GLU LEU GLU ARG PRO
SEQRES 17 A 393 GLU LEU PHE GLY ILE ASN PRO GLU THR GLY HIS GLU GLN
SEQRES 18 A 393 MET SER ASN LEU ASN PHE THR GLN GLY ILE ALA GLN ALA
SEQRES 19 A 393 LEU TRP HIS LYS LYS LEU PHE HIS ILE ASP LEU ASN GLY
SEQRES 20 A 393 GLN HIS GLY PRO LYS PHE ASP GLN ASP LEU VAL PHE GLY
SEQRES 21 A 393 HIS GLY ASP LEU LEU ASN ALA PHE SER LEU VAL ASP LEU
SEQRES 22 A 393 LEU GLU ASN GLY PRO ASP GLY ALA PRO ALA TYR ASP GLY
SEQRES 23 A 393 PRO ARG HIS PHE ASP TYR LYS PRO SER ARG THR GLU ASP
SEQRES 24 A 393 TYR ASP GLY VAL TRP GLU SER ALA LYS ALA ASN ILE ARG
SEQRES 25 A 393 MET TYR LEU LEU LEU LYS GLU ARG ALA LYS ALA PHE ARG
SEQRES 26 A 393 ALA ASP PRO GLU VAL GLN GLU ALA LEU ALA ALA SER LYS
SEQRES 27 A 393 VAL ALA GLU LEU LYS THR PRO THR LEU ASN PRO GLY GLU
SEQRES 28 A 393 GLY TYR ALA GLU LEU LEU ALA ASP ARG SER ALA PHE GLU
SEQRES 29 A 393 ASP TYR ASP ALA ASP ALA VAL GLY ALA LYS GLY PHE GLY
SEQRES 30 A 393 PHE VAL LYS LEU ASN GLN LEU ALA ILE GLU HIS LEU LEU
SEQRES 31 A 393 GLY ALA ARG
SEQRES 1 B 393 SER VAL GLN ALA THR ARG GLU ASP LYS PHE SER PHE GLY
SEQRES 2 B 393 LEU TRP THR VAL GLY TRP GLN ALA ARG ASP ALA PHE GLY
SEQRES 3 B 393 ASP ALA THR ARG THR ALA LEU ASP PRO VAL GLU ALA VAL
SEQRES 4 B 393 HIS LYS LEU ALA GLU ILE GLY ALA TYR GLY ILE THR PHE
SEQRES 5 B 393 HIS ASP ASP ASP LEU VAL PRO PHE GLY SER ASP ALA GLN
SEQRES 6 B 393 THR ARG ASP GLY ILE ILE ALA GLY PHE LYS LYS ALA LEU
SEQRES 7 B 393 ASP GLU THR GLY LEU ILE VAL PRO MET VAL THR THR ASN
SEQRES 8 B 393 LEU PHE THR HIS PRO VAL PHE LYS ASP GLY GLY PHE THR
SEQRES 9 B 393 SER ASN ASP ARG SER VAL ARG ARG TYR ALA ILE ARG LYS
SEQRES 10 B 393 VAL LEU ARG GLN MET ASP LEU GLY ALA GLU LEU GLY ALA
SEQRES 11 B 393 LYS THR LEU VAL LEU TRP GLY GLY ARG GLU GLY ALA GLU
SEQRES 12 B 393 TYR ASP SER ALA LYS ASP VAL SER ALA ALA LEU ASP ARG
SEQRES 13 B 393 TYR ARG GLU ALA LEU ASN LEU LEU ALA GLN TYR SER GLU
SEQRES 14 B 393 ASP ARG GLY TYR GLY LEU ARG PHE ALA ILE GLN PRO LYS
SEQRES 15 B 393 PRO ASN GLU PRO ARG GLY ASP ILE LEU LEU PRO THR ALA
SEQRES 16 B 393 GLY HIS ALA ILE ALA PHE VAL GLN GLU LEU GLU ARG PRO
SEQRES 17 B 393 GLU LEU PHE GLY ILE ASN PRO GLU THR GLY HIS GLU GLN
SEQRES 18 B 393 MET SER ASN LEU ASN PHE THR GLN GLY ILE ALA GLN ALA
SEQRES 19 B 393 LEU TRP HIS LYS LYS LEU PHE HIS ILE ASP LEU ASN GLY
SEQRES 20 B 393 GLN HIS GLY PRO LYS PHE ASP GLN ASP LEU VAL PHE GLY
SEQRES 21 B 393 HIS GLY ASP LEU LEU ASN ALA PHE SER LEU VAL ASP LEU
SEQRES 22 B 393 LEU GLU ASN GLY PRO ASP GLY ALA PRO ALA TYR ASP GLY
SEQRES 23 B 393 PRO ARG HIS PHE ASP TYR LYS PRO SER ARG THR GLU ASP
SEQRES 24 B 393 TYR ASP GLY VAL TRP GLU SER ALA LYS ALA ASN ILE ARG
SEQRES 25 B 393 MET TYR LEU LEU LEU LYS GLU ARG ALA LYS ALA PHE ARG
SEQRES 26 B 393 ALA ASP PRO GLU VAL GLN GLU ALA LEU ALA ALA SER LYS
SEQRES 27 B 393 VAL ALA GLU LEU LYS THR PRO THR LEU ASN PRO GLY GLU
SEQRES 28 B 393 GLY TYR ALA GLU LEU LEU ALA ASP ARG SER ALA PHE GLU
SEQRES 29 B 393 ASP TYR ASP ALA ASP ALA VAL GLY ALA LYS GLY PHE GLY
SEQRES 30 B 393 PHE VAL LYS LEU ASN GLN LEU ALA ILE GLU HIS LEU LEU
SEQRES 31 B 393 GLY ALA ARG
SEQRES 1 C 393 SER VAL GLN ALA THR ARG GLU ASP LYS PHE SER PHE GLY
SEQRES 2 C 393 LEU TRP THR VAL GLY TRP GLN ALA ARG ASP ALA PHE GLY
SEQRES 3 C 393 ASP ALA THR ARG THR ALA LEU ASP PRO VAL GLU ALA VAL
SEQRES 4 C 393 HIS LYS LEU ALA GLU ILE GLY ALA TYR GLY ILE THR PHE
SEQRES 5 C 393 HIS ASP ASP ASP LEU VAL PRO PHE GLY SER ASP ALA GLN
SEQRES 6 C 393 THR ARG ASP GLY ILE ILE ALA GLY PHE LYS LYS ALA LEU
SEQRES 7 C 393 ASP GLU THR GLY LEU ILE VAL PRO MET VAL THR THR ASN
SEQRES 8 C 393 LEU PHE THR HIS PRO VAL PHE LYS ASP GLY GLY PHE THR
SEQRES 9 C 393 SER ASN ASP ARG SER VAL ARG ARG TYR ALA ILE ARG LYS
SEQRES 10 C 393 VAL LEU ARG GLN MET ASP LEU GLY ALA GLU LEU GLY ALA
SEQRES 11 C 393 LYS THR LEU VAL LEU TRP GLY GLY ARG GLU GLY ALA GLU
SEQRES 12 C 393 TYR ASP SER ALA LYS ASP VAL SER ALA ALA LEU ASP ARG
SEQRES 13 C 393 TYR ARG GLU ALA LEU ASN LEU LEU ALA GLN TYR SER GLU
SEQRES 14 C 393 ASP ARG GLY TYR GLY LEU ARG PHE ALA ILE GLN PRO LYS
SEQRES 15 C 393 PRO ASN GLU PRO ARG GLY ASP ILE LEU LEU PRO THR ALA
SEQRES 16 C 393 GLY HIS ALA ILE ALA PHE VAL GLN GLU LEU GLU ARG PRO
SEQRES 17 C 393 GLU LEU PHE GLY ILE ASN PRO GLU THR GLY HIS GLU GLN
SEQRES 18 C 393 MET SER ASN LEU ASN PHE THR GLN GLY ILE ALA GLN ALA
SEQRES 19 C 393 LEU TRP HIS LYS LYS LEU PHE HIS ILE ASP LEU ASN GLY
SEQRES 20 C 393 GLN HIS GLY PRO LYS PHE ASP GLN ASP LEU VAL PHE GLY
SEQRES 21 C 393 HIS GLY ASP LEU LEU ASN ALA PHE SER LEU VAL ASP LEU
SEQRES 22 C 393 LEU GLU ASN GLY PRO ASP GLY ALA PRO ALA TYR ASP GLY
SEQRES 23 C 393 PRO ARG HIS PHE ASP TYR LYS PRO SER ARG THR GLU ASP
SEQRES 24 C 393 TYR ASP GLY VAL TRP GLU SER ALA LYS ALA ASN ILE ARG
SEQRES 25 C 393 MET TYR LEU LEU LEU LYS GLU ARG ALA LYS ALA PHE ARG
SEQRES 26 C 393 ALA ASP PRO GLU VAL GLN GLU ALA LEU ALA ALA SER LYS
SEQRES 27 C 393 VAL ALA GLU LEU LYS THR PRO THR LEU ASN PRO GLY GLU
SEQRES 28 C 393 GLY TYR ALA GLU LEU LEU ALA ASP ARG SER ALA PHE GLU
SEQRES 29 C 393 ASP TYR ASP ALA ASP ALA VAL GLY ALA LYS GLY PHE GLY
SEQRES 30 C 393 PHE VAL LYS LEU ASN GLN LEU ALA ILE GLU HIS LEU LEU
SEQRES 31 C 393 GLY ALA ARG
SEQRES 1 D 393 SER VAL GLN ALA THR ARG GLU ASP LYS PHE SER PHE GLY
SEQRES 2 D 393 LEU TRP THR VAL GLY TRP GLN ALA ARG ASP ALA PHE GLY
SEQRES 3 D 393 ASP ALA THR ARG THR ALA LEU ASP PRO VAL GLU ALA VAL
SEQRES 4 D 393 HIS LYS LEU ALA GLU ILE GLY ALA TYR GLY ILE THR PHE
SEQRES 5 D 393 HIS ASP ASP ASP LEU VAL PRO PHE GLY SER ASP ALA GLN
SEQRES 6 D 393 THR ARG ASP GLY ILE ILE ALA GLY PHE LYS LYS ALA LEU
SEQRES 7 D 393 ASP GLU THR GLY LEU ILE VAL PRO MET VAL THR THR ASN
SEQRES 8 D 393 LEU PHE THR HIS PRO VAL PHE LYS ASP GLY GLY PHE THR
SEQRES 9 D 393 SER ASN ASP ARG SER VAL ARG ARG TYR ALA ILE ARG LYS
SEQRES 10 D 393 VAL LEU ARG GLN MET ASP LEU GLY ALA GLU LEU GLY ALA
SEQRES 11 D 393 LYS THR LEU VAL LEU TRP GLY GLY ARG GLU GLY ALA GLU
SEQRES 12 D 393 TYR ASP SER ALA LYS ASP VAL SER ALA ALA LEU ASP ARG
SEQRES 13 D 393 TYR ARG GLU ALA LEU ASN LEU LEU ALA GLN TYR SER GLU
SEQRES 14 D 393 ASP ARG GLY TYR GLY LEU ARG PHE ALA ILE GLN PRO LYS
SEQRES 15 D 393 PRO ASN GLU PRO ARG GLY ASP ILE LEU LEU PRO THR ALA
SEQRES 16 D 393 GLY HIS ALA ILE ALA PHE VAL GLN GLU LEU GLU ARG PRO
SEQRES 17 D 393 GLU LEU PHE GLY ILE ASN PRO GLU THR GLY HIS GLU GLN
SEQRES 18 D 393 MET SER ASN LEU ASN PHE THR GLN GLY ILE ALA GLN ALA
SEQRES 19 D 393 LEU TRP HIS LYS LYS LEU PHE HIS ILE ASP LEU ASN GLY
SEQRES 20 D 393 GLN HIS GLY PRO LYS PHE ASP GLN ASP LEU VAL PHE GLY
SEQRES 21 D 393 HIS GLY ASP LEU LEU ASN ALA PHE SER LEU VAL ASP LEU
SEQRES 22 D 393 LEU GLU ASN GLY PRO ASP GLY ALA PRO ALA TYR ASP GLY
SEQRES 23 D 393 PRO ARG HIS PHE ASP TYR LYS PRO SER ARG THR GLU ASP
SEQRES 24 D 393 TYR ASP GLY VAL TRP GLU SER ALA LYS ALA ASN ILE ARG
SEQRES 25 D 393 MET TYR LEU LEU LEU LYS GLU ARG ALA LYS ALA PHE ARG
SEQRES 26 D 393 ALA ASP PRO GLU VAL GLN GLU ALA LEU ALA ALA SER LYS
SEQRES 27 D 393 VAL ALA GLU LEU LYS THR PRO THR LEU ASN PRO GLY GLU
SEQRES 28 D 393 GLY TYR ALA GLU LEU LEU ALA ASP ARG SER ALA PHE GLU
SEQRES 29 D 393 ASP TYR ASP ALA ASP ALA VAL GLY ALA LYS GLY PHE GLY
SEQRES 30 D 393 PHE VAL LYS LEU ASN GLN LEU ALA ILE GLU HIS LEU LEU
SEQRES 31 D 393 GLY ALA ARG
FORMUL 5 HOH *904(H2 O)
HELIX 1 1 THR A 6 ASP A 9 5 4
HELIX 2 2 LEU A 15 GLY A 19 1 5
HELIX 3 3 ASP A 35 GLY A 47 1 13
HELIX 4 4 HIS A 54 VAL A 59 1 6
HELIX 5 5 ASP A 64 GLY A 83 1 20
HELIX 6 6 HIS A 96 LYS A 100 5 5
HELIX 7 7 ASP A 108 LEU A 129 1 22
HELIX 8 8 TYR A 145 LYS A 149 5 5
HELIX 9 9 ASP A 150 GLY A 173 1 24
HELIX 10 10 THR A 195 GLN A 204 1 10
HELIX 11 11 ARG A 208 GLU A 210 5 3
HELIX 12 12 GLU A 217 MET A 223 1 7
HELIX 13 13 ASN A 227 LYS A 239 1 13
HELIX 14 14 ASP A 264 ASN A 277 1 14
HELIX 15 15 ASP A 300 ASP A 328 1 29
HELIX 16 16 ASP A 328 SER A 338 1 11
HELIX 17 17 LYS A 339 THR A 345 5 7
HELIX 18 18 GLY A 353 ASP A 360 1 8
HELIX 19 19 ARG A 361 PHE A 364 5 4
HELIX 20 20 ASP A 368 ALA A 374 1 7
HELIX 21 21 GLY A 378 LEU A 391 1 14
HELIX 22 22 THR B 6 ASP B 9 5 4
HELIX 23 23 LEU B 15 GLY B 19 1 5
HELIX 24 24 ASP B 35 GLY B 47 1 13
HELIX 25 25 HIS B 54 VAL B 59 1 6
HELIX 26 26 ASP B 64 GLY B 83 1 20
HELIX 27 27 HIS B 96 LYS B 100 5 5
HELIX 28 28 ASP B 108 GLY B 130 1 23
HELIX 29 29 TYR B 145 LYS B 149 5 5
HELIX 30 30 ASP B 150 GLY B 173 1 24
HELIX 31 31 THR B 195 GLN B 204 1 10
HELIX 32 32 ARG B 208 GLU B 210 5 3
HELIX 33 33 GLU B 217 MET B 223 1 7
HELIX 34 34 ASN B 227 LYS B 239 1 13
HELIX 35 35 ASP B 264 ASN B 277 1 14
HELIX 36 36 ASP B 300 ASP B 328 1 29
HELIX 37 37 ASP B 328 LYS B 339 1 12
HELIX 38 38 VAL B 340 THR B 345 5 6
HELIX 39 39 GLY B 353 ASP B 360 1 8
HELIX 40 40 ARG B 361 PHE B 364 5 4
HELIX 41 41 ASP B 368 ALA B 374 1 7
HELIX 42 42 GLY B 378 LEU B 391 1 14
HELIX 43 43 THR C 6 ASP C 9 5 4
HELIX 44 44 LEU C 15 GLY C 19 1 5
HELIX 45 45 ASP C 35 GLY C 47 1 13
HELIX 46 46 HIS C 54 VAL C 59 1 6
HELIX 47 47 ASP C 64 GLY C 83 1 20
HELIX 48 48 HIS C 96 LYS C 100 5 5
HELIX 49 49 ASP C 108 GLY C 130 1 23
HELIX 50 50 TYR C 145 LYS C 149 5 5
HELIX 51 51 ASP C 150 GLY C 173 1 24
HELIX 52 52 THR C 195 GLN C 204 1 10
HELIX 53 53 ARG C 208 GLU C 210 5 3
HELIX 54 54 GLU C 217 MET C 223 1 7
HELIX 55 55 ASN C 227 HIS C 238 1 12
HELIX 56 56 ASP C 264 ASN C 277 1 14
HELIX 57 57 ASP C 300 ASP C 328 1 29
HELIX 58 58 ASP C 328 SER C 338 1 11
HELIX 59 59 LYS C 339 THR C 345 5 7
HELIX 60 60 GLY C 353 ASP C 360 1 8
HELIX 61 61 ARG C 361 PHE C 364 5 4
HELIX 62 62 ASP C 368 GLY C 373 1 6
HELIX 63 63 GLY C 378 LEU C 391 1 14
HELIX 64 64 THR D 6 ASP D 9 5 4
HELIX 65 65 LEU D 15 GLY D 19 1 5
HELIX 66 66 ASP D 35 GLY D 47 1 13
HELIX 67 67 HIS D 54 VAL D 59 1 6
HELIX 68 68 ASP D 64 GLY D 83 1 20
HELIX 69 69 HIS D 96 LYS D 100 5 5
HELIX 70 70 ASP D 108 LEU D 129 1 22
HELIX 71 71 TYR D 145 LYS D 149 5 5
HELIX 72 72 ASP D 150 GLY D 173 1 24
HELIX 73 73 THR D 195 GLN D 204 1 10
HELIX 74 74 ARG D 208 GLU D 210 5 3
HELIX 75 75 GLU D 217 MET D 223 1 7
HELIX 76 76 ASN D 227 LYS D 239 1 13
HELIX 77 77 ASP D 264 ASN D 277 1 14
HELIX 78 78 ASP D 300 ALA D 327 1 28
HELIX 79 79 ASP D 328 LYS D 339 1 12
HELIX 80 80 VAL D 340 THR D 345 5 6
HELIX 81 81 GLY D 353 ASP D 360 1 8
HELIX 82 82 ARG D 361 PHE D 364 5 4
HELIX 83 83 ASP D 368 ALA D 374 1 7
HELIX 84 84 GLY D 378 LEU D 391 1 14
SHEET 1 A 4 GLY A 50 THR A 52 0
SHEET 2 A 4 PHE A 11 GLY A 14 1 O PHE A 11 N GLY A 50
SHEET 3 A 4 ARG A 289 PHE A 291 1 O ARG A 289 N SER A 12
SHEET 4 A 4 ASP A 245 LEU A 246 1 N LEU A 246 O HIS A 290
SHEET 1 B 4 MET A 88 THR A 90 0
SHEET 2 B 4 THR A 133 TRP A 137 1 O THR A 133 N VAL A 89
SHEET 3 B 4 ARG A 177 GLN A 181 1 O ARG A 177 N LEU A 134
SHEET 4 B 4 PHE A 212 ILE A 214 1 N GLY A 213 O PHE A 178
SHEET 1 C 2 GLY A 142 ALA A 143 0
SHEET 2 C 2 ASP A 190 ILE A 191 -1 O ASP A 190 N ALA A 143
SHEET 1 D 4 GLY B 50 THR B 52 0
SHEET 2 D 4 PHE B 11 GLY B 14 1 O PHE B 11 N GLY B 50
SHEET 3 D 4 ARG B 289 PHE B 291 1 O ARG B 289 N SER B 12
SHEET 4 D 4 ILE B 244 LEU B 246 1 O ILE B 244 N HIS B 290
SHEET 1 E 4 MET B 88 THR B 90 0
SHEET 2 E 4 THR B 133 TRP B 137 1 O THR B 133 N VAL B 89
SHEET 3 E 4 ARG B 177 GLN B 181 1 O ARG B 177 N LEU B 134
SHEET 4 E 4 PHE B 212 ILE B 214 1 N GLY B 213 O PHE B 178
SHEET 1 F 2 GLY B 142 ALA B 143 0
SHEET 2 F 2 ASP B 190 ILE B 191 -1 O ASP B 190 N ALA B 143
SHEET 1 G 4 GLY C 50 THR C 52 0
SHEET 2 G 4 PHE C 11 GLY C 14 1 O PHE C 11 N GLY C 50
SHEET 3 G 4 ARG C 289 PHE C 291 1 O ARG C 289 N SER C 12
SHEET 4 G 4 ASP C 245 LEU C 246 1 N LEU C 246 O HIS C 290
SHEET 1 H 4 MET C 88 THR C 90 0
SHEET 2 H 4 THR C 133 TRP C 137 1 O THR C 133 N VAL C 89
SHEET 3 H 4 ARG C 177 GLN C 181 1 O ARG C 177 N LEU C 134
SHEET 4 H 4 PHE C 212 ILE C 214 1 N GLY C 213 O PHE C 178
SHEET 1 I 2 GLY C 142 ALA C 143 0
SHEET 2 I 2 ASP C 190 ILE C 191 -1 O ASP C 190 N ALA C 143
SHEET 1 J 4 GLY D 50 THR D 52 0
SHEET 2 J 4 PHE D 11 GLY D 14 1 O PHE D 11 N GLY D 50
SHEET 3 J 4 ARG D 289 PHE D 291 1 O ARG D 289 N SER D 12
SHEET 4 J 4 ASP D 245 LEU D 246 1 N LEU D 246 O HIS D 290
SHEET 1 K 4 MET D 88 THR D 90 0
SHEET 2 K 4 THR D 133 LEU D 136 1 O THR D 133 N VAL D 89
SHEET 3 K 4 ARG D 177 ILE D 180 1 O ARG D 177 N LEU D 134
SHEET 4 K 4 PHE D 212 ILE D 214 1 N GLY D 213 O PHE D 178
SHEET 1 L 2 GLY D 142 ALA D 143 0
SHEET 2 L 2 ASP D 190 ILE D 191 -1 O ASP D 190 N ALA D 143
CISPEP 1 GLU A 186 PRO A 187 0 3.55
CISPEP 2 GLU B 186 PRO B 187 0 3.96
CISPEP 3 GLU C 186 PRO C 187 0 3.73
CISPEP 4 GLU D 186 PRO D 187 0 5.63
CRYST1 143.450 143.450 231.500 90.00 90.00 120.00 P 32 2 1 24
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 0.006971 0.004025 0.000000 0.00000
SCALE2 0.000000 0.008049 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004320 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
