HEADER ISOMERASE 10-JUN-98 1BHW
TITLE LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF XYLOSE ISOMERASE FROM
TITLE 2 MASC DATA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: XYLOSE ISOMERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 5.3.1.5;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACTINOPLANES MISSOURIENSIS;
SOURCE 3 ORGANISM_TAXID: 1866;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: K527;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PMA5-I
KEYWDS ISOMERASE, MASC, MULTIWAVELENGTH ANOMALOUS SOLVENT CONTRAST
EXPDTA X-RAY DIFFRACTION
AUTHOR M.RAMIN,W.SHEPARD,R.FOURME,R.KAHN
REVDAT 5 02-AUG-23 1BHW 1 SEQADV
REVDAT 4 24-FEB-09 1BHW 1 VERSN
REVDAT 3 01-APR-03 1BHW 1 JRNL
REVDAT 2 18-NOV-98 1BHW 1 SOURCE COMPND REMARK KEYWDS
REVDAT 2 2 1 HEADER
REVDAT 1 04-NOV-98 1BHW 0
JRNL AUTH M.RAMIN,W.SHEPARD,R.FOURME,R.KAHN
JRNL TITL MULTIWAVELENGTH ANOMALOUS SOLVENT CONTRAST (MASC):
JRNL TITL 2 DERIVATION OF ENVELOPE STRUCTURE-FACTOR AMPLITUDES AND
JRNL TITL 3 COMPARISON WITH MODEL VALUES.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 55 157 1999
JRNL REFN ISSN 0907-4449
JRNL PMID 10089406
JRNL DOI 10.1107/S090744499800626X
REMARK 1
REMARK 1 REFERENCE 1
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 A MODEL OF XYLOSE ISOMERASE
REMARK 1 TITL 2 FROM ACTINOPLANES MISSOURIENSIS
REMARK 1 REF PROTEINS V. 4 165 1988
REMARK 1 REFN ISSN 0887-3585
REMARK 2
REMARK 2 RESOLUTION. 4.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 4.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
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 SET) : 0.315
REMARK 3 FREE R VALUE : 0.321
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12248
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
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 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : 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 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BHW 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_1000171776.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JUN-95
REMARK 200 TEMPERATURE (KELVIN) : 124
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (AGROVATA, SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19684
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.120
REMARK 200 RESOLUTION RANGE LOW (A) : 105.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.03700
REMARK 200 R SYM (I) : 0.03700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.04100
REMARK 200 R SYM FOR SHELL (I) : 0.04100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 16.10
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT,
REMARK 200 RIGID BODY REFINEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: 1XIN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM AMMONIUM
REMARK 280 SULPHATE
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 151.65333
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 75.82667
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 75.82667
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 151.65333
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: 32180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -113.0 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 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 OD1 ASP C 280 N GLY C 281 1.17
REMARK 500 NE2 GLN C 66 N THR C 67 1.23
REMARK 500 OE1 GLN B 204 OE1 GLN D 204 1.33
REMARK 500 OE1 GLN A 204 OE1 GLN C 204 1.44
REMARK 500 OD1 ASP D 280 N GLY D 281 1.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLN A 4 CB GLN A 4 CG -0.975
REMARK 500 GLN A 4 CG GLN A 4 CD -1.043
REMARK 500 GLN A 4 CD GLN A 4 OE1 -0.801
REMARK 500 GLN A 4 CD GLN A 4 NE2 -0.457
REMARK 500 GLN A 66 CB GLN A 66 CG -1.065
REMARK 500 GLN A 66 CG GLN A 66 CD -1.072
REMARK 500 GLN A 66 CD GLN A 66 OE1 -0.803
REMARK 500 GLN A 66 CD GLN A 66 NE2 -0.459
REMARK 500 ASP A 280 CB ASP A 280 CG -0.797
REMARK 500 ASP A 280 CG ASP A 280 OD2 0.144
REMARK 500 ASP A 328 C PRO A 329 N -0.136
REMARK 500 GLN B 4 CB GLN B 4 CG -0.973
REMARK 500 GLN B 4 CG GLN B 4 CD -0.893
REMARK 500 GLN B 4 CD GLN B 4 OE1 -0.802
REMARK 500 GLN B 4 CD GLN B 4 NE2 -0.458
REMARK 500 GLN B 66 CB GLN B 66 CG -1.044
REMARK 500 GLN B 66 CG GLN B 66 CD -0.893
REMARK 500 GLN B 66 CD GLN B 66 OE1 -0.175
REMARK 500 GLN B 66 CD GLN B 66 NE2 0.797
REMARK 500 ASP B 280 CB ASP B 280 CG -0.640
REMARK 500 ASP B 280 CG ASP B 280 OD2 -0.499
REMARK 500 ASP B 328 C PRO B 329 N -0.133
REMARK 500 GLN C 4 CB GLN C 4 CG -0.800
REMARK 500 GLN C 4 CG GLN C 4 CD -1.073
REMARK 500 GLN C 4 CD GLN C 4 OE1 -0.802
REMARK 500 GLN C 4 CD GLN C 4 NE2 -0.457
REMARK 500 GLN C 66 CB GLN C 66 CG -1.084
REMARK 500 GLN C 66 CG GLN C 66 CD -1.072
REMARK 500 GLN C 66 CD GLN C 66 OE1 -0.802
REMARK 500 GLN C 66 CD GLN C 66 NE2 -0.294
REMARK 500 ASP C 280 CB ASP C 280 CG -0.619
REMARK 500 ASP C 280 CG ASP C 280 OD1 0.351
REMARK 500 ASP C 280 CG ASP C 280 OD2 -0.420
REMARK 500 ASP C 328 C PRO C 329 N -0.191
REMARK 500 GLN D 4 CB GLN D 4 CG -1.034
REMARK 500 GLN D 4 CG GLN D 4 CD -1.099
REMARK 500 GLN D 4 CD GLN D 4 OE1 -0.174
REMARK 500 GLN D 4 CD GLN D 4 NE2 -0.242
REMARK 500 GLN D 66 CB GLN D 66 CG -0.916
REMARK 500 GLN D 66 CG GLN D 66 CD -0.893
REMARK 500 GLN D 66 CD GLN D 66 OE1 -0.406
REMARK 500 GLN D 66 CD GLN D 66 NE2 -0.460
REMARK 500 ASP D 280 CB ASP D 280 CG -0.888
REMARK 500 ASP D 280 CG ASP D 280 OD1 0.304
REMARK 500 ASP D 280 CG ASP D 280 OD2 -0.534
REMARK 500 ASP D 328 C PRO D 329 N -0.211
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 GLN A 4 CA - CB - CG ANGL. DEV. = -79.1 DEGREES
REMARK 500 GLN A 4 CB - CG - CD ANGL. DEV. = 52.7 DEGREES
REMARK 500 GLN A 4 OE1 - CD - NE2 ANGL. DEV. = 121.8 DEGREES
REMARK 500 GLN A 4 CG - CD - OE1 ANGL. DEV. = 53.4 DEGREES
REMARK 500 GLN A 4 CG - CD - NE2 ANGL. DEV. = 58.2 DEGREES
REMARK 500 ARG A 7 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP A 24 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG A 31 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ASP A 55 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 55 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ASP A 57 CB - CG - OD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 GLN A 66 CA - CB - CG ANGL. DEV. = -95.4 DEGREES
REMARK 500 GLN A 66 CB - CG - CD ANGL. DEV. = 56.3 DEGREES
REMARK 500 GLN A 66 OE1 - CD - NE2 ANGL. DEV. = 121.8 DEGREES
REMARK 500 GLN A 66 CG - CD - OE1 ANGL. DEV. = 58.3 DEGREES
REMARK 500 GLN A 66 CG - CD - NE2 ANGL. DEV. = 63.2 DEGREES
REMARK 500 ARG A 68 CD - NE - CZ ANGL. DEV. = 9.7 DEGREES
REMARK 500 ARG A 68 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ASP A 80 CA - CB - CG ANGL. DEV. = -19.2 DEGREES
REMARK 500 ASP A 80 OD1 - CG - OD2 ANGL. DEV. = 14.0 DEGREES
REMARK 500 ASP A 80 CB - CG - OD1 ANGL. DEV. = -10.3 DEGREES
REMARK 500 ARG A 109 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 112 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 117 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 117 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 121 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 121 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ASP A 124 CB - CG - OD1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 ASP A 146 CB - CG - OD1 ANGL. DEV. = 8.3 DEGREES
REMARK 500 ASP A 150 CB - CG - OD1 ANGL. DEV. = 8.5 DEGREES
REMARK 500 TYR A 158 CB - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG A 172 CD - NE - CZ ANGL. DEV. = 12.5 DEGREES
REMARK 500 ARG A 172 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 172 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 GLU A 186 OE1 - CD - OE2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 ARG A 188 CD - NE - CZ ANGL. DEV. = 12.3 DEGREES
REMARK 500 ARG A 188 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 GLU A 205 OE1 - CD - OE2 ANGL. DEV. = -12.1 DEGREES
REMARK 500 GLU A 205 CG - CD - OE2 ANGL. DEV. = 13.3 DEGREES
REMARK 500 ASP A 273 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ASP A 280 CA - CB - CG ANGL. DEV. = 107.4 DEGREES
REMARK 500 ASP A 280 OD1 - CG - OD2 ANGL. DEV. = -84.2 DEGREES
REMARK 500 ASP A 280 CB - CG - OD1 ANGL. DEV. = -11.9 DEGREES
REMARK 500 ASP A 280 CB - CG - OD2 ANGL. DEV. = -31.7 DEGREES
REMARK 500 ARG A 297 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ASP A 300 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 313 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 GLU A 320 OE1 - CD - OE2 ANGL. DEV. = -8.6 DEGREES
REMARK 500 ARG A 321 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 213 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 -74.97 -81.15
REMARK 500 GLU A 186 106.26 75.70
REMARK 500 ASN A 247 -174.15 -171.70
REMARK 500 HIS A 250 72.58 -109.20
REMARK 500 PHE A 364 -74.87 -160.49
REMARK 500 THR B 17 -77.22 -79.29
REMARK 500 ALA B 22 36.78 73.64
REMARK 500 GLU B 186 107.54 70.73
REMARK 500 LEU B 193 61.42 67.67
REMARK 500 HIS B 250 73.32 -112.49
REMARK 500 PRO B 252 99.60 -67.12
REMARK 500 ASP B 280 46.30 70.97
REMARK 500 PHE B 364 -75.92 -155.29
REMARK 500 THR C 17 -73.10 -81.86
REMARK 500 GLU C 186 109.68 73.84
REMARK 500 LEU C 193 65.31 61.86
REMARK 500 ARG C 208 73.46 -119.47
REMARK 500 ASN C 247 -172.54 -171.05
REMARK 500 HIS C 250 73.09 -109.77
REMARK 500 LYS C 253 -177.52 -170.31
REMARK 500 PRO C 279 -72.84 -27.16
REMARK 500 ASP C 280 -93.48 -63.74
REMARK 500 ASP C 300 -167.55 -101.20
REMARK 500 PHE C 364 -68.01 -164.78
REMARK 500 THR D 17 -74.46 -81.13
REMARK 500 ASP D 24 -167.72 -104.01
REMARK 500 PHE D 94 -25.80 -140.16
REMARK 500 GLU D 186 105.66 75.41
REMARK 500 LEU D 193 63.24 60.04
REMARK 500 HIS D 250 78.39 -113.71
REMARK 500 LYS D 253 -179.84 -170.85
REMARK 500 PHE D 254 163.41 -49.61
REMARK 500 ASN D 277 56.71 -97.04
REMARK 500 ASP D 280 37.25 84.79
REMARK 500 PRO D 346 150.68 -49.83
REMARK 500 PHE D 364 -68.49 -160.33
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 A 23 0.10 SIDE CHAIN
REMARK 500 ASP A 280 0.18 SIDE CHAIN
REMARK 500 ARG B 172 0.14 SIDE CHAIN
REMARK 500 ARG C 172 0.12 SIDE CHAIN
REMARK 500 ARG D 208 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BHW A 2 394 UNP P12851 XYLA_ACTMI 1 393
DBREF 1BHW B 2 394 UNP P12851 XYLA_ACTMI 1 393
DBREF 1BHW C 2 394 UNP P12851 XYLA_ACTMI 1 393
DBREF 1BHW D 2 394 UNP P12851 XYLA_ACTMI 1 393
SEQADV 1BHW ASN A 220 UNP P12851 HIS 219 CONFLICT
SEQADV 1BHW ASN B 220 UNP P12851 HIS 219 CONFLICT
SEQADV 1BHW ASN C 220 UNP P12851 HIS 219 CONFLICT
SEQADV 1BHW ASN D 220 UNP P12851 HIS 219 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 GLU 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 ASN 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 GLU 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 ASN 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 GLU 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 ASN 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 GLU 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 ASN 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
HELIX 1 1 ARG A 7 ASP A 9 5 3
HELIX 2 2 LEU A 15 VAL A 18 1 4
HELIX 3 3 PRO A 36 ILE A 46 1 11
HELIX 4 4 ASP A 55 LEU A 58 1 4
HELIX 5 5 ALA A 65 THR A 82 1 18
HELIX 6 6 PRO A 97 PHE A 99 5 3
HELIX 7 7 ARG A 109 LEU A 129 1 21
HELIX 8 8 ASP A 146 ALA A 148 5 3
HELIX 9 9 VAL A 151 ASP A 171 1 21
HELIX 10 10 ALA A 196 GLU A 205 1 10
HELIX 11 11 PRO A 209 LEU A 211 5 3
HELIX 12 12 THR A 218 SER A 224 1 7
HELIX 13 13 PHE A 228 HIS A 238 1 11
HELIX 14 14 LEU A 265 GLU A 276 1 12
HELIX 15 15 TYR A 301 ALA A 327 1 27
HELIX 16 16 PRO A 329 ALA A 337 1 9
HELIX 17 17 VAL A 340 LYS A 344 5 5
HELIX 18 18 TYR A 354 ALA A 359 1 6
HELIX 19 19 ARG A 361 ALA A 363 5 3
HELIX 20 20 ALA A 369 ALA A 374 1 6
HELIX 21 21 PHE A 379 LEU A 390 1 12
HELIX 22 22 ARG B 7 ASP B 9 5 3
HELIX 23 23 LEU B 15 VAL B 18 1 4
HELIX 24 24 PRO B 36 ILE B 46 1 11
HELIX 25 25 ASP B 55 LEU B 58 1 4
HELIX 26 26 ALA B 65 THR B 82 1 18
HELIX 27 27 PRO B 97 PHE B 99 5 3
HELIX 28 28 ARG B 109 LEU B 129 1 21
HELIX 29 29 ASP B 146 ALA B 148 5 3
HELIX 30 30 VAL B 151 ARG B 172 1 22
HELIX 31 31 ALA B 196 GLU B 205 1 10
HELIX 32 32 PRO B 209 LEU B 211 5 3
HELIX 33 33 THR B 218 SER B 224 1 7
HELIX 34 34 PHE B 228 HIS B 238 1 11
HELIX 35 35 LEU B 265 GLU B 276 1 12
HELIX 36 36 TYR B 301 ALA B 327 1 27
HELIX 37 37 PRO B 329 SER B 338 1 10
HELIX 38 38 VAL B 340 LYS B 344 5 5
HELIX 39 39 TYR B 354 ALA B 359 1 6
HELIX 40 40 ARG B 361 ALA B 363 5 3
HELIX 41 41 ALA B 369 ALA B 374 1 6
HELIX 42 42 PHE B 379 LEU B 390 1 12
HELIX 43 43 ARG C 7 ASP C 9 5 3
HELIX 44 44 LEU C 15 VAL C 18 1 4
HELIX 45 45 PRO C 36 ILE C 46 1 11
HELIX 46 46 ASP C 55 LEU C 58 1 4
HELIX 47 47 ALA C 65 THR C 82 1 18
HELIX 48 48 PRO C 97 PHE C 99 5 3
HELIX 49 49 ARG C 109 LEU C 129 1 21
HELIX 50 50 ASP C 146 ALA C 148 5 3
HELIX 51 51 VAL C 151 ARG C 172 1 22
HELIX 52 52 ALA C 196 GLU C 205 1 10
HELIX 53 53 PRO C 209 LEU C 211 5 3
HELIX 54 54 THR C 218 SER C 224 1 7
HELIX 55 55 PHE C 228 TRP C 237 1 10
HELIX 56 56 LEU C 265 GLU C 276 1 12
HELIX 57 57 TYR C 301 ALA C 327 1 27
HELIX 58 58 PRO C 329 ALA C 337 1 9
HELIX 59 59 VAL C 340 LYS C 344 5 5
HELIX 60 60 TYR C 354 ALA C 359 1 6
HELIX 61 61 ARG C 361 ALA C 363 5 3
HELIX 62 62 ALA C 369 ALA C 374 1 6
HELIX 63 63 PHE C 379 LEU C 390 1 12
HELIX 64 64 ARG D 7 ASP D 9 5 3
HELIX 65 65 LEU D 15 VAL D 18 1 4
HELIX 66 66 PRO D 36 ILE D 46 1 11
HELIX 67 67 ASP D 55 LEU D 58 1 4
HELIX 68 68 ALA D 65 THR D 82 1 18
HELIX 69 69 PRO D 97 PHE D 99 5 3
HELIX 70 70 ARG D 109 LEU D 129 1 21
HELIX 71 71 ASP D 146 ALA D 148 5 3
HELIX 72 72 VAL D 151 ARG D 172 1 22
HELIX 73 73 ALA D 196 GLU D 205 1 10
HELIX 74 74 PRO D 209 LEU D 211 5 3
HELIX 75 75 THR D 218 SER D 224 1 7
HELIX 76 76 PHE D 228 HIS D 238 1 11
HELIX 77 77 LEU D 265 GLU D 276 1 12
HELIX 78 78 TYR D 301 ARG D 326 1 26
HELIX 79 79 PRO D 329 SER D 338 1 10
HELIX 80 80 ALA D 341 LYS D 344 5 4
HELIX 81 81 TYR D 354 ALA D 359 1 6
HELIX 82 82 ARG D 361 ALA D 363 5 3
HELIX 83 83 ALA D 369 GLY D 373 1 5
HELIX 84 84 PHE D 379 LEU D 390 1 12
SHEET 1 A 3 ARG A 289 PHE A 291 0
SHEET 2 A 3 PHE A 11 GLY A 14 1 N SER A 12 O ARG A 289
SHEET 3 A 3 GLY A 50 THR A 52 1 N GLY A 50 O PHE A 13
SHEET 1 B 5 MET A 88 THR A 90 0
SHEET 2 B 5 THR A 133 TRP A 137 1 N THR A 133 O VAL A 89
SHEET 3 B 5 ARG A 177 GLU A 181 1 N ARG A 177 O LEU A 134
SHEET 4 B 5 PHE A 212 GLU A 217 1 N GLY A 213 O PHE A 178
SHEET 5 B 5 LEU A 241 ASP A 245 1 N PHE A 242 O ILE A 214
SHEET 1 C 3 ARG B 289 PHE B 291 0
SHEET 2 C 3 PHE B 11 GLY B 14 1 N SER B 12 O ARG B 289
SHEET 3 C 3 GLY B 50 THR B 52 1 N GLY B 50 O PHE B 13
SHEET 1 D 5 MET B 88 THR B 90 0
SHEET 2 D 5 THR B 133 TRP B 137 1 N THR B 133 O VAL B 89
SHEET 3 D 5 ARG B 177 GLU B 181 1 N ARG B 177 O LEU B 134
SHEET 4 D 5 PHE B 212 GLU B 217 1 N GLY B 213 O PHE B 178
SHEET 5 D 5 LEU B 241 ASP B 245 1 N PHE B 242 O ILE B 214
SHEET 1 E 3 ARG C 289 PHE C 291 0
SHEET 2 E 3 PHE C 11 GLY C 14 1 N SER C 12 O ARG C 289
SHEET 3 E 3 GLY C 50 THR C 52 1 N GLY C 50 O PHE C 13
SHEET 1 F 5 MET C 88 THR C 90 0
SHEET 2 F 5 THR C 133 TRP C 137 1 N THR C 133 O VAL C 89
SHEET 3 F 5 ARG C 177 GLU C 181 1 N ARG C 177 O LEU C 134
SHEET 4 F 5 PHE C 212 GLU C 217 1 N GLY C 213 O PHE C 178
SHEET 5 F 5 LEU C 241 ASP C 245 1 N PHE C 242 O ILE C 214
SHEET 1 G 3 ARG D 289 PHE D 291 0
SHEET 2 G 3 PHE D 11 GLY D 14 1 N SER D 12 O ARG D 289
SHEET 3 G 3 GLY D 50 THR D 52 1 N GLY D 50 O PHE D 13
SHEET 1 H 5 MET D 88 THR D 90 0
SHEET 2 H 5 THR D 133 LEU D 136 1 N THR D 133 O VAL D 89
SHEET 3 H 5 ARG D 177 ILE D 180 1 N ARG D 177 O LEU D 134
SHEET 4 H 5 PHE D 212 GLU D 217 1 N GLY D 213 O PHE D 178
SHEET 5 H 5 LEU D 241 ASP D 245 1 N PHE D 242 O ILE D 214
CISPEP 1 GLU A 186 PRO A 187 0 3.64
CISPEP 2 GLU B 186 PRO B 187 0 3.26
CISPEP 3 GLU C 186 PRO C 187 0 3.35
CISPEP 4 GLU D 186 PRO D 187 0 4.20
CRYST1 141.910 141.910 227.480 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 0.007047 0.004068 0.000000 0.00000
SCALE2 0.000000 0.008137 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004396 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
