HEADER HYDROLASE 14-NOV-03 1RH9
TITLE FAMILY GH5 ENDO-BETA-MANNANASE FROM LYCOPERSICON ESCULENTUM (TOMATO)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-BETA-MANNANASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 27-399;
COMPND 5 EC: 3.2.1.78;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SOLANUM LYCOPERSICUM;
SOURCE 3 ORGANISM_TAXID: 4081;
SOURCE 4 GENE: LEMAN4A;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH5-ALPHA;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMAL-C2X
KEYWDS ENDO-BETA-MANNASE, RETAINING, GLYCOSIDE HYDROLASE FAMILY 5, MANNAN,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.J.OAKLEY,R.BOURGAULT,J.D.BEWLEY,M.C.J.WILCE
REVDAT 4 25-OCT-23 1RH9 1 REMARK
REVDAT 3 24-FEB-09 1RH9 1 VERSN
REVDAT 2 26-APR-05 1RH9 1 JRNL
REVDAT 1 19-APR-05 1RH9 0
JRNL AUTH R.BOURGAULT,A.J.OAKLEY,J.D.BEWLEY,M.C.WILCE
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF (1,4)-BETA-D-MANNAN
JRNL TITL 2 MANNANOHYDROLASE FROM TOMATO FRUIT.
JRNL REF PROTEIN SCI. V. 14 1233 2005
JRNL REFN ISSN 0961-8368
JRNL PMID 15840830
JRNL DOI 10.1110/PS.041260905
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.19
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : -1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 53236
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2853
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3906
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE SET COUNT : 200
REMARK 3 BIN FREE R VALUE : 0.3210
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2971
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) : 18.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.43000
REMARK 3 B22 (A**2) : -1.22000
REMARK 3 B33 (A**2) : 0.79000
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): 0.084
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.081
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.068
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.977
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.962
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3240 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2801 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4413 ; 1.224 ; 1.927
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6564 ; 0.781 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 405 ; 6.423 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 463 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3694 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 687 ; 0.005 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 698 ; 0.221 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3379 ; 0.237 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1767 ; 0.103 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 299 ; 0.150 ; 0.200
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): 16 ; 0.166 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 82 ; 0.222 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 36 ; 0.228 ; 0.200
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): 1957 ; 0.591 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3179 ; 1.084 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1283 ; 1.606 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1234 ; 2.571 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 1RH9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020745.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAR-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.900
REMARK 200 MONOCHROMATOR : BEAMLINE OPTICS
REMARK 200 OPTICS : BEAMLINE OPTICS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56178
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 54.233
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.74300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1QNP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 0.1M NA CITRATE, 0.2M
REMARK 280 NH4 ACETATE, PH 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
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 29.77000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.50300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.26050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.50300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.77000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.26050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 300 REMARK: THE ASYMMETRIC UNIT CONTAINS THE BIOLOGICAL ASSEMBLY (A
REMARK 300 MONOMER).
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 PHE A 27
REMARK 465 SER A 28
REMARK 465 ASN A 29
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 ASN A 31 12.03 20.36
REMARK 500 ASN A 31 12.03 -35.64
REMARK 500 ALA A 54 83.61 -151.16
REMARK 500 ALA A 89 36.32 -99.51
REMARK 500 LEU A 98 -64.75 -93.59
REMARK 500 ASP A 136 171.04 81.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BQC RELATED DB: PDB
REMARK 900 FAMILY GH5 MANNANASE FROM THERMOMONOSPORA FUSCA
REMARK 900 RELATED ID: 1QNP RELATED DB: PDB
REMARK 900 FAMILY GH5 MANNANASE FROM TRICHODERMA REESEI
DBREF 1RH9 A 27 399 UNP Q93WT4 Q93WT4_LYCES 27 399
SEQRES 1 A 373 PHE SER ASN ASN ASN PHE VAL TYR THR ASP GLY THR HIS
SEQRES 2 A 373 PHE ALA LEU ASN GLY LYS SER LEU TYR ILE ASN GLY PHE
SEQRES 3 A 373 ASN ALA TYR TRP LEU MET TYR ILE ALA TYR ASP PRO SER
SEQRES 4 A 373 THR ARG ILE LYS VAL THR ASN THR PHE GLN GLN ALA SER
SEQRES 5 A 373 LYS TYR LYS MET ASN VAL ALA ARG THR TRP ALA PHE SER
SEQRES 6 A 373 HIS GLY GLY SER ARG PRO LEU GLN SER ALA PRO GLY VAL
SEQRES 7 A 373 TYR ASN GLU GLN MET PHE GLN GLY LEU ASP PHE VAL ILE
SEQRES 8 A 373 SER GLU ALA LYS LYS TYR GLY ILE HIS LEU ILE MET SER
SEQRES 9 A 373 LEU VAL ASN ASN TRP ASP ALA PHE GLY GLY LYS LYS GLN
SEQRES 10 A 373 TYR VAL GLU TRP ALA VAL GLN ARG GLY GLN LYS LEU THR
SEQRES 11 A 373 SER ASP ASP ASP PHE PHE THR ASN PRO MET VAL LYS GLY
SEQRES 12 A 373 PHE TYR LYS ASN ASN VAL LYS VAL VAL LEU THR ARG VAL
SEQRES 13 A 373 ASN THR ILE THR LYS VAL ALA TYR LYS ASP ASP PRO THR
SEQRES 14 A 373 ILE LEU SER TRP GLU LEU ILE ASN GLU PRO ARG CYS PRO
SEQRES 15 A 373 SER ASP LEU SER GLY LYS THR PHE GLN ASN TRP VAL LEU
SEQRES 16 A 373 GLU MET ALA GLY TYR LEU LYS SER ILE ASP SER ASN HIS
SEQRES 17 A 373 LEU LEU GLU ILE GLY LEU GLU GLY PHE TYR GLY ASN ASP
SEQRES 18 A 373 MET ARG GLN TYR ASN PRO ASN SER TYR ILE PHE GLY THR
SEQRES 19 A 373 ASN PHE ILE SER ASN ASN GLN VAL GLN GLY ILE ASP PHE
SEQRES 20 A 373 THR THR ILE HIS MET TYR PRO ASN GLN TRP LEU PRO GLY
SEQRES 21 A 373 LEU THR GLN GLU ALA GLN ASP LYS TRP ALA SER GLN TRP
SEQRES 22 A 373 ILE GLN VAL HIS ILE ASP ASP SER LYS MET LEU LYS LYS
SEQRES 23 A 373 PRO LEU LEU ILE ALA GLU PHE GLY LYS SER THR LYS THR
SEQRES 24 A 373 PRO GLY TYR THR VAL ALA LYS ARG ASP ASN TYR PHE GLU
SEQRES 25 A 373 LYS ILE TYR GLY THR ILE PHE ASN CYS ALA LYS SER GLY
SEQRES 26 A 373 GLY PRO CYS GLY GLY GLY LEU PHE TRP GLN VAL LEU GLY
SEQRES 27 A 373 GLN GLY MET SER SER PHE ASP ASP GLY TYR GLN VAL VAL
SEQRES 28 A 373 LEU GLN GLU SER PRO SER THR SER ARG VAL ILE LEU LEU
SEQRES 29 A 373 GLN SER LEU ARG LEU SER LYS LEU SER
HELIX 1 1 TRP A 56 ASP A 63 1 8
HELIX 2 2 ARG A 67 TYR A 80 1 14
HELIX 3 3 ASN A 106 TYR A 123 1 18
HELIX 4 4 GLY A 140 ARG A 151 1 12
HELIX 5 5 SER A 157 THR A 163 5 7
HELIX 6 6 ASN A 164 ARG A 181 1 18
HELIX 7 7 ALA A 189 ASP A 193 5 5
HELIX 8 8 GLY A 213 ASP A 231 1 19
HELIX 9 9 GLY A 245 TYR A 256 5 12
HELIX 10 10 ASN A 261 GLN A 267 1 7
HELIX 11 11 TYR A 279 LEU A 284 1 6
HELIX 12 12 THR A 288 LYS A 311 1 24
HELIX 13 13 THR A 329 SER A 350 1 22
HELIX 14 14 MET A 367 ASP A 371 5 5
HELIX 15 15 VAL A 377 GLU A 380 5 4
HELIX 16 16 SER A 381 SER A 396 1 16
SHEET 1 A 3 TYR A 34 ASP A 36 0
SHEET 2 A 3 HIS A 39 LEU A 42 -1 O ALA A 41 N TYR A 34
SHEET 3 A 3 LYS A 45 LEU A 47 -1 O LYS A 45 N LEU A 42
SHEET 1 B 8 LEU A 235 GLU A 237 0
SHEET 2 B 8 ILE A 196 GLU A 200 1 N TRP A 199 O LEU A 235
SHEET 3 B 8 HIS A 126 SER A 130 1 N LEU A 127 O LEU A 197
SHEET 4 B 8 VAL A 84 TRP A 88 1 N THR A 87 O SER A 130
SHEET 5 B 8 ILE A 49 ASN A 53 1 N PHE A 52 O ARG A 86
SHEET 6 B 8 CYS A 354 PHE A 359 1 O GLY A 355 N ILE A 49
SHEET 7 B 8 LEU A 314 GLU A 318 1 N LEU A 314 O GLY A 355
SHEET 8 B 8 THR A 274 HIS A 277 1 N THR A 274 O LEU A 315
SHEET 1 C 2 GLN A 99 ALA A 101 0
SHEET 2 C 2 VAL A 104 TYR A 105 -1 O VAL A 104 N ALA A 101
SSBOND 1 CYS A 347 CYS A 354 1555 1555 2.82
CISPEP 1 TRP A 360 GLN A 361 0 -0.40
CRYST1 59.540 74.521 79.006 90.00 90.00 90.00 P 21 21 21 4
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 0.016795 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013419 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012657 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
