HEADER OXIDOREDUCTASE 25-OCT-13 4ND5
TITLE CRYSTAL STRUCTURE OF THE LACTATE DEHYDROGENASE FROM CRYPTOSPORIDIUM
TITLE 2 PARVUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LACTATE DEHYDROGENASE, ADJACENT GENE ENCODES PREDICTED
COMPND 3 MALATE DEHYDROGENASE;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 EC: 1.1.1.27;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRYPTOSPORIDIUM PARVUM;
SOURCE 3 ORGANISM_TAXID: 353152;
SOURCE 4 STRAIN: IOWA II;
SOURCE 5 GENE: CGD7_480, LDH1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS APOENZYME STRUCTURE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.CHATTOPADHYAY,W.J.COOK
REVDAT 4 20-SEP-23 4ND5 1 REMARK
REVDAT 3 17-JUL-19 4ND5 1 REMARK LINK
REVDAT 2 11-MAR-15 4ND5 1 JRNL
REVDAT 1 17-DEC-14 4ND5 0
SPRSDE 17-DEC-14 4ND5 2FRM
JRNL AUTH W.J.COOK,O.SENKOVICH,A.HERNANDEZ,H.SPEED,D.CHATTOPADHYAY
JRNL TITL BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF
JRNL TITL 2 CRYPTOSPORIDIUM PARVUM LACTATE DEHYDROGENASE.
JRNL REF INT.J.BIOL.MACROMOL. V. 74C 608 2014
JRNL REFN ISSN 0141-8130
JRNL PMID 25542170
JRNL DOI 10.1016/J.IJBIOMAC.2014.12.019
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.3
REMARK 3 NUMBER OF REFLECTIONS : 91538
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) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4880
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3948
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 54.24
REMARK 3 BIN R VALUE (WORKING SET) : 0.2920
REMARK 3 BIN FREE R VALUE SET COUNT : 191
REMARK 3 BIN FREE R VALUE : 0.3260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8905
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 194
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.37000
REMARK 3 B22 (A**2) : 1.37000
REMARK 3 B33 (A**2) : -4.44000
REMARK 3 B12 (A**2) : 1.37000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.177
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.138
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.294
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9049 ; 0.004 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8906 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12254 ; 0.844 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): 20507 ; 0.650 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1193 ; 4.607 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 333 ;35.918 ;25.435
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1544 ;11.179 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;14.519 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1463 ; 0.048 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10247 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1893 ; 0.001 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 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 : 1.20
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 4ND5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-OCT-13.
REMARK 100 THE DEPOSITION ID IS D_1000083052.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9998
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 100051
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 64.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.29400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: CNS
REMARK 200 STARTING MODEL: 2EWD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16.5% PEG 2000, 0.1 M TRIS-HCL, 0.08%
REMARK 280 B-D-GLYCOPYRANOSIDE, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 1 2
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+1/3
REMARK 290 5555 -X+Y,Y,-Z+2/3
REMARK 290 6555 X,X-Y,-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 -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 113.48000
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 56.74000
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 56.74000
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 113.48000
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 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL
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 BIOMT1 2 0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 56.74000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 14570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 272.98000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 113.48000
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 100
REMARK 465 ILE A 101
REMARK 465 PRO A 102
REMARK 465 GLY A 103
REMARK 465 ARG A 104
REMARK 465 PRO A 105
REMARK 465 LYS A 106
REMARK 465 ASP A 107
REMARK 465 ASP A 108
REMARK 465 ARG A 109
REMARK 465 SER A 110
REMARK 465 GLU A 111
REMARK 465 ASN A 331
REMARK 465 ALA A 332
REMARK 465 PRO A 333
REMARK 465 ALA A 334
REMARK 465 ALA A 335
REMARK 465 GLY A 336
REMARK 465 ALA A 337
REMARK 465 SER B 100
REMARK 465 ILE B 101
REMARK 465 PRO B 102
REMARK 465 GLY B 103
REMARK 465 ARG B 104
REMARK 465 PRO B 105
REMARK 465 LYS B 106
REMARK 465 ASP B 107
REMARK 465 ASP B 108
REMARK 465 ARG B 109
REMARK 465 SER B 110
REMARK 465 GLU B 111
REMARK 465 ASP B 330
REMARK 465 ASN B 331
REMARK 465 ALA B 332
REMARK 465 PRO B 333
REMARK 465 ALA B 334
REMARK 465 ALA B 335
REMARK 465 GLY B 336
REMARK 465 ALA B 337
REMARK 465 MET C 17
REMARK 465 SER C 100
REMARK 465 ILE C 101
REMARK 465 PRO C 102
REMARK 465 GLY C 103
REMARK 465 ARG C 104
REMARK 465 PRO C 105
REMARK 465 LYS C 106
REMARK 465 ASP C 107
REMARK 465 ASP C 108
REMARK 465 ARG C 109
REMARK 465 SER C 110
REMARK 465 GLU C 111
REMARK 465 ASP C 330
REMARK 465 ASN C 331
REMARK 465 ALA C 332
REMARK 465 PRO C 333
REMARK 465 ALA C 334
REMARK 465 ALA C 335
REMARK 465 GLY C 336
REMARK 465 ALA C 337
REMARK 465 MET D 17
REMARK 465 SER D 100
REMARK 465 ILE D 101
REMARK 465 PRO D 102
REMARK 465 GLY D 103
REMARK 465 ARG D 104
REMARK 465 PRO D 105
REMARK 465 LYS D 106
REMARK 465 ASP D 107
REMARK 465 ASP D 108
REMARK 465 ARG D 109
REMARK 465 SER D 110
REMARK 465 GLU D 111
REMARK 465 VAL D 328
REMARK 465 LEU D 329
REMARK 465 ASP D 330
REMARK 465 ASN D 331
REMARK 465 ALA D 332
REMARK 465 PRO D 333
REMARK 465 ALA D 334
REMARK 465 ALA D 335
REMARK 465 GLY D 336
REMARK 465 ALA D 337
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 CYS A 131 63.38 -153.18
REMARK 500 ALA A 164 -52.73 -159.35
REMARK 500 ALA A 202 93.22 -68.46
REMARK 500 LYS A 244A -54.03 74.71
REMARK 500 TYR A 247 -26.81 -149.44
REMARK 500 VAL A 328 98.66 -65.52
REMARK 500 LEU A 329 80.31 -159.86
REMARK 500 SER B 29 30.65 -99.06
REMARK 500 CYS B 131 64.28 -155.14
REMARK 500 ALA B 164 -52.98 -149.19
REMARK 500 LYS B 244A -42.11 71.59
REMARK 500 TYR B 247 -22.91 -142.69
REMARK 500 ALA C 164 -54.06 -154.45
REMARK 500 LYS C 244A -68.39 71.63
REMARK 500 SER D 29 37.26 -98.94
REMARK 500 ALA D 164 -54.68 -163.21
REMARK 500 LYS D 244A -63.89 71.83
REMARK 500 TYR D 247 -29.45 -154.40
REMARK 500 ASN D 277 50.49 -161.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ND1 RELATED DB: PDB
REMARK 900 RELATED ID: 4ND2 RELATED DB: PDB
REMARK 900 RELATED ID: 4ND3 RELATED DB: PDB
REMARK 900 RELATED ID: 4ND4 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 PEPTIDE SEQUENCE FOR THIS ENTRY WAS TRANSLATED FROM DNA SEQUENCING
REMARK 999 OF ACTUAL CLONE USED FOR PROTEIN EXPRESSION. AUTHORS DO NOT KNOW IF
REMARK 999 THE SEQUENCE DIFFERENCES ARE PCR ERRORS OR MUTATIONS CORRESPONDING
REMARK 999 DNA POLYMORPHISM OR THERE WERE ERRORS IN PROTEIN DATABASE.
DBREF 4ND5 A 17 337 UNP Q5CYZ2 Q5CYZ2_CRYPI 17 337
DBREF 4ND5 B 17 337 UNP Q5CYZ2 Q5CYZ2_CRYPI 17 337
DBREF 4ND5 C 17 337 UNP Q5CYZ2 Q5CYZ2_CRYPI 17 337
DBREF 4ND5 D 17 337 UNP Q5CYZ2 Q5CYZ2_CRYPI 17 337
SEQADV 4ND5 ALA A 202 UNP Q5CYZ2 VAL 200 SEE REMARK 999
SEQADV 4ND5 ALA B 202 UNP Q5CYZ2 VAL 200 SEE REMARK 999
SEQADV 4ND5 ALA C 202 UNP Q5CYZ2 VAL 200 SEE REMARK 999
SEQADV 4ND5 ALA D 202 UNP Q5CYZ2 VAL 200 SEE REMARK 999
SEQRES 1 A 321 MET ILE GLU ARG ARG LYS ILE ALA VAL ILE GLY SER GLY
SEQRES 2 A 321 GLN ILE GLY GLY ASN ILE ALA TYR ILE VAL GLY LYS ASP
SEQRES 3 A 321 ASN LEU ALA ASP VAL VAL LEU PHE ASP ILE ALA GLU GLY
SEQRES 4 A 321 ILE PRO GLN GLY LYS ALA LEU ASP ILE THR HIS SER MET
SEQRES 5 A 321 VAL MET PHE GLY SER THR SER LYS VAL ILE GLY THR ASN
SEQRES 6 A 321 ASP TYR ALA ASP ILE SER GLY SER ASP VAL VAL ILE ILE
SEQRES 7 A 321 THR ALA SER ILE PRO GLY ARG PRO LYS ASP ASP ARG SER
SEQRES 8 A 321 GLU LEU LEU PHE GLY ASN ALA ARG ILE LEU ASP SER VAL
SEQRES 9 A 321 ALA GLU GLY VAL LYS LYS TYR CYS PRO ASN ALA PHE VAL
SEQRES 10 A 321 ILE CYS ILE THR ASN PRO LEU ASP VAL MET VAL SER HIS
SEQRES 11 A 321 PHE GLN LYS VAL SER GLY LEU PRO HIS ASN LYS VAL CYS
SEQRES 12 A 321 GLY MET ALA GLY VAL LEU ASP SER SER ARG PHE ARG THR
SEQRES 13 A 321 PHE ILE ALA GLN HIS PHE GLY VAL ASN ALA SER ASP VAL
SEQRES 14 A 321 SER ALA ASN VAL ILE GLY GLY HIS GLY ASP GLY MET VAL
SEQRES 15 A 321 PRO ALA THR SER SER VAL SER VAL GLY GLY VAL PRO LEU
SEQRES 16 A 321 SER SER PHE ILE LYS GLN GLY LEU ILE THR GLN GLU GLN
SEQRES 17 A 321 ILE ASP GLU ILE VAL CYS HIS THR ARG ILE ALA TRP LYS
SEQRES 18 A 321 GLU VAL ALA ASP ASN LEU LYS THR GLY THR ALA TYR PHE
SEQRES 19 A 321 ALA PRO ALA ALA ALA ALA VAL LYS MET ALA GLU ALA TYR
SEQRES 20 A 321 LEU LYS ASP LYS LYS ALA VAL VAL PRO CYS SER ALA PHE
SEQRES 21 A 321 CYS SER ASN HIS TYR GLY VAL LYS GLY ILE TYR MET GLY
SEQRES 22 A 321 VAL PRO THR ILE ILE GLY LYS ASN GLY VAL GLU ASP ILE
SEQRES 23 A 321 LEU GLU LEU ASP LEU THR PRO LEU GLU GLN LYS LEU LEU
SEQRES 24 A 321 GLY GLU SER ILE ASN GLU VAL ASN THR ILE SER LYS VAL
SEQRES 25 A 321 LEU ASP ASN ALA PRO ALA ALA GLY ALA
SEQRES 1 B 321 MET ILE GLU ARG ARG LYS ILE ALA VAL ILE GLY SER GLY
SEQRES 2 B 321 GLN ILE GLY GLY ASN ILE ALA TYR ILE VAL GLY LYS ASP
SEQRES 3 B 321 ASN LEU ALA ASP VAL VAL LEU PHE ASP ILE ALA GLU GLY
SEQRES 4 B 321 ILE PRO GLN GLY LYS ALA LEU ASP ILE THR HIS SER MET
SEQRES 5 B 321 VAL MET PHE GLY SER THR SER LYS VAL ILE GLY THR ASN
SEQRES 6 B 321 ASP TYR ALA ASP ILE SER GLY SER ASP VAL VAL ILE ILE
SEQRES 7 B 321 THR ALA SER ILE PRO GLY ARG PRO LYS ASP ASP ARG SER
SEQRES 8 B 321 GLU LEU LEU PHE GLY ASN ALA ARG ILE LEU ASP SER VAL
SEQRES 9 B 321 ALA GLU GLY VAL LYS LYS TYR CYS PRO ASN ALA PHE VAL
SEQRES 10 B 321 ILE CYS ILE THR ASN PRO LEU ASP VAL MET VAL SER HIS
SEQRES 11 B 321 PHE GLN LYS VAL SER GLY LEU PRO HIS ASN LYS VAL CYS
SEQRES 12 B 321 GLY MET ALA GLY VAL LEU ASP SER SER ARG PHE ARG THR
SEQRES 13 B 321 PHE ILE ALA GLN HIS PHE GLY VAL ASN ALA SER ASP VAL
SEQRES 14 B 321 SER ALA ASN VAL ILE GLY GLY HIS GLY ASP GLY MET VAL
SEQRES 15 B 321 PRO ALA THR SER SER VAL SER VAL GLY GLY VAL PRO LEU
SEQRES 16 B 321 SER SER PHE ILE LYS GLN GLY LEU ILE THR GLN GLU GLN
SEQRES 17 B 321 ILE ASP GLU ILE VAL CYS HIS THR ARG ILE ALA TRP LYS
SEQRES 18 B 321 GLU VAL ALA ASP ASN LEU LYS THR GLY THR ALA TYR PHE
SEQRES 19 B 321 ALA PRO ALA ALA ALA ALA VAL LYS MET ALA GLU ALA TYR
SEQRES 20 B 321 LEU LYS ASP LYS LYS ALA VAL VAL PRO CYS SER ALA PHE
SEQRES 21 B 321 CYS SER ASN HIS TYR GLY VAL LYS GLY ILE TYR MET GLY
SEQRES 22 B 321 VAL PRO THR ILE ILE GLY LYS ASN GLY VAL GLU ASP ILE
SEQRES 23 B 321 LEU GLU LEU ASP LEU THR PRO LEU GLU GLN LYS LEU LEU
SEQRES 24 B 321 GLY GLU SER ILE ASN GLU VAL ASN THR ILE SER LYS VAL
SEQRES 25 B 321 LEU ASP ASN ALA PRO ALA ALA GLY ALA
SEQRES 1 C 321 MET ILE GLU ARG ARG LYS ILE ALA VAL ILE GLY SER GLY
SEQRES 2 C 321 GLN ILE GLY GLY ASN ILE ALA TYR ILE VAL GLY LYS ASP
SEQRES 3 C 321 ASN LEU ALA ASP VAL VAL LEU PHE ASP ILE ALA GLU GLY
SEQRES 4 C 321 ILE PRO GLN GLY LYS ALA LEU ASP ILE THR HIS SER MET
SEQRES 5 C 321 VAL MET PHE GLY SER THR SER LYS VAL ILE GLY THR ASN
SEQRES 6 C 321 ASP TYR ALA ASP ILE SER GLY SER ASP VAL VAL ILE ILE
SEQRES 7 C 321 THR ALA SER ILE PRO GLY ARG PRO LYS ASP ASP ARG SER
SEQRES 8 C 321 GLU LEU LEU PHE GLY ASN ALA ARG ILE LEU ASP SER VAL
SEQRES 9 C 321 ALA GLU GLY VAL LYS LYS TYR CYS PRO ASN ALA PHE VAL
SEQRES 10 C 321 ILE CYS ILE THR ASN PRO LEU ASP VAL MET VAL SER HIS
SEQRES 11 C 321 PHE GLN LYS VAL SER GLY LEU PRO HIS ASN LYS VAL CYS
SEQRES 12 C 321 GLY MET ALA GLY VAL LEU ASP SER SER ARG PHE ARG THR
SEQRES 13 C 321 PHE ILE ALA GLN HIS PHE GLY VAL ASN ALA SER ASP VAL
SEQRES 14 C 321 SER ALA ASN VAL ILE GLY GLY HIS GLY ASP GLY MET VAL
SEQRES 15 C 321 PRO ALA THR SER SER VAL SER VAL GLY GLY VAL PRO LEU
SEQRES 16 C 321 SER SER PHE ILE LYS GLN GLY LEU ILE THR GLN GLU GLN
SEQRES 17 C 321 ILE ASP GLU ILE VAL CYS HIS THR ARG ILE ALA TRP LYS
SEQRES 18 C 321 GLU VAL ALA ASP ASN LEU LYS THR GLY THR ALA TYR PHE
SEQRES 19 C 321 ALA PRO ALA ALA ALA ALA VAL LYS MET ALA GLU ALA TYR
SEQRES 20 C 321 LEU LYS ASP LYS LYS ALA VAL VAL PRO CYS SER ALA PHE
SEQRES 21 C 321 CYS SER ASN HIS TYR GLY VAL LYS GLY ILE TYR MET GLY
SEQRES 22 C 321 VAL PRO THR ILE ILE GLY LYS ASN GLY VAL GLU ASP ILE
SEQRES 23 C 321 LEU GLU LEU ASP LEU THR PRO LEU GLU GLN LYS LEU LEU
SEQRES 24 C 321 GLY GLU SER ILE ASN GLU VAL ASN THR ILE SER LYS VAL
SEQRES 25 C 321 LEU ASP ASN ALA PRO ALA ALA GLY ALA
SEQRES 1 D 321 MET ILE GLU ARG ARG LYS ILE ALA VAL ILE GLY SER GLY
SEQRES 2 D 321 GLN ILE GLY GLY ASN ILE ALA TYR ILE VAL GLY LYS ASP
SEQRES 3 D 321 ASN LEU ALA ASP VAL VAL LEU PHE ASP ILE ALA GLU GLY
SEQRES 4 D 321 ILE PRO GLN GLY LYS ALA LEU ASP ILE THR HIS SER MET
SEQRES 5 D 321 VAL MET PHE GLY SER THR SER LYS VAL ILE GLY THR ASN
SEQRES 6 D 321 ASP TYR ALA ASP ILE SER GLY SER ASP VAL VAL ILE ILE
SEQRES 7 D 321 THR ALA SER ILE PRO GLY ARG PRO LYS ASP ASP ARG SER
SEQRES 8 D 321 GLU LEU LEU PHE GLY ASN ALA ARG ILE LEU ASP SER VAL
SEQRES 9 D 321 ALA GLU GLY VAL LYS LYS TYR CYS PRO ASN ALA PHE VAL
SEQRES 10 D 321 ILE CYS ILE THR ASN PRO LEU ASP VAL MET VAL SER HIS
SEQRES 11 D 321 PHE GLN LYS VAL SER GLY LEU PRO HIS ASN LYS VAL CYS
SEQRES 12 D 321 GLY MET ALA GLY VAL LEU ASP SER SER ARG PHE ARG THR
SEQRES 13 D 321 PHE ILE ALA GLN HIS PHE GLY VAL ASN ALA SER ASP VAL
SEQRES 14 D 321 SER ALA ASN VAL ILE GLY GLY HIS GLY ASP GLY MET VAL
SEQRES 15 D 321 PRO ALA THR SER SER VAL SER VAL GLY GLY VAL PRO LEU
SEQRES 16 D 321 SER SER PHE ILE LYS GLN GLY LEU ILE THR GLN GLU GLN
SEQRES 17 D 321 ILE ASP GLU ILE VAL CYS HIS THR ARG ILE ALA TRP LYS
SEQRES 18 D 321 GLU VAL ALA ASP ASN LEU LYS THR GLY THR ALA TYR PHE
SEQRES 19 D 321 ALA PRO ALA ALA ALA ALA VAL LYS MET ALA GLU ALA TYR
SEQRES 20 D 321 LEU LYS ASP LYS LYS ALA VAL VAL PRO CYS SER ALA PHE
SEQRES 21 D 321 CYS SER ASN HIS TYR GLY VAL LYS GLY ILE TYR MET GLY
SEQRES 22 D 321 VAL PRO THR ILE ILE GLY LYS ASN GLY VAL GLU ASP ILE
SEQRES 23 D 321 LEU GLU LEU ASP LEU THR PRO LEU GLU GLN LYS LEU LEU
SEQRES 24 D 321 GLY GLU SER ILE ASN GLU VAL ASN THR ILE SER LYS VAL
SEQRES 25 D 321 LEU ASP ASN ALA PRO ALA ALA GLY ALA
FORMUL 5 HOH *194(H2 O)
HELIX 1 1 GLY A 30 ASN A 44 1 15
HELIX 2 2 GLY A 57 GLY A 73B 1 18
HELIX 3 3 ASP A 84 SER A 89 5 6
HELIX 4 4 LEU A 113 CYS A 131 1 19
HELIX 5 5 PRO A 141 GLY A 154 1 14
HELIX 6 6 PRO A 156 ASN A 158 5 3
HELIX 7 7 ALA A 164 GLY A 181 1 18
HELIX 8 8 ASN A 183 SER A 185 5 3
HELIX 9 9 HIS A 195 ASP A 197 5 3
HELIX 10 10 LEU A 212 GLN A 218A 1 7
HELIX 11 11 THR A 221 LYS A 244A 1 24
HELIX 12 12 TYR A 247 LYS A 263 1 17
HELIX 13 13 THR A 308 VAL A 328 1 21
HELIX 14 14 GLY B 30 ASN B 44 1 15
HELIX 15 15 GLY B 57 MET B 70 1 14
HELIX 16 16 ASP B 84 SER B 89 5 6
HELIX 17 17 LEU B 113 CYS B 131 1 19
HELIX 18 18 PRO B 141 GLY B 154 1 14
HELIX 19 19 PRO B 156 ASN B 158 5 3
HELIX 20 20 ALA B 164 GLY B 181 1 18
HELIX 21 21 ASN B 183 SER B 185 5 3
HELIX 22 22 HIS B 195 ASP B 197 5 3
HELIX 23 23 THR B 203 SER B 205 5 3
HELIX 24 24 LEU B 212 GLN B 218A 1 7
HELIX 25 25 THR B 221 LYS B 244A 1 24
HELIX 26 26 TYR B 247 LYS B 263 1 17
HELIX 27 27 THR B 308 LEU B 329 1 22
HELIX 28 28 GLY C 30 ASP C 43 1 14
HELIX 29 29 GLY C 57 GLY C 73B 1 18
HELIX 30 30 ASP C 84 SER C 89 5 6
HELIX 31 31 LEU C 113 CYS C 131 1 19
HELIX 32 32 PRO C 141 GLY C 154 1 14
HELIX 33 33 PRO C 156 ASN C 158 5 3
HELIX 34 34 ALA C 164 GLY C 181 1 18
HELIX 35 35 ASN C 183 SER C 185 5 3
HELIX 36 36 HIS C 195 ASP C 197 5 3
HELIX 37 37 THR C 203 SER C 205 5 3
HELIX 38 38 LEU C 212 GLN C 218A 1 7
HELIX 39 39 THR C 221 LYS C 244A 1 24
HELIX 40 40 TYR C 247 LYS C 263 1 17
HELIX 41 41 THR C 308 LEU C 329 1 22
HELIX 42 42 GLY D 30 ASN D 44 1 15
HELIX 43 43 GLY D 57 GLY D 73B 1 18
HELIX 44 44 ASP D 84 SER D 89 5 6
HELIX 45 45 LEU D 113 CYS D 131 1 19
HELIX 46 46 PRO D 141 GLY D 154 1 14
HELIX 47 47 PRO D 156 ASN D 158 5 3
HELIX 48 48 ALA D 164 GLY D 181 1 18
HELIX 49 49 ASN D 183 SER D 185 5 3
HELIX 50 50 HIS D 195 ASP D 197 5 3
HELIX 51 51 THR D 203 VAL D 206 5 4
HELIX 52 52 PRO D 210B GLN D 218A 1 8
HELIX 53 53 THR D 221 LYS D 244A 1 24
HELIX 54 54 TYR D 247 LYS D 263 1 17
HELIX 55 55 THR D 308 SER D 326 1 19
SHEET 1 A 6 VAL A 78 THR A 81 0
SHEET 2 A 6 ASP A 48 PHE A 52 1 N LEU A 51 O ILE A 79
SHEET 3 A 6 LYS A 23 ILE A 27 1 N VAL A 26 O PHE A 52
SHEET 4 A 6 VAL A 93 ILE A 96 1 O ILE A 95 N ILE A 27
SHEET 5 A 6 PHE A 134 CYS A 137 1 O ILE A 136 N VAL A 94
SHEET 6 A 6 VAL A 160 GLY A 162 1 O CYS A 161 N CYS A 137
SHEET 1 B 3 VAL A 187 GLY A 193 0
SHEET 2 B 3 MET A 199 VAL A 208 -1 O SER A 207 N SER A 188
SHEET 3 B 3 VAL A 210A PRO A 210B-1 O VAL A 210A N VAL A 208
SHEET 1 C 3 ALA A 267 CYS A 275 0
SHEET 2 C 3 ILE A 285 GLY A 294 -1 O ILE A 285 N CYS A 275
SHEET 3 C 3 GLY A 297 ILE A 302 -1 O GLU A 299 N ILE A 292
SHEET 1 D 6 VAL B 78 THR B 81 0
SHEET 2 D 6 ASP B 48 PHE B 52 1 N LEU B 51 O ILE B 79
SHEET 3 D 6 LYS B 23 ILE B 27 1 N VAL B 26 O VAL B 50
SHEET 4 D 6 VAL B 93 ILE B 96 1 O ILE B 95 N ILE B 27
SHEET 5 D 6 PHE B 134 CYS B 137 1 O ILE B 136 N VAL B 94
SHEET 6 D 6 VAL B 160 GLY B 162 1 O CYS B 161 N CYS B 137
SHEET 1 E 3 VAL B 187 SER B 188 0
SHEET 2 E 3 SER B 207 VAL B 208 -1 O SER B 207 N SER B 188
SHEET 3 E 3 VAL B 210A PRO B 210B-1 O VAL B 210A N VAL B 208
SHEET 1 F 2 VAL B 191 GLY B 193 0
SHEET 2 F 2 MET B 199 PRO B 201 -1 O VAL B 200 N ILE B 192
SHEET 1 G 3 ALA B 267 CYS B 275 0
SHEET 2 G 3 ILE B 285 GLY B 294 -1 O ILE B 285 N CYS B 275
SHEET 3 G 3 GLY B 297 ILE B 302 -1 O GLU B 299 N ILE B 292
SHEET 1 H 6 VAL C 78 THR C 81 0
SHEET 2 H 6 ASP C 48 PHE C 52 1 N LEU C 51 O ILE C 79
SHEET 3 H 6 LYS C 23 ILE C 27 1 N VAL C 26 O PHE C 52
SHEET 4 H 6 VAL C 93 ILE C 96 1 O ILE C 95 N ALA C 25
SHEET 5 H 6 PHE C 134 CYS C 137 1 O ILE C 136 N VAL C 94
SHEET 6 H 6 VAL C 160 GLY C 162 1 O CYS C 161 N CYS C 137
SHEET 1 I 3 VAL C 187 SER C 188 0
SHEET 2 I 3 SER C 207 VAL C 208 -1 O SER C 207 N SER C 188
SHEET 3 I 3 VAL C 210A PRO C 210B-1 O VAL C 210A N VAL C 208
SHEET 1 J 2 VAL C 191 GLY C 193 0
SHEET 2 J 2 MET C 199 PRO C 201 -1 O VAL C 200 N ILE C 192
SHEET 1 K 3 ALA C 267 CYS C 275 0
SHEET 2 K 3 ILE C 285 GLY C 294 -1 O THR C 291 N VAL C 269
SHEET 3 K 3 GLY C 297 ILE C 302 -1 O GLU C 299 N ILE C 292
SHEET 1 L 6 VAL D 78 THR D 81 0
SHEET 2 L 6 ASP D 48 PHE D 52 1 N LEU D 51 O ILE D 79
SHEET 3 L 6 LYS D 23 ILE D 27 1 N VAL D 26 O PHE D 52
SHEET 4 L 6 VAL D 93 ILE D 96 1 O VAL D 93 N ALA D 25
SHEET 5 L 6 PHE D 134 CYS D 137 1 O ILE D 136 N VAL D 94
SHEET 6 L 6 VAL D 160 GLY D 162 1 O CYS D 161 N CYS D 137
SHEET 1 M 2 VAL D 187 SER D 188 0
SHEET 2 M 2 SER D 207 VAL D 208 -1 O SER D 207 N SER D 188
SHEET 1 N 2 VAL D 191 GLY D 193 0
SHEET 2 N 2 MET D 199 PRO D 201 -1 O VAL D 200 N ILE D 192
SHEET 1 O 3 ALA D 267 CYS D 275 0
SHEET 2 O 3 ILE D 285 GLY D 294 -1 O ILE D 285 N CYS D 275
SHEET 3 O 3 GLY D 297 ILE D 302 -1 O GLU D 299 N ILE D 292
LINK C ARG A 20 N ARG A 22 1555 1555 1.33
LINK C ALA A 46 N ASP A 48 1555 1555 1.33
LINK C PHE A 73A N GLY A 73B 1555 1555 1.33
LINK C THR A 81 N ASN A 83 1555 1555 1.33
LINK C PRO A 132A N ASN A 132B 1555 1555 1.33
LINK C GLY A 209A N GLY A 209B 1555 1555 1.33
LINK C VAL A 210A N PRO A 210B 1555 1555 1.33
LINK C PRO A 210B N LEU A 212 1555 1555 1.33
LINK C GLN A 218A N GLY A 218B 1555 1555 1.33
LINK C LYS A 244A N THR A 244B 1555 1555 1.33
LINK C THR A 244B N GLY A 244C 1555 1555 1.33
LINK C GLY A 283 N ILE A 285 1555 1555 1.33
LINK C GLU A 299 N ASP A 301 1555 1555 1.33
LINK C ARG B 20 N ARG B 22 1555 1555 1.33
LINK C ALA B 46 N ASP B 48 1555 1555 1.33
LINK C PHE B 73A N GLY B 73B 1555 1555 1.33
LINK C THR B 81 N ASN B 83 1555 1555 1.33
LINK C PRO B 132A N ASN B 132B 1555 1555 1.33
LINK C GLY B 209A N GLY B 209B 1555 1555 1.33
LINK C VAL B 210A N PRO B 210B 1555 1555 1.34
LINK C PRO B 210B N LEU B 212 1555 1555 1.33
LINK C GLN B 218A N GLY B 218B 1555 1555 1.33
LINK C LYS B 244A N THR B 244B 1555 1555 1.33
LINK C THR B 244B N GLY B 244C 1555 1555 1.33
LINK C GLY B 283 N ILE B 285 1555 1555 1.33
LINK C GLU B 299 N ASP B 301 1555 1555 1.33
LINK C ARG C 20 N ARG C 22 1555 1555 1.33
LINK C ALA C 46 N ASP C 48 1555 1555 1.33
LINK C PHE C 73A N GLY C 73B 1555 1555 1.33
LINK C THR C 81 N ASN C 83 1555 1555 1.33
LINK C PRO C 132A N ASN C 132B 1555 1555 1.33
LINK C GLY C 209A N GLY C 209B 1555 1555 1.33
LINK C VAL C 210A N PRO C 210B 1555 1555 1.33
LINK C PRO C 210B N LEU C 212 1555 1555 1.33
LINK C GLN C 218A N GLY C 218B 1555 1555 1.33
LINK C LYS C 244A N THR C 244B 1555 1555 1.33
LINK C THR C 244B N GLY C 244C 1555 1555 1.33
LINK C GLY C 283 N ILE C 285 1555 1555 1.33
LINK C GLU C 299 N ASP C 301 1555 1555 1.33
LINK C ARG D 20 N ARG D 22 1555 1555 1.33
LINK C ALA D 46 N ASP D 48 1555 1555 1.33
LINK C PHE D 73A N GLY D 73B 1555 1555 1.33
LINK C THR D 81 N ASN D 83 1555 1555 1.33
LINK C PRO D 132A N ASN D 132B 1555 1555 1.33
LINK C GLY D 209A N GLY D 209B 1555 1555 1.33
LINK C VAL D 210A N PRO D 210B 1555 1555 1.34
LINK C PRO D 210B N LEU D 212 1555 1555 1.33
LINK C GLN D 218A N GLY D 218B 1555 1555 1.33
LINK C LYS D 244A N THR D 244B 1555 1555 1.33
LINK C THR D 244B N GLY D 244C 1555 1555 1.33
LINK C GLY D 283 N ILE D 285 1555 1555 1.33
LINK C GLU D 299 N ASP D 301 1555 1555 1.33
CISPEP 1 ASN A 140 PRO A 141 0 -4.53
CISPEP 2 ASN B 140 PRO B 141 0 -3.93
CISPEP 3 ASN C 140 PRO C 141 0 -3.59
CISPEP 4 ASN D 140 PRO D 141 0 0.22
CRYST1 136.490 136.490 170.220 90.00 90.00 120.00 P 32 1 2 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 0.007327 0.004230 0.000000 0.00000
SCALE2 0.000000 0.008460 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005875 0.00000
(ATOM LINES ARE NOT SHOWN.)
END