HEADER HYDROLASE 26-MAR-08 2VR5
TITLE CRYSTAL STRUCTURE OF TREX FROM SULFOLOBUS SOLFATARICUS IN COMPLEX WITH
TITLE 2 ACARBOSE INTERMEDIATE AND GLUCOSE
CAVEAT 2VR5 GLU A 161 HAS WRONG CHIRALITY AT ATOM CA CYS A 261 HAS WRONG
CAVEAT 2 2VR5 CHIRALITY AT ATOM CA LEU B 372 HAS WRONG CHIRALITY AT ATOM
CAVEAT 3 2VR5 CA A16 A 1722 HAS WRONG CHIRALITY AT ATOM C5A A16 B 1720
CAVEAT 4 2VR5 HAS WRONG CHIRALITY AT ATOM C5A GLU A 161 HAS WRONG
CAVEAT 5 2VR5 CHIRALITY FOR AN L-AMINO ACID CYS A 261 HAS WRONG CHIRALITY
CAVEAT 6 2VR5 FOR AN L-AMINO ACID LEU B 372 HAS WRONG CHIRALITY FOR AN L-
CAVEAT 7 2VR5 AMINO ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOGEN OPERON PROTEIN GLGX;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TREX, GLYCOGEN DEBRANCHING ENZYME;
COMPND 5 EC: 3.2.1.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: DISULFIDE BOND BETWEEN A 254 AND A 261, A 505 AND A
COMPND 8 519, B 254 AND B 261, B 505 AND B 519
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE 3 ORGANISM_TAXID: 2287;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE, GLYCOSIDASE, GLYCOSYL HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.-N.SONG,S.-M.YOON,S.-J.LEE,H.-J.CHA,K.-H.PARK,E.-J.WOO
REVDAT 6 13-DEC-23 2VR5 1 HETSYN
REVDAT 5 29-JUL-20 2VR5 1 CAVEAT COMPND REMARK HETNAM
REVDAT 5 2 1 LINK SITE
REVDAT 4 01-APR-15 2VR5 1 JRNL
REVDAT 3 29-AUG-12 2VR5 1 CAVEAT KEYWDS JRNL REMARK
REVDAT 3 2 1 VERSN HETSYN FORMUL
REVDAT 2 24-FEB-09 2VR5 1 VERSN
REVDAT 1 29-JUL-08 2VR5 0
JRNL AUTH E.WOO,S.LEE,H.CHA,J.PARK,S.YOON,H.SONG,K.PARK
JRNL TITL STRUCTURAL INSIGHT INTO THE BIFUNCTIONAL MECHANISM OF THE
JRNL TITL 2 GLYCOGEN-DEBRANCHING ENZYME TREX FROM THE ARCHAEON
JRNL TITL 3 SULFOLOBUS SOLFATARICUS.
JRNL REF J.BIOL.CHEM. V. 283 28641 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18703518
JRNL DOI 10.1074/JBC.M802560200
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 48122.730
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 51460
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) : 0.214
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2573
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7824
REMARK 3 BIN R VALUE (WORKING SET) : 0.3290
REMARK 3 BIN FREE R VALUE : 0.3690
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 403
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11685
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 123
REMARK 3 SOLVENT ATOMS : 401
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 3.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 9.08000
REMARK 3 B22 (A**2) : 9.08000
REMARK 3 B33 (A**2) : -18.15000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.55
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.44
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.73
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 0.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.220
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 4.340 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 6.340 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 6.610 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 8.450 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.30
REMARK 3 BSOL : 21.56
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ADR2_PAR.TXT
REMARK 3 PARAMETER FILE 3 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : GLC_PAR.TXT
REMARK 3 PARAMETER FILE 5 : GOL_PAR.TXT
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ADR2_TOP.TXT
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : GLC_TOP.TXT
REMARK 3 TOPOLOGY FILE 5 : GOL_TOP.TXT
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 2VR5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-MAR-08.
REMARK 100 THE DEPOSITION ID IS D_1290035158.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-07
REMARK 200 TEMPERATURE (KELVIN) : 97
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51526
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.27000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 2VNC
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3K 8%, 0.2M LITHIUM SULFATE, 0.1M
REMARK 280 PH 8.0 IMIDAZOLE BUFFER
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 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
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
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 0.00000
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 0.00000
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 0.00000
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
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 26690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 141220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.2 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 -102.40700
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 177.37413
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -204.81400
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 LEU A 3
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 LEU B 3
REMARK 465 PHE B 4
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 ASN A 515 CG OD1 ND2
REMARK 470 VAL A 516 CG1 CG2
REMARK 470 VAL A 517 CG1 CG2
REMARK 470 ASN B 515 CG OD1 ND2
REMARK 470 VAL B 516 CG1 CG2
REMARK 470 VAL B 517 CG1 CG2
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 OE2 GLU A 161 ND1 HIS A 356 1.82
REMARK 500 OD2 ASP B 624 O HOH B 2165 1.87
REMARK 500 N THR B 627 O HOH B 2165 1.94
REMARK 500 OH TYR A 126 O LEU A 298 1.99
REMARK 500 ND2 ASN B 482 ND2 ASN B 504 2.02
REMARK 500 OE1 GLU B 157 O HOH B 2062 2.05
REMARK 500 CD2 LEU B 135 NH1 ARG B 321 2.08
REMARK 500 NH1 ARG A 305 OH TYR A 323 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O ARG A 653 O ILE B 654 2565 1.79
REMARK 500 NH2 ARG A 653 O ASP B 656 2565 2.18
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 PHE A 5 -166.88 -121.08
REMARK 500 ASP A 29 68.50 34.47
REMARK 500 SER A 37 114.03 -173.36
REMARK 500 LYS A 65 99.85 -162.76
REMARK 500 LYS A 92 74.20 -157.41
REMARK 500 ASN A 114 -75.96 -69.92
REMARK 500 ASN A 120 129.39 -178.82
REMARK 500 ASN A 132 41.22 -90.62
REMARK 500 GLN A 133 134.86 -31.20
REMARK 500 ASP A 134 -8.05 66.35
REMARK 500 ASP A 160 -7.21 58.83
REMARK 500 GLU A 161 -70.86 -39.35
REMARK 500 ILE A 164 24.44 -71.29
REMARK 500 LYS A 167 66.59 -69.19
REMARK 500 LYS A 168 -159.59 -76.79
REMARK 500 THR A 185 6.08 -153.45
REMARK 500 LEU A 187 30.33 -95.35
REMARK 500 ARG A 188 78.11 -104.24
REMARK 500 GLU A 193 166.30 -48.94
REMARK 500 ASN A 194 -9.29 82.27
REMARK 500 PRO A 223 129.79 -38.77
REMARK 500 HIS A 226 119.99 -29.93
REMARK 500 GLN A 230 137.39 -30.36
REMARK 500 TYR A 244 46.65 -76.12
REMARK 500 CYS A 261 -12.17 86.88
REMARK 500 ASN A 296 -163.68 -71.57
REMARK 500 LEU A 298 -25.04 68.97
REMARK 500 SER A 303 -78.95 -149.62
REMARK 500 ASP A 308 89.76 -167.24
REMARK 500 TYR A 312 -40.61 76.68
REMARK 500 GLN A 316 108.75 -49.85
REMARK 500 LEU A 335 22.61 -75.66
REMARK 500 GLU A 371 -74.93 -99.22
REMARK 500 MET A 377 8.44 -62.49
REMARK 500 PRO A 400 22.03 -75.61
REMARK 500 TYR A 415 159.84 -44.75
REMARK 500 GLN A 416 -13.41 84.74
REMARK 500 SER A 427 -70.62 -50.24
REMARK 500 GLU A 435 145.34 -39.80
REMARK 500 SER A 469 159.58 171.91
REMARK 500 HIS A 485 70.23 -112.34
REMARK 500 ASN A 486 50.13 -103.53
REMARK 500 ASN A 492 40.46 37.80
REMARK 500 TYR A 501 47.41 33.41
REMARK 500 ALA A 507 -159.80 -172.78
REMARK 500 ASP A 513 104.72 -55.82
REMARK 500 THR A 530 -72.86 -55.61
REMARK 500 VAL A 533 -7.24 -142.48
REMARK 500 ASN A 555 51.02 -153.48
REMARK 500 ALA A 556 47.84 -82.02
REMARK 500
REMARK 500 THIS ENTRY HAS 122 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 56 LYS A 57 147.06
REMARK 500 GLY A 125 TYR A 126 149.81
REMARK 500 GLU A 161 ASP A 162 -140.36
REMARK 500 LYS A 165 GLY A 166 -91.28
REMARK 500 THR A 259 GLY A 260 -112.60
REMARK 500 GLY A 260 CYS A 261 96.26
REMARK 500 ASN A 296 HIS A 297 149.52
REMARK 500 LEU A 618 GLU A 619 127.92
REMARK 500 GLU A 619 GLY A 620 -112.11
REMARK 500 GLY A 620 ARG A 621 -138.62
REMARK 500 LYS A 678 TRP A 679 -140.37
REMARK 500 ASP B 159 ASP B 160 -101.44
REMARK 500 ASP B 160 GLU B 161 148.81
REMARK 500 PHE B 163 ILE B 164 148.96
REMARK 500 LYS B 165 GLY B 166 -88.19
REMARK 500 LEU B 189 ASP B 190 130.01
REMARK 500 PRO B 192 GLU B 193 147.20
REMARK 500 GLU B 193 ASN B 194 -140.16
REMARK 500 GLU B 371 LEU B 372 -128.59
REMARK 500 ALA B 398 GLU B 399 148.12
REMARK 500 ASN B 504 CYS B 505 -146.16
REMARK 500 CYS B 505 GLY B 506 144.40
REMARK 500 PRO B 675 LYS B 676 -140.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2077 DISTANCE = 6.07 ANGSTROMS
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AC" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "BD" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VNC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GLYCOGEN DEBRANCHING ENZYME TREX FROM
REMARK 900 SULFOLOBUS SOLFATARICUS
REMARK 900 RELATED ID: 2VUY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GLYCOGEN DEBRANCHING EXZYME TREX FROM
REMARK 900 SULFOLOBUS SOLFATARIUS
DBREF 2VR5 A 1 718 UNP P95868 P95868_SULSO 1 718
DBREF 2VR5 B 1 718 UNP P95868 P95868_SULSO 1 718
SEQRES 1 A 718 MET ALA LEU PHE PHE ARG THR ARG ASP ARG PRO LEU ARG
SEQRES 2 A 718 PRO GLY ASP PRO TYR PRO LEU GLY SER ASN TRP ILE GLU
SEQRES 3 A 718 ASP ASP ASP GLY VAL ASN PHE SER LEU PHE SER GLU ASN
SEQRES 4 A 718 ALA GLU LYS VAL GLU LEU LEU LEU TYR SER LEU THR ASN
SEQRES 5 A 718 GLN LYS TYR PRO LYS GLU ILE ILE GLU VAL LYS ASN LYS
SEQRES 6 A 718 THR GLY ASP ILE TRP HIS VAL PHE VAL PRO GLY LEU ARG
SEQRES 7 A 718 PRO GLY GLN LEU TYR ALA TYR ARG VAL TYR GLY PRO TYR
SEQRES 8 A 718 LYS PRO GLU LEU GLY LEU ARG PHE ASN PRO ASN LYS VAL
SEQRES 9 A 718 LEU ILE ASP PRO TYR ALA LYS ALA ILE ASN GLY SER VAL
SEQRES 10 A 718 ILE TRP ASN ASP ALA VAL PHE GLY TYR LYS ILE GLY ASP
SEQRES 11 A 718 GLN ASN GLN ASP LEU THR TYR ASP GLU ARG ASP SER GLY
SEQRES 12 A 718 GLU TYR VAL PRO LYS SER VAL VAL ILE ASN PRO TYR PHE
SEQRES 13 A 718 GLU TRP ASP ASP GLU ASP PHE ILE LYS GLY LYS LYS VAL
SEQRES 14 A 718 PRO LEU LYS ASP THR VAL ILE TYR GLU VAL HIS VAL LYS
SEQRES 15 A 718 GLY PHE THR LYS LEU ARG LEU ASP LEU PRO GLU ASN ILE
SEQRES 16 A 718 ARG GLY THR TYR GLU GLY LEU ALA SER GLU GLN MET ILE
SEQRES 17 A 718 SER TYR LEU LYS ASP LEU GLY ILE THR THR VAL GLU LEU
SEQRES 18 A 718 MET PRO VAL PHE HIS PHE ILE ASP GLN ARG PHE LEU THR
SEQRES 19 A 718 ASP LYS GLY LEU THR ASN TYR TRP GLY TYR ASP PRO ILE
SEQRES 20 A 718 ASN PHE PHE SER PRO GLU CYS ARG TYR SER SER THR GLY
SEQRES 21 A 718 CYS LEU GLY GLY GLN VAL LEU SER PHE LYS LYS MET VAL
SEQRES 22 A 718 ASN GLU LEU HIS ASN ALA GLY ILE GLU VAL ILE ILE ASP
SEQRES 23 A 718 VAL VAL TYR ASN HIS THR ALA GLU GLY ASN HIS LEU GLY
SEQRES 24 A 718 PRO THR LEU SER PHE ARG GLY ILE ASP ASN THR ALA TYR
SEQRES 25 A 718 TYR MET LEU GLN PRO ASP ASN LYS ARG TYR TYR LEU ASP
SEQRES 26 A 718 PHE THR GLY THR GLY ASN THR LEU ASN LEU SER HIS PRO
SEQRES 27 A 718 ARG VAL ILE GLN MET VAL LEU ASP SER LEU ARG TYR TRP
SEQRES 28 A 718 VAL THR GLU MET HIS VAL ASP GLY PHE ARG PHE ASP LEU
SEQRES 29 A 718 ALA ALA ALA LEU ALA ARG GLU LEU TYR SER VAL ASN MET
SEQRES 30 A 718 LEU ASN THR PHE PHE ILE ALA LEU GLN GLN ASP PRO ILE
SEQRES 31 A 718 LEU SER GLN VAL LYS LEU ILE ALA GLU PRO TRP ASP VAL
SEQRES 32 A 718 GLY GLN GLY GLY TYR GLN VAL GLY ASN PHE PRO TYR GLN
SEQRES 33 A 718 TRP ALA GLU TRP ASN GLY LYS TYR ARG ASP SER ILE ARG
SEQRES 34 A 718 ARG PHE TRP ARG GLY GLU ALA LEU PRO TYR SER GLU ILE
SEQRES 35 A 718 ALA ASN ARG LEU LEU GLY SER PRO ASP ILE TYR LEU GLY
SEQRES 36 A 718 ASN ASN LYS THR PRO PHE ALA SER ILE ASN TYR VAL THR
SEQRES 37 A 718 SER HIS ASP GLY PHE THR LEU GLU ASP LEU VAL SER TYR
SEQRES 38 A 718 ASN GLN LYS HIS ASN GLU ALA ASN GLY PHE ASN ASN GLN
SEQRES 39 A 718 ASP GLY MET ASN GLU ASN TYR SER TRP ASN CYS GLY ALA
SEQRES 40 A 718 GLU GLY PRO THR ASN ASP GLN ASN VAL VAL ILE CYS ARG
SEQRES 41 A 718 GLU LYS GLN LYS ARG ASN PHE MET ILE THR LEU LEU VAL
SEQRES 42 A 718 SER GLN GLY THR PRO MET ILE LEU GLY GLY ASP GLU LEU
SEQRES 43 A 718 SER ARG THR GLN ARG GLY ASN ASN ASN ALA PHE CYS GLN
SEQRES 44 A 718 ASP ASN GLU ILE THR TRP PHE ASP TRP ASN LEU ASP GLU
SEQRES 45 A 718 ARG LYS SER LYS PHE LEU GLU PHE VAL LYS LYS MET ILE
SEQRES 46 A 718 GLN PHE TYR ARG ALA HIS PRO ALA PHE ARG ARG GLU ARG
SEQRES 47 A 718 TYR PHE GLN GLY LYS LYS LEU PHE GLY MET PRO LEU LYS
SEQRES 48 A 718 ASP VAL THR PHE TYR THR LEU GLU GLY ARG GLU VAL ASP
SEQRES 49 A 718 GLU LYS THR TRP SER SER PRO THR GLN LEU VAL ILE PHE
SEQRES 50 A 718 VAL LEU GLU GLY SER VAL MET ASP GLU ILE ASN MET TYR
SEQRES 51 A 718 GLY GLU ARG ILE ALA ASP ASP SER PHE LEU ILE ILE LEU
SEQRES 52 A 718 ASN ALA ASN PRO ASN ASN VAL LYS VAL LYS PHE PRO LYS
SEQRES 53 A 718 GLY LYS TRP GLU LEU VAL ILE SER SER TYR LEU ARG GLU
SEQRES 54 A 718 ILE LYS PRO GLU GLU ARG ILE ILE GLU GLY GLU LYS GLU
SEQRES 55 A 718 LEU GLU ILE GLU GLY ARG THR ALA LEU VAL TYR ARG ARG
SEQRES 56 A 718 ILE GLU LEU
SEQRES 1 B 718 MET ALA LEU PHE PHE ARG THR ARG ASP ARG PRO LEU ARG
SEQRES 2 B 718 PRO GLY ASP PRO TYR PRO LEU GLY SER ASN TRP ILE GLU
SEQRES 3 B 718 ASP ASP ASP GLY VAL ASN PHE SER LEU PHE SER GLU ASN
SEQRES 4 B 718 ALA GLU LYS VAL GLU LEU LEU LEU TYR SER LEU THR ASN
SEQRES 5 B 718 GLN LYS TYR PRO LYS GLU ILE ILE GLU VAL LYS ASN LYS
SEQRES 6 B 718 THR GLY ASP ILE TRP HIS VAL PHE VAL PRO GLY LEU ARG
SEQRES 7 B 718 PRO GLY GLN LEU TYR ALA TYR ARG VAL TYR GLY PRO TYR
SEQRES 8 B 718 LYS PRO GLU LEU GLY LEU ARG PHE ASN PRO ASN LYS VAL
SEQRES 9 B 718 LEU ILE ASP PRO TYR ALA LYS ALA ILE ASN GLY SER VAL
SEQRES 10 B 718 ILE TRP ASN ASP ALA VAL PHE GLY TYR LYS ILE GLY ASP
SEQRES 11 B 718 GLN ASN GLN ASP LEU THR TYR ASP GLU ARG ASP SER GLY
SEQRES 12 B 718 GLU TYR VAL PRO LYS SER VAL VAL ILE ASN PRO TYR PHE
SEQRES 13 B 718 GLU TRP ASP ASP GLU ASP PHE ILE LYS GLY LYS LYS VAL
SEQRES 14 B 718 PRO LEU LYS ASP THR VAL ILE TYR GLU VAL HIS VAL LYS
SEQRES 15 B 718 GLY PHE THR LYS LEU ARG LEU ASP LEU PRO GLU ASN ILE
SEQRES 16 B 718 ARG GLY THR TYR GLU GLY LEU ALA SER GLU GLN MET ILE
SEQRES 17 B 718 SER TYR LEU LYS ASP LEU GLY ILE THR THR VAL GLU LEU
SEQRES 18 B 718 MET PRO VAL PHE HIS PHE ILE ASP GLN ARG PHE LEU THR
SEQRES 19 B 718 ASP LYS GLY LEU THR ASN TYR TRP GLY TYR ASP PRO ILE
SEQRES 20 B 718 ASN PHE PHE SER PRO GLU CYS ARG TYR SER SER THR GLY
SEQRES 21 B 718 CYS LEU GLY GLY GLN VAL LEU SER PHE LYS LYS MET VAL
SEQRES 22 B 718 ASN GLU LEU HIS ASN ALA GLY ILE GLU VAL ILE ILE ASP
SEQRES 23 B 718 VAL VAL TYR ASN HIS THR ALA GLU GLY ASN HIS LEU GLY
SEQRES 24 B 718 PRO THR LEU SER PHE ARG GLY ILE ASP ASN THR ALA TYR
SEQRES 25 B 718 TYR MET LEU GLN PRO ASP ASN LYS ARG TYR TYR LEU ASP
SEQRES 26 B 718 PHE THR GLY THR GLY ASN THR LEU ASN LEU SER HIS PRO
SEQRES 27 B 718 ARG VAL ILE GLN MET VAL LEU ASP SER LEU ARG TYR TRP
SEQRES 28 B 718 VAL THR GLU MET HIS VAL ASP GLY PHE ARG PHE ASP LEU
SEQRES 29 B 718 ALA ALA ALA LEU ALA ARG GLU LEU TYR SER VAL ASN MET
SEQRES 30 B 718 LEU ASN THR PHE PHE ILE ALA LEU GLN GLN ASP PRO ILE
SEQRES 31 B 718 LEU SER GLN VAL LYS LEU ILE ALA GLU PRO TRP ASP VAL
SEQRES 32 B 718 GLY GLN GLY GLY TYR GLN VAL GLY ASN PHE PRO TYR GLN
SEQRES 33 B 718 TRP ALA GLU TRP ASN GLY LYS TYR ARG ASP SER ILE ARG
SEQRES 34 B 718 ARG PHE TRP ARG GLY GLU ALA LEU PRO TYR SER GLU ILE
SEQRES 35 B 718 ALA ASN ARG LEU LEU GLY SER PRO ASP ILE TYR LEU GLY
SEQRES 36 B 718 ASN ASN LYS THR PRO PHE ALA SER ILE ASN TYR VAL THR
SEQRES 37 B 718 SER HIS ASP GLY PHE THR LEU GLU ASP LEU VAL SER TYR
SEQRES 38 B 718 ASN GLN LYS HIS ASN GLU ALA ASN GLY PHE ASN ASN GLN
SEQRES 39 B 718 ASP GLY MET ASN GLU ASN TYR SER TRP ASN CYS GLY ALA
SEQRES 40 B 718 GLU GLY PRO THR ASN ASP GLN ASN VAL VAL ILE CYS ARG
SEQRES 41 B 718 GLU LYS GLN LYS ARG ASN PHE MET ILE THR LEU LEU VAL
SEQRES 42 B 718 SER GLN GLY THR PRO MET ILE LEU GLY GLY ASP GLU LEU
SEQRES 43 B 718 SER ARG THR GLN ARG GLY ASN ASN ASN ALA PHE CYS GLN
SEQRES 44 B 718 ASP ASN GLU ILE THR TRP PHE ASP TRP ASN LEU ASP GLU
SEQRES 45 B 718 ARG LYS SER LYS PHE LEU GLU PHE VAL LYS LYS MET ILE
SEQRES 46 B 718 GLN PHE TYR ARG ALA HIS PRO ALA PHE ARG ARG GLU ARG
SEQRES 47 B 718 TYR PHE GLN GLY LYS LYS LEU PHE GLY MET PRO LEU LYS
SEQRES 48 B 718 ASP VAL THR PHE TYR THR LEU GLU GLY ARG GLU VAL ASP
SEQRES 49 B 718 GLU LYS THR TRP SER SER PRO THR GLN LEU VAL ILE PHE
SEQRES 50 B 718 VAL LEU GLU GLY SER VAL MET ASP GLU ILE ASN MET TYR
SEQRES 51 B 718 GLY GLU ARG ILE ALA ASP ASP SER PHE LEU ILE ILE LEU
SEQRES 52 B 718 ASN ALA ASN PRO ASN ASN VAL LYS VAL LYS PHE PRO LYS
SEQRES 53 B 718 GLY LYS TRP GLU LEU VAL ILE SER SER TYR LEU ARG GLU
SEQRES 54 B 718 ILE LYS PRO GLU GLU ARG ILE ILE GLU GLY GLU LYS GLU
SEQRES 55 B 718 LEU GLU ILE GLU GLY ARG THR ALA LEU VAL TYR ARG ARG
SEQRES 56 B 718 ILE GLU LEU
HET GLC A1719 12
HET GLC A1720 12
HET GLC A1721 12
HET A16 A1722 32
HET SO4 A1723 5
HET GOL A1724 6
HET GLC B1719 12
HET A16 B1720 32
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM A16 4-O-(4,6-DIDEOXY-4-{[(1S,2S,3S,4R,5S)-2,3,4-TRIHYDROXY-
HETNAM 2 A16 5-(HYDROXYMETHYL)CYCLOHEXYL]AMINO}-ALPHA-D-
HETNAM 3 A16 GLUCOPYRANOSYL)-BETA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GLC 4(C6 H12 O6)
FORMUL 6 A16 2(C19 H35 N O13)
FORMUL 7 SO4 O4 S 2-
FORMUL 8 GOL C3 H8 O3
FORMUL 11 HOH *401(H2 O)
HELIX 1 1 GLU A 26 ASP A 28 5 3
HELIX 2 2 ASN A 120 PHE A 124 5 5
HELIX 3 3 ASP A 160 LYS A 165 5 6
HELIX 4 4 THR A 198 ALA A 203 1 6
HELIX 5 5 SER A 204 GLY A 215 1 12
HELIX 6 6 GLN A 230 ASP A 235 1 6
HELIX 7 7 GLU A 253 SER A 257 5 5
HELIX 8 8 GLY A 263 ASN A 278 1 16
HELIX 9 9 SER A 303 ASN A 309 1 7
HELIX 10 10 HIS A 337 GLU A 354 1 18
HELIX 11 11 LEU A 364 ALA A 369 5 6
HELIX 12 12 ASN A 379 ASP A 388 1 10
HELIX 13 13 ILE A 390 VAL A 394 5 5
HELIX 14 14 ASN A 421 GLY A 434 1 14
HELIX 15 15 TYR A 439 LEU A 447 1 9
HELIX 16 16 SER A 449 LEU A 454 1 6
HELIX 17 17 GLY A 455 ASN A 457 5 3
HELIX 18 18 THR A 459 PHE A 461 5 3
HELIX 19 19 THR A 474 VAL A 479 1 6
HELIX 20 20 ASN A 486 GLY A 490 5 5
HELIX 21 21 ASP A 513 LEU A 532 1 20
HELIX 22 22 ASP A 571 HIS A 591 1 21
HELIX 23 23 PRO A 592 ARG A 595 5 4
HELIX 24 24 SER A 642 MET A 644 5 3
HELIX 25 25 GLU B 26 ASP B 28 5 3
HELIX 26 26 ASN B 120 PHE B 124 5 5
HELIX 27 27 ASN B 132 THR B 136 5 5
HELIX 28 28 SER B 142 VAL B 146 5 5
HELIX 29 29 PRO B 170 THR B 174 5 5
HELIX 30 30 HIS B 180 LEU B 187 1 8
HELIX 31 31 THR B 198 ALA B 203 1 6
HELIX 32 32 SER B 204 GLY B 215 1 12
HELIX 33 33 GLN B 230 ASP B 235 1 6
HELIX 34 34 GLU B 253 SER B 257 5 5
HELIX 35 35 GLY B 263 ALA B 279 1 17
HELIX 36 36 SER B 303 ASP B 308 1 6
HELIX 37 37 ASP B 308 TYR B 313 1 6
HELIX 38 38 HIS B 337 GLU B 354 1 18
HELIX 39 39 LEU B 364 ALA B 369 5 6
HELIX 40 40 ASN B 379 ASP B 388 1 10
HELIX 41 41 ASN B 421 GLY B 434 1 14
HELIX 42 42 TYR B 439 LEU B 447 1 9
HELIX 43 43 SER B 449 LEU B 454 1 6
HELIX 44 44 THR B 459 PHE B 461 5 3
HELIX 45 45 THR B 474 VAL B 479 1 6
HELIX 46 46 ASN B 486 GLY B 490 5 5
HELIX 47 47 ASP B 513 LEU B 532 1 20
HELIX 48 48 ASP B 571 ARG B 589 1 19
HELIX 49 49 GLU B 625 SER B 630 1 6
HELIX 50 50 GLY B 641 MET B 644 5 4
HELIX 51 51 LYS B 691 GLU B 694 5 4
SHEET 1 AA 4 GLY A 21 ILE A 25 0
SHEET 2 AA 4 GLY A 30 PHE A 36 -1 O GLY A 30 N ILE A 25
SHEET 3 AA 4 ILE A 69 PRO A 75 -1 O TRP A 70 N LEU A 35
SHEET 4 AA 4 ASN A 64 LYS A 65 -1 O ASN A 64 N HIS A 71
SHEET 1 AB 4 GLU A 58 VAL A 62 0
SHEET 2 AB 4 LYS A 42 LEU A 47 -1 O VAL A 43 N VAL A 62
SHEET 3 AB 4 LEU A 82 TYR A 88 -1 O ALA A 84 N LEU A 46
SHEET 4 AB 4 SER A 149 VAL A 150 -1 O SER A 149 N TYR A 83
SHEET 1 AC 9 ILE A 176 VAL A 179 0
SHEET 2 AC 9 THR A 218 LEU A 221 1 O THR A 218 N TYR A 177
SHEET 3 AC 9 GLU A 282 VAL A 287 1 O GLU A 282 N VAL A 219
SHEET 4 AC 9 GLY A 359 PHE A 362 1 O GLY A 359 N ILE A 285
SHEET 5 AC 9 LYS A 395 ALA A 398 1 O LYS A 395 N PHE A 360
SHEET 6 AC 9 TRP A 417 TRP A 420 1 O ALA A 418 N ALA A 398
SHEET 7 AC 9 SER A 463 ASN A 465 1 N ILE A 464 O GLU A 419
SHEET 8 AC 9 THR A 537 LEU A 541 1 O THR A 537 N ASN A 465
SHEET 9 AC 9 ILE A 176 VAL A 179 1 O ILE A 176 N ILE A 540
SHEET 1 AD 2 LEU A 437 PRO A 438 0
SHEET 2 AD 2 PRO A 631 THR A 632 -1 O THR A 632 N LEU A 437
SHEET 1 AE 5 VAL A 613 TYR A 616 0
SHEET 2 AE 5 LEU A 634 GLU A 640 -1 O ILE A 636 N TYR A 616
SHEET 3 AE 5 SER A 658 ASN A 664 -1 O PHE A 659 N LEU A 639
SHEET 4 AE 5 THR A 709 GLU A 717 -1 O THR A 709 N ASN A 664
SHEET 5 AE 5 LYS A 678 SER A 684 -1 O LYS A 678 N ILE A 716
SHEET 1 AF 2 VAL A 670 LYS A 673 0
SHEET 2 AF 2 GLU A 702 ILE A 705 -1 O LEU A 703 N VAL A 672
SHEET 1 BA 3 GLY B 21 ILE B 25 0
SHEET 2 BA 3 GLY B 30 PHE B 36 -1 O GLY B 30 N ILE B 25
SHEET 3 BA 3 ILE B 69 PRO B 75 -1 O TRP B 70 N LEU B 35
SHEET 1 BB 5 GLU B 58 GLU B 61 0
SHEET 2 BB 5 LYS B 42 TYR B 48 -1 O LEU B 45 N ILE B 60
SHEET 3 BB 5 LEU B 82 TYR B 88 -1 O LEU B 82 N TYR B 48
SHEET 4 BB 5 LYS B 148 VAL B 150 -1 O SER B 149 N TYR B 83
SHEET 5 BB 5 ILE B 113 ASN B 114 -1 O ASN B 114 N LYS B 148
SHEET 1 BC 2 TYR B 91 LYS B 92 0
SHEET 2 BC 2 LEU B 97 ARG B 98 -1 O LEU B 97 N LYS B 92
SHEET 1 BD 9 ILE B 176 VAL B 179 0
SHEET 2 BD 9 THR B 218 LEU B 221 1 O THR B 218 N TYR B 177
SHEET 3 BD 9 GLU B 282 VAL B 287 1 O GLU B 282 N VAL B 219
SHEET 4 BD 9 GLY B 359 PHE B 362 1 O GLY B 359 N ILE B 285
SHEET 5 BD 9 LYS B 395 ALA B 398 1 O LYS B 395 N PHE B 360
SHEET 6 BD 9 TRP B 417 TRP B 420 1 O ALA B 418 N ALA B 398
SHEET 7 BD 9 SER B 463 ASN B 465 1 N ILE B 464 O GLU B 419
SHEET 8 BD 9 THR B 537 LEU B 541 1 O THR B 537 N ASN B 465
SHEET 9 BD 9 ILE B 176 VAL B 179 1 O ILE B 176 N ILE B 540
SHEET 1 BE 2 LEU B 437 PRO B 438 0
SHEET 2 BE 2 PRO B 631 THR B 632 -1 O THR B 632 N LEU B 437
SHEET 1 BF 6 VAL B 613 TYR B 616 0
SHEET 2 BF 6 LEU B 634 LEU B 639 -1 O ILE B 636 N TYR B 616
SHEET 3 BF 6 PHE B 659 ASN B 664 -1 O PHE B 659 N LEU B 639
SHEET 4 BF 6 THR B 709 GLU B 717 -1 O THR B 709 N ASN B 664
SHEET 5 BF 6 LYS B 678 SER B 684 -1 O LYS B 678 N GLU B 717
SHEET 6 BF 6 ILE B 696 GLU B 698 -1 O ILE B 697 N TRP B 679
SHEET 1 BG 2 VAL B 670 LYS B 673 0
SHEET 2 BG 2 GLU B 702 ILE B 705 -1 O LEU B 703 N VAL B 672
SSBOND 1 CYS A 254 CYS A 261 1555 1555 2.28
SSBOND 2 CYS A 505 CYS A 519 1555 1555 2.43
SSBOND 3 CYS B 254 CYS B 261 1555 1555 2.18
SSBOND 4 CYS B 505 CYS B 519 1555 1555 2.33
LINK OD2 ASP A 363 C1C A16 A1722 1555 1555 1.40
LINK OD2 ASP B 363 C1C A16 B1720 1555 1555 1.39
CISPEP 1 TYR A 18 PRO A 19 0 20.18
CISPEP 2 TYR B 18 PRO B 19 0 -7.21
CRYST1 204.814 204.814 89.558 90.00 90.00 120.00 P 3 2 1 12
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 0.004882 0.002819 0.000000 0.00000
SCALE2 0.000000 0.005638 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011166 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
