HEADER HYDROLASE 17-MAR-17 5NGK
TITLE THE ENDO-BETA1,6-GLUCANASE BT3312
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOSYLCERAMIDASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: BT3312;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES THETAIOTAOMICRON;
SOURCE 3 ORGANISM_TAXID: 818;
SOURCE 4 GENE: ERS852430_01553;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GLYCOSIDE HYDROLASE, ENDO-BETA1, 6-CLUCANASE, BETA-1, 6-GLUCAN,
KEYWDS 2 BACTEROIDES, HUMAN GUT MICROBIOTA, YEAST GLYCAN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.BASLE,M.TEMPLE,F.CUSKIN,E.LOWE,H.GILBERT
REVDAT 4 17-JAN-24 5NGK 1 REMARK
REVDAT 3 05-JUL-17 5NGK 1 JRNL
REVDAT 2 17-MAY-17 5NGK 1 JRNL
REVDAT 1 10-MAY-17 5NGK 0
JRNL AUTH M.J.TEMPLE,F.CUSKIN,A.BASLE,N.HICKEY,G.SPECIALE,
JRNL AUTH 2 S.J.WILLIAMS,H.J.GILBERT,E.C.LOWE
JRNL TITL A BACTEROIDETES LOCUS DEDICATED TO FUNGAL 1,6-BETA-GLUCAN
JRNL TITL 2 DEGRADATION: UNIQUE SUBSTRATE CONFORMATION DRIVES
JRNL TITL 3 SPECIFICITY OF THE KEY ENDO-1,6-BETA-GLUCANASE.
JRNL REF J. BIOL. CHEM. V. 292 10639 2017
JRNL REFN ESSN 1083-351X
JRNL PMID 28461332
JRNL DOI 10.1074/JBC.M117.787606
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.24
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 108363
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 : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 5560
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7243
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.41
REMARK 3 BIN R VALUE (WORKING SET) : 0.3410
REMARK 3 BIN FREE R VALUE SET COUNT : 362
REMARK 3 BIN FREE R VALUE : 0.3470
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10808
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 607
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.58
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.42000
REMARK 3 B22 (A**2) : 3.21000
REMARK 3 B33 (A**2) : 1.28000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.43000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.151
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.139
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.126
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.701
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11075 ; 0.013 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 9777 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15049 ; 1.526 ; 1.939
REMARK 3 BOND ANGLES OTHERS (DEGREES): 22763 ; 0.986 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1363 ; 7.014 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 529 ;35.640 ;24.726
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1803 ;13.320 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ;15.432 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1631 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12434 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2294 ; 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): 5464 ; 2.161 ; 3.276
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5463 ; 2.159 ; 3.275
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6820 ; 3.124 ; 4.901
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 6821 ; 3.124 ; 4.902
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5611 ; 2.531 ; 3.522
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 5611 ; 2.531 ; 3.522
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 8229 ; 3.856 ; 5.185
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 12777 ; 5.247 ;38.173
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 12693 ; 5.222 ;38.068
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 : NULL
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 5NGK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1200003627.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JAN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 114209
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 48.240
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
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: 3RIL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM SODIUM BROMIDE 100 MM BIS TRIS
REMARK 280 PROPANE PH 6.5 AND 20 % PEG 3350., VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 78.00050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 MET A 3
REMARK 465 GLY A 4
REMARK 465 SER A 5
REMARK 465 SER A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 HIS A 11
REMARK 465 HIS A 12
REMARK 465 SER A 13
REMARK 465 SER A 14
REMARK 465 GLY A 15
REMARK 465 PRO A 16
REMARK 465 GLN A 17
REMARK 465 GLN A 18
REMARK 465 GLY A 19
REMARK 465 LEU A 20
REMARK 465 ARG A 21
REMARK 465 SER A 22
REMARK 465 ASN A 23
REMARK 465 SER A 24
REMARK 465 ASP A 25
REMARK 465 ASP A 26
REMARK 465 ALA A 27
REMARK 465 GLU A 28
REMARK 465 LYS A 29
REMARK 465 PRO A 30
REMARK 465 VAL A 31
REMARK 465 VAL A 32
REMARK 465 PRO A 33
REMARK 465 VAL A 34
REMARK 465 PRO A 35
REMARK 465 ASP A 63
REMARK 465 ASN A 64
REMARK 465 LYS A 496
REMARK 465 MET B 3
REMARK 465 GLY B 4
REMARK 465 SER B 5
REMARK 465 SER B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 HIS B 9
REMARK 465 HIS B 10
REMARK 465 HIS B 11
REMARK 465 HIS B 12
REMARK 465 SER B 13
REMARK 465 SER B 14
REMARK 465 GLY B 15
REMARK 465 PRO B 16
REMARK 465 GLN B 17
REMARK 465 GLN B 18
REMARK 465 GLY B 19
REMARK 465 LEU B 20
REMARK 465 ARG B 21
REMARK 465 SER B 22
REMARK 465 ASN B 23
REMARK 465 SER B 24
REMARK 465 ASP B 25
REMARK 465 ASP B 26
REMARK 465 ALA B 27
REMARK 465 GLU B 28
REMARK 465 LYS B 29
REMARK 465 PRO B 30
REMARK 465 VAL B 31
REMARK 465 VAL B 32
REMARK 465 PRO B 33
REMARK 465 VAL B 34
REMARK 465 LYS B 62
REMARK 465 ASP B 63
REMARK 465 ASN B 64
REMARK 465 LEU B 65
REMARK 465 ALA B 66
REMARK 465 PRO B 67
REMARK 465 THR B 68
REMARK 465 MET C 3
REMARK 465 GLY C 4
REMARK 465 SER C 5
REMARK 465 SER C 6
REMARK 465 HIS C 7
REMARK 465 HIS C 8
REMARK 465 HIS C 9
REMARK 465 HIS C 10
REMARK 465 HIS C 11
REMARK 465 HIS C 12
REMARK 465 SER C 13
REMARK 465 SER C 14
REMARK 465 GLY C 15
REMARK 465 PRO C 16
REMARK 465 GLN C 17
REMARK 465 GLN C 18
REMARK 465 GLY C 19
REMARK 465 LEU C 20
REMARK 465 ARG C 21
REMARK 465 SER C 22
REMARK 465 ASN C 23
REMARK 465 SER C 24
REMARK 465 ASP C 25
REMARK 465 ASP C 26
REMARK 465 ALA C 27
REMARK 465 GLU C 28
REMARK 465 LYS C 29
REMARK 465 PRO C 30
REMARK 465 VAL C 31
REMARK 465 VAL C 32
REMARK 465 PRO C 33
REMARK 465 VAL C 34
REMARK 465 LYS C 62
REMARK 465 ASP C 63
REMARK 465 ASN C 64
REMARK 465 LEU C 65
REMARK 465 ALA C 66
REMARK 465 PRO C 67
REMARK 465 THR C 68
REMARK 465 LYS C 496
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 432 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG A 432 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG B 432 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG B 432 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG C 104 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP C 286 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
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 ALA A 66 155.15 176.42
REMARK 500 TYR A 78 -135.44 -118.64
REMARK 500 CYS A 140 60.86 -162.00
REMARK 500 TYR A 157 -60.01 -123.90
REMARK 500 ARG A 193 39.35 -86.17
REMARK 500 ASN A 201 -164.18 72.18
REMARK 500 GLN A 236 132.49 -172.29
REMARK 500 ASN A 244 -172.72 68.45
REMARK 500 ALA A 262 -61.26 -141.20
REMARK 500 PHE A 279 -84.58 83.35
REMARK 500 HIS A 281 -157.93 -143.36
REMARK 500 ALA A 363 -79.96 -81.88
REMARK 500 TRP A 370 -0.78 87.51
REMARK 500 TRP A 377 -142.45 -83.20
REMARK 500 LYS A 408 -54.03 -139.72
REMARK 500 LEU B 52 47.04 39.86
REMARK 500 TYR B 78 -133.93 -116.46
REMARK 500 CYS B 140 61.64 -152.26
REMARK 500 TYR B 157 -62.00 -130.20
REMARK 500 ASN B 201 -171.22 72.64
REMARK 500 GLN B 236 132.20 -170.84
REMARK 500 ASN B 244 -172.79 65.87
REMARK 500 ALA B 262 -67.92 -134.40
REMARK 500 PHE B 279 -83.88 81.47
REMARK 500 HIS B 281 -157.22 -147.86
REMARK 500 ASP B 286 25.48 49.67
REMARK 500 ALA B 363 -78.53 -89.69
REMARK 500 TRP B 370 -4.88 91.55
REMARK 500 TRP B 377 -144.51 -78.34
REMARK 500 LYS B 408 -46.60 -147.69
REMARK 500 TYR B 438 113.84 -29.12
REMARK 500 LEU C 52 47.28 39.77
REMARK 500 ALA C 75 48.22 -96.73
REMARK 500 GLU C 76 89.97 -160.74
REMARK 500 TYR C 78 -138.18 -117.13
REMARK 500 CYS C 140 63.31 -161.16
REMARK 500 TYR C 157 -59.81 -128.24
REMARK 500 ARG C 193 35.76 -85.34
REMARK 500 ASN C 201 -170.23 65.24
REMARK 500 ASN C 244 -170.65 65.32
REMARK 500 ALA C 262 -59.95 -140.45
REMARK 500 PHE C 279 -80.95 75.43
REMARK 500 HIS C 281 -157.28 -144.91
REMARK 500 ALA C 363 -74.96 -90.66
REMARK 500 TRP C 370 -6.07 88.99
REMARK 500 TRP C 377 -136.38 -79.01
REMARK 500 LYS C 408 -47.36 -138.37
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 5NGK A 22 496 UNP A0A173SYZ2_BACT4
DBREF2 5NGK A A0A173SYZ2 19 493
DBREF1 5NGK B 22 496 UNP A0A173SYZ2_BACT4
DBREF2 5NGK B A0A173SYZ2 19 493
DBREF1 5NGK C 22 496 UNP A0A173SYZ2_BACT4
DBREF2 5NGK C A0A173SYZ2 19 493
SEQADV 5NGK MET A 3 UNP A0A173SYZ INITIATING METHIONINE
SEQADV 5NGK GLY A 4 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK SER A 5 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK SER A 6 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK HIS A 7 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK HIS A 8 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK HIS A 9 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK HIS A 10 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK HIS A 11 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK HIS A 12 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK SER A 13 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK SER A 14 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK GLY A 15 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK PRO A 16 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK GLN A 17 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK GLN A 18 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK GLY A 19 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK LEU A 20 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK ARG A 21 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK MET B 3 UNP A0A173SYZ INITIATING METHIONINE
SEQADV 5NGK GLY B 4 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK SER B 5 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK SER B 6 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK HIS B 7 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK HIS B 8 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK HIS B 9 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK HIS B 10 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK HIS B 11 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK HIS B 12 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK SER B 13 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK SER B 14 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK GLY B 15 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK PRO B 16 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK GLN B 17 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK GLN B 18 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK GLY B 19 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK LEU B 20 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK ARG B 21 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK MET C 3 UNP A0A173SYZ INITIATING METHIONINE
SEQADV 5NGK GLY C 4 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK SER C 5 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK SER C 6 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK HIS C 7 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK HIS C 8 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK HIS C 9 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK HIS C 10 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK HIS C 11 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK HIS C 12 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK SER C 13 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK SER C 14 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK GLY C 15 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK PRO C 16 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK GLN C 17 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK GLN C 18 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK GLY C 19 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK LEU C 20 UNP A0A173SYZ EXPRESSION TAG
SEQADV 5NGK ARG C 21 UNP A0A173SYZ EXPRESSION TAG
SEQRES 1 A 494 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 494 PRO GLN GLN GLY LEU ARG SER ASN SER ASP ASP ALA GLU
SEQRES 3 A 494 LYS PRO VAL VAL PRO VAL PRO THR GLY ASP VAL ALA ILE
SEQRES 4 A 494 TYR THR THR THR SER SER LEU THR ARG ASP LEU THR ARG
SEQRES 5 A 494 ASP ALA VAL ASN PHE SER PRO LYS ASP ASN LEU ALA PRO
SEQRES 6 A 494 THR THR ILE THR LEU ASN PRO ALA GLU GLN TYR GLN THR
SEQRES 7 A 494 MET ASP GLY PHE GLY ALA ALA ILE THR GLY SER THR CYS
SEQRES 8 A 494 TYR ASN LEU LEU LEU MET LYS PRO ALA ASP ARG HIS ALA
SEQRES 9 A 494 PHE LEU THR GLU THR PHE SER ASP LYS ASP GLY PHE GLY
SEQRES 10 A 494 PHE SER TYR ILE ARG ILE SER ILE GLY CYS SER ASP PHE
SEQRES 11 A 494 SER LEU SER GLU TYR THR CYS CYS ASP THR LYS GLY ILE
SEQRES 12 A 494 GLU ASN PHE ALA LEU GLN SER GLU GLU LYS ASP TYR ILE
SEQRES 13 A 494 LEU PRO ILE LEU LYS GLU ILE LEU ALA ILE ASN PRO SER
SEQRES 14 A 494 ILE LYS VAL ILE ALA ALA PRO TRP THR CYS PRO LYS TRP
SEQRES 15 A 494 MET LYS VAL LYS SER LEU THR ASP ARG THR PRO LEU ASP
SEQRES 16 A 494 SER TRP THR ASN GLY GLN LEU ASN PRO ASP TYR TYR GLN
SEQRES 17 A 494 ASP TYR ALA THR TYR PHE VAL LYS TRP ILE GLN ALA PHE
SEQRES 18 A 494 LYS ALA GLU GLY ILE ASP ILE TYR ALA VAL THR PRO GLN
SEQRES 19 A 494 ASN GLU PRO LEU ASN ARG GLY ASN SER ALA SER LEU TYR
SEQRES 20 A 494 MET GLU TRP GLU GLU GLN ARG ASP PHE VAL LYS THR ALA
SEQRES 21 A 494 LEU GLY PRO GLN MET LYS ALA ALA GLY LEU SER THR LYS
SEQRES 22 A 494 ILE TYR ALA PHE ASP HIS ASN TYR ASN TYR ASP ASN ILE
SEQRES 23 A 494 GLU SER GLN LYS ASN TYR PRO GLY LYS ILE TYR GLU ASP
SEQRES 24 A 494 ALA ALA ALA SER GLN TYR LEU ALA GLY ALA ALA TYR HIS
SEQRES 25 A 494 ASN TYR GLY GLY ASN ARG GLU GLU LEU LEU ASN ILE HIS
SEQRES 26 A 494 GLN ALA TYR PRO GLU LYS GLU LEU LEU PHE THR GLU THR
SEQRES 27 A 494 SER ILE GLY THR TRP ASN SER GLY ARG ASP LEU SER LYS
SEQRES 28 A 494 ARG LEU MET GLU ASP MET GLU GLU VAL ALA LEU GLY THR
SEQRES 29 A 494 ILE ASN ASN TRP CYS LYS GLY VAL ILE VAL TRP ASN LEU
SEQRES 30 A 494 MET LEU ASP ASN ASP ARG GLY PRO ASN ARG GLU GLY GLY
SEQRES 31 A 494 CYS GLN THR CYS TYR GLY ALA VAL ASP ILE ASN ASN SER
SEQRES 32 A 494 ASP TYR LYS THR ILE ILE ARG ASN SER HIS TYR TYR ILE
SEQRES 33 A 494 ILE ALA HIS LEU SER SER VAL VAL LYS PRO GLY ALA VAL
SEQRES 34 A 494 ARG ILE ALA THR THR GLY TYR THR ASP ASN GLY ILE THR
SEQRES 35 A 494 CYS SER ALA PHE GLU ASN THR ASP GLY THR TYR ALA PHE
SEQRES 36 A 494 VAL LEU ILE ASN ASN ASN GLU LYS SER LYS LYS ILE THR
SEQRES 37 A 494 VAL SER ASP GLY GLN ARG HIS PHE ALA TYR ASP VAL PRO
SEQRES 38 A 494 GLY LYS SER VAL THR SER TYR ARG TRP ALA LYS SER LYS
SEQRES 1 B 494 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 494 PRO GLN GLN GLY LEU ARG SER ASN SER ASP ASP ALA GLU
SEQRES 3 B 494 LYS PRO VAL VAL PRO VAL PRO THR GLY ASP VAL ALA ILE
SEQRES 4 B 494 TYR THR THR THR SER SER LEU THR ARG ASP LEU THR ARG
SEQRES 5 B 494 ASP ALA VAL ASN PHE SER PRO LYS ASP ASN LEU ALA PRO
SEQRES 6 B 494 THR THR ILE THR LEU ASN PRO ALA GLU GLN TYR GLN THR
SEQRES 7 B 494 MET ASP GLY PHE GLY ALA ALA ILE THR GLY SER THR CYS
SEQRES 8 B 494 TYR ASN LEU LEU LEU MET LYS PRO ALA ASP ARG HIS ALA
SEQRES 9 B 494 PHE LEU THR GLU THR PHE SER ASP LYS ASP GLY PHE GLY
SEQRES 10 B 494 PHE SER TYR ILE ARG ILE SER ILE GLY CYS SER ASP PHE
SEQRES 11 B 494 SER LEU SER GLU TYR THR CYS CYS ASP THR LYS GLY ILE
SEQRES 12 B 494 GLU ASN PHE ALA LEU GLN SER GLU GLU LYS ASP TYR ILE
SEQRES 13 B 494 LEU PRO ILE LEU LYS GLU ILE LEU ALA ILE ASN PRO SER
SEQRES 14 B 494 ILE LYS VAL ILE ALA ALA PRO TRP THR CYS PRO LYS TRP
SEQRES 15 B 494 MET LYS VAL LYS SER LEU THR ASP ARG THR PRO LEU ASP
SEQRES 16 B 494 SER TRP THR ASN GLY GLN LEU ASN PRO ASP TYR TYR GLN
SEQRES 17 B 494 ASP TYR ALA THR TYR PHE VAL LYS TRP ILE GLN ALA PHE
SEQRES 18 B 494 LYS ALA GLU GLY ILE ASP ILE TYR ALA VAL THR PRO GLN
SEQRES 19 B 494 ASN GLU PRO LEU ASN ARG GLY ASN SER ALA SER LEU TYR
SEQRES 20 B 494 MET GLU TRP GLU GLU GLN ARG ASP PHE VAL LYS THR ALA
SEQRES 21 B 494 LEU GLY PRO GLN MET LYS ALA ALA GLY LEU SER THR LYS
SEQRES 22 B 494 ILE TYR ALA PHE ASP HIS ASN TYR ASN TYR ASP ASN ILE
SEQRES 23 B 494 GLU SER GLN LYS ASN TYR PRO GLY LYS ILE TYR GLU ASP
SEQRES 24 B 494 ALA ALA ALA SER GLN TYR LEU ALA GLY ALA ALA TYR HIS
SEQRES 25 B 494 ASN TYR GLY GLY ASN ARG GLU GLU LEU LEU ASN ILE HIS
SEQRES 26 B 494 GLN ALA TYR PRO GLU LYS GLU LEU LEU PHE THR GLU THR
SEQRES 27 B 494 SER ILE GLY THR TRP ASN SER GLY ARG ASP LEU SER LYS
SEQRES 28 B 494 ARG LEU MET GLU ASP MET GLU GLU VAL ALA LEU GLY THR
SEQRES 29 B 494 ILE ASN ASN TRP CYS LYS GLY VAL ILE VAL TRP ASN LEU
SEQRES 30 B 494 MET LEU ASP ASN ASP ARG GLY PRO ASN ARG GLU GLY GLY
SEQRES 31 B 494 CYS GLN THR CYS TYR GLY ALA VAL ASP ILE ASN ASN SER
SEQRES 32 B 494 ASP TYR LYS THR ILE ILE ARG ASN SER HIS TYR TYR ILE
SEQRES 33 B 494 ILE ALA HIS LEU SER SER VAL VAL LYS PRO GLY ALA VAL
SEQRES 34 B 494 ARG ILE ALA THR THR GLY TYR THR ASP ASN GLY ILE THR
SEQRES 35 B 494 CYS SER ALA PHE GLU ASN THR ASP GLY THR TYR ALA PHE
SEQRES 36 B 494 VAL LEU ILE ASN ASN ASN GLU LYS SER LYS LYS ILE THR
SEQRES 37 B 494 VAL SER ASP GLY GLN ARG HIS PHE ALA TYR ASP VAL PRO
SEQRES 38 B 494 GLY LYS SER VAL THR SER TYR ARG TRP ALA LYS SER LYS
SEQRES 1 C 494 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 494 PRO GLN GLN GLY LEU ARG SER ASN SER ASP ASP ALA GLU
SEQRES 3 C 494 LYS PRO VAL VAL PRO VAL PRO THR GLY ASP VAL ALA ILE
SEQRES 4 C 494 TYR THR THR THR SER SER LEU THR ARG ASP LEU THR ARG
SEQRES 5 C 494 ASP ALA VAL ASN PHE SER PRO LYS ASP ASN LEU ALA PRO
SEQRES 6 C 494 THR THR ILE THR LEU ASN PRO ALA GLU GLN TYR GLN THR
SEQRES 7 C 494 MET ASP GLY PHE GLY ALA ALA ILE THR GLY SER THR CYS
SEQRES 8 C 494 TYR ASN LEU LEU LEU MET LYS PRO ALA ASP ARG HIS ALA
SEQRES 9 C 494 PHE LEU THR GLU THR PHE SER ASP LYS ASP GLY PHE GLY
SEQRES 10 C 494 PHE SER TYR ILE ARG ILE SER ILE GLY CYS SER ASP PHE
SEQRES 11 C 494 SER LEU SER GLU TYR THR CYS CYS ASP THR LYS GLY ILE
SEQRES 12 C 494 GLU ASN PHE ALA LEU GLN SER GLU GLU LYS ASP TYR ILE
SEQRES 13 C 494 LEU PRO ILE LEU LYS GLU ILE LEU ALA ILE ASN PRO SER
SEQRES 14 C 494 ILE LYS VAL ILE ALA ALA PRO TRP THR CYS PRO LYS TRP
SEQRES 15 C 494 MET LYS VAL LYS SER LEU THR ASP ARG THR PRO LEU ASP
SEQRES 16 C 494 SER TRP THR ASN GLY GLN LEU ASN PRO ASP TYR TYR GLN
SEQRES 17 C 494 ASP TYR ALA THR TYR PHE VAL LYS TRP ILE GLN ALA PHE
SEQRES 18 C 494 LYS ALA GLU GLY ILE ASP ILE TYR ALA VAL THR PRO GLN
SEQRES 19 C 494 ASN GLU PRO LEU ASN ARG GLY ASN SER ALA SER LEU TYR
SEQRES 20 C 494 MET GLU TRP GLU GLU GLN ARG ASP PHE VAL LYS THR ALA
SEQRES 21 C 494 LEU GLY PRO GLN MET LYS ALA ALA GLY LEU SER THR LYS
SEQRES 22 C 494 ILE TYR ALA PHE ASP HIS ASN TYR ASN TYR ASP ASN ILE
SEQRES 23 C 494 GLU SER GLN LYS ASN TYR PRO GLY LYS ILE TYR GLU ASP
SEQRES 24 C 494 ALA ALA ALA SER GLN TYR LEU ALA GLY ALA ALA TYR HIS
SEQRES 25 C 494 ASN TYR GLY GLY ASN ARG GLU GLU LEU LEU ASN ILE HIS
SEQRES 26 C 494 GLN ALA TYR PRO GLU LYS GLU LEU LEU PHE THR GLU THR
SEQRES 27 C 494 SER ILE GLY THR TRP ASN SER GLY ARG ASP LEU SER LYS
SEQRES 28 C 494 ARG LEU MET GLU ASP MET GLU GLU VAL ALA LEU GLY THR
SEQRES 29 C 494 ILE ASN ASN TRP CYS LYS GLY VAL ILE VAL TRP ASN LEU
SEQRES 30 C 494 MET LEU ASP ASN ASP ARG GLY PRO ASN ARG GLU GLY GLY
SEQRES 31 C 494 CYS GLN THR CYS TYR GLY ALA VAL ASP ILE ASN ASN SER
SEQRES 32 C 494 ASP TYR LYS THR ILE ILE ARG ASN SER HIS TYR TYR ILE
SEQRES 33 C 494 ILE ALA HIS LEU SER SER VAL VAL LYS PRO GLY ALA VAL
SEQRES 34 C 494 ARG ILE ALA THR THR GLY TYR THR ASP ASN GLY ILE THR
SEQRES 35 C 494 CYS SER ALA PHE GLU ASN THR ASP GLY THR TYR ALA PHE
SEQRES 36 C 494 VAL LEU ILE ASN ASN ASN GLU LYS SER LYS LYS ILE THR
SEQRES 37 C 494 VAL SER ASP GLY GLN ARG HIS PHE ALA TYR ASP VAL PRO
SEQRES 38 C 494 GLY LYS SER VAL THR SER TYR ARG TRP ALA LYS SER LYS
FORMUL 4 HOH *607(H2 O)
HELIX 1 AA1 THR A 89 MET A 99 1 11
HELIX 2 AA2 LYS A 100 SER A 113 1 14
HELIX 3 AA3 GLY A 144 PHE A 148 5 5
HELIX 4 AA4 GLN A 151 TYR A 157 1 7
HELIX 5 AA5 TYR A 157 ASN A 169 1 13
HELIX 6 AA6 PRO A 182 TRP A 184 5 3
HELIX 7 AA7 TYR A 208 GLU A 226 1 19
HELIX 8 AA8 GLU A 251 ALA A 262 1 12
HELIX 9 AA9 ALA A 262 ALA A 270 1 9
HELIX 10 AB1 ASN A 284 LYS A 292 5 9
HELIX 11 AB2 ASN A 293 GLU A 300 1 8
HELIX 12 AB3 ASP A 301 GLN A 306 1 6
HELIX 13 AB4 ARG A 320 TYR A 330 1 11
HELIX 14 AB5 TRP A 345 SER A 347 5 3
HELIX 15 AB6 ASP A 350 VAL A 362 1 13
HELIX 16 AB7 ALA A 363 ASN A 368 1 6
HELIX 17 AB8 ASN A 413 SER A 424 1 12
HELIX 18 AB9 THR B 89 MET B 99 1 11
HELIX 19 AC1 LYS B 100 SER B 113 1 14
HELIX 20 AC2 GLY B 144 PHE B 148 5 5
HELIX 21 AC3 GLN B 151 TYR B 157 1 7
HELIX 22 AC4 TYR B 157 ASN B 169 1 13
HELIX 23 AC5 PRO B 182 TRP B 184 5 3
HELIX 24 AC6 TYR B 208 GLU B 226 1 19
HELIX 25 AC7 GLU B 251 ALA B 262 1 12
HELIX 26 AC8 ALA B 262 ALA B 270 1 9
HELIX 27 AC9 ASN B 284 LYS B 292 5 9
HELIX 28 AD1 ASN B 293 GLU B 300 1 8
HELIX 29 AD2 ASP B 301 GLN B 306 1 6
HELIX 30 AD3 ARG B 320 TYR B 330 1 11
HELIX 31 AD4 TRP B 345 SER B 347 5 3
HELIX 32 AD5 ASP B 350 VAL B 362 1 13
HELIX 33 AD6 ALA B 363 ASN B 368 1 6
HELIX 34 AD7 ASN B 413 SER B 424 1 12
HELIX 35 AD8 THR C 89 MET C 99 1 11
HELIX 36 AD9 LYS C 100 SER C 113 1 14
HELIX 37 AE1 GLY C 144 PHE C 148 5 5
HELIX 38 AE2 GLN C 151 TYR C 157 1 7
HELIX 39 AE3 TYR C 157 ASN C 169 1 13
HELIX 40 AE4 PRO C 182 TRP C 184 5 3
HELIX 41 AE5 TYR C 208 GLU C 226 1 19
HELIX 42 AE6 GLU C 251 ALA C 262 1 12
HELIX 43 AE7 ALA C 262 ALA C 270 1 9
HELIX 44 AE8 ASN C 284 LYS C 292 5 9
HELIX 45 AE9 ASN C 293 GLU C 300 1 8
HELIX 46 AF1 ASP C 301 GLN C 306 1 6
HELIX 47 AF2 GLU C 321 TYR C 330 1 10
HELIX 48 AF3 GLY C 343 SER C 347 5 5
HELIX 49 AF4 ASP C 350 VAL C 362 1 13
HELIX 50 AF5 ALA C 363 ASN C 368 1 6
HELIX 51 AF6 ASN C 413 SER C 424 1 12
SHEET 1 AA1 9 THR A 53 VAL A 57 0
SHEET 2 AA1 9 VAL A 39 THR A 45 -1 N VAL A 39 O VAL A 57
SHEET 3 AA1 9 SER A 486 ALA A 493 -1 O VAL A 487 N THR A 44
SHEET 4 AA1 9 THR A 454 ASN A 461 -1 N TYR A 455 O TRP A 492
SHEET 5 AA1 9 ILE A 443 GLU A 449 -1 N THR A 444 O ILE A 460
SHEET 6 AA1 9 VAL A 431 GLY A 437 -1 N VAL A 431 O GLU A 449
SHEET 7 AA1 9 THR A 69 THR A 80 -1 N THR A 71 O THR A 436
SHEET 8 AA1 9 LYS A 467 SER A 472 1 O SER A 472 N LEU A 72
SHEET 9 AA1 9 HIS A 477 VAL A 482 -1 O VAL A 482 N LYS A 467
SHEET 1 AA2 9 GLY A 83 ALA A 87 0
SHEET 2 AA2 9 TYR A 122 ILE A 127 1 N TYR A 122 O PHE A 84
SHEET 3 AA2 9 LYS A 173 PRO A 178 1 O LYS A 173 N ILE A 123
SHEET 4 AA2 9 ALA A 232 VAL A 233 1 O ALA A 232 N VAL A 174
SHEET 5 AA2 9 LYS A 275 ASN A 282 1 O TYR A 277 N VAL A 233
SHEET 6 AA2 9 GLY A 310 HIS A 314 1 O GLY A 310 N ALA A 278
SHEET 7 AA2 9 GLU A 334 GLU A 339 1 O GLU A 334 N ALA A 311
SHEET 8 AA2 9 GLY A 373 ASN A 378 1 O GLY A 373 N PHE A 337
SHEET 9 AA2 9 GLY A 83 ALA A 87 1 N ALA A 87 O TRP A 377
SHEET 1 AA3 2 LYS A 186 VAL A 187 0
SHEET 2 AA3 2 GLN A 203 LEU A 204 -1 O GLN A 203 N VAL A 187
SHEET 1 AA4 2 ILE A 342 GLY A 343 0
SHEET 2 AA4 2 CYS A 396 TYR A 397 -1 O TYR A 397 N ILE A 342
SHEET 1 AA5 3 MET A 380 ASP A 382 0
SHEET 2 AA5 3 VAL A 400 ILE A 402 1 O ILE A 402 N LEU A 381
SHEET 3 AA5 3 ILE A 410 ARG A 412 -1 O ILE A 411 N ASP A 401
SHEET 1 AA6 9 THR B 53 VAL B 57 0
SHEET 2 AA6 9 VAL B 39 THR B 45 -1 N VAL B 39 O VAL B 57
SHEET 3 AA6 9 SER B 486 ALA B 493 -1 O ARG B 491 N ALA B 40
SHEET 4 AA6 9 THR B 454 ASN B 461 -1 N TYR B 455 O TRP B 492
SHEET 5 AA6 9 ILE B 443 GLU B 449 -1 N THR B 444 O ILE B 460
SHEET 6 AA6 9 VAL B 431 GLY B 437 -1 N VAL B 431 O GLU B 449
SHEET 7 AA6 9 ILE B 70 THR B 80 -1 N TYR B 78 O ARG B 432
SHEET 8 AA6 9 LYS B 467 SER B 472 1 O SER B 472 N LEU B 72
SHEET 9 AA6 9 HIS B 477 VAL B 482 -1 O VAL B 482 N LYS B 467
SHEET 1 AA7 9 GLY B 83 ALA B 87 0
SHEET 2 AA7 9 TYR B 122 ILE B 127 1 N TYR B 122 O PHE B 84
SHEET 3 AA7 9 LYS B 173 PRO B 178 1 O LYS B 173 N ILE B 123
SHEET 4 AA7 9 ALA B 232 VAL B 233 1 O ALA B 232 N VAL B 174
SHEET 5 AA7 9 LYS B 275 ASN B 282 1 O TYR B 277 N VAL B 233
SHEET 6 AA7 9 GLY B 310 HIS B 314 1 O ALA B 312 N ALA B 278
SHEET 7 AA7 9 GLU B 334 GLU B 339 1 O LEU B 336 N TYR B 313
SHEET 8 AA7 9 GLY B 373 ASN B 378 1 O ILE B 375 N PHE B 337
SHEET 9 AA7 9 GLY B 83 ALA B 87 1 N ALA B 87 O TRP B 377
SHEET 1 AA8 2 LYS B 186 VAL B 187 0
SHEET 2 AA8 2 GLN B 203 LEU B 204 -1 O GLN B 203 N VAL B 187
SHEET 1 AA9 2 ILE B 342 GLY B 343 0
SHEET 2 AA9 2 CYS B 396 TYR B 397 -1 O TYR B 397 N ILE B 342
SHEET 1 AB1 3 MET B 380 ASP B 382 0
SHEET 2 AB1 3 VAL B 400 ILE B 402 1 O ILE B 402 N LEU B 381
SHEET 3 AB1 3 ILE B 410 ARG B 412 -1 O ILE B 411 N ASP B 401
SHEET 1 AB2 9 THR C 53 VAL C 57 0
SHEET 2 AB2 9 VAL C 39 THR C 45 -1 N THR C 43 O THR C 53
SHEET 3 AB2 9 SER C 486 ALA C 493 -1 O ARG C 491 N ALA C 40
SHEET 4 AB2 9 THR C 454 ASN C 461 -1 N TYR C 455 O TRP C 492
SHEET 5 AB2 9 ILE C 443 GLU C 449 -1 N THR C 444 O ILE C 460
SHEET 6 AB2 9 ALA C 430 THR C 436 -1 N ILE C 433 O ALA C 447
SHEET 7 AB2 9 ILE C 70 MET C 81 -1 N TYR C 78 O ARG C 432
SHEET 8 AB2 9 LYS C 467 SER C 472 1 O SER C 472 N LEU C 72
SHEET 9 AB2 9 HIS C 477 VAL C 482 -1 O VAL C 482 N LYS C 467
SHEET 1 AB3 2 GLY C 83 ALA C 87 0
SHEET 2 AB3 2 GLY C 373 ASN C 378 1 O TRP C 377 N ALA C 87
SHEET 1 AB4 6 TYR C 122 ILE C 127 0
SHEET 2 AB4 6 LYS C 173 PRO C 178 1 O LYS C 173 N ILE C 123
SHEET 3 AB4 6 ALA C 232 VAL C 233 1 O ALA C 232 N VAL C 174
SHEET 4 AB4 6 LYS C 275 ASN C 282 1 O LYS C 275 N VAL C 233
SHEET 5 AB4 6 GLY C 310 HIS C 314 1 O ALA C 312 N ALA C 278
SHEET 6 AB4 6 GLU C 334 GLU C 339 1 O LEU C 336 N TYR C 313
SHEET 1 AB5 2 LYS C 186 VAL C 187 0
SHEET 2 AB5 2 GLN C 203 LEU C 204 -1 O GLN C 203 N VAL C 187
SHEET 1 AB6 3 MET C 380 ASP C 382 0
SHEET 2 AB6 3 VAL C 400 ILE C 402 1 O ILE C 402 N LEU C 381
SHEET 3 AB6 3 ILE C 410 ARG C 412 -1 O ILE C 411 N ASP C 401
SSBOND 1 CYS A 393 CYS A 396 1555 1555 2.13
SSBOND 2 CYS B 393 CYS B 396 1555 1555 2.10
SSBOND 3 CYS C 393 CYS C 396 1555 1555 2.10
CISPEP 1 GLY A 386 PRO A 387 0 4.76
CISPEP 2 GLY B 386 PRO B 387 0 -3.39
CISPEP 3 GLY C 386 PRO C 387 0 -4.16
CRYST1 62.418 156.001 78.050 90.00 100.41 90.00 P 1 21 1 6
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 0.016021 0.000000 0.002944 0.00000
SCALE2 0.000000 0.006410 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013027 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
