HEADER TRANSFERASE 08-MAR-12 4AMC
TITLE CRYSTAL STRUCTURE OF LACTOBACILLUS REUTERI 121 N-TERMINALLY TRUNCATED
TITLE 2 GLUCANSUCRASE GTFA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCANSUCRASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINALLY TRUNCATED, RESIDUES 741-1781;
COMPND 5 SYNONYM: GLUCANSUCRASE GTFA;
COMPND 6 EC: 2.4.1.5;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS REUTERI;
SOURCE 3 ORGANISM_TAXID: 1598;
SOURCE 4 STRAIN: 121;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: STAR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET15B
KEYWDS TRANSFERASE, GLYCOSYLTRANSFERASE, REUTERANSUCRASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.PIJNING,A.VUJICIC-ZAGAR,S.KRALJ,L.DIJKHUIZEN,B.W.DIJKSTRA
REVDAT 4 20-DEC-23 4AMC 1 REMARK LINK
REVDAT 3 12-DEC-12 4AMC 1 JRNL
REVDAT 2 05-DEC-12 4AMC 1 JRNL
REVDAT 1 07-NOV-12 4AMC 0
JRNL AUTH T.PIJNING,A.VUJICIC-ZAGAR,S.KRALJ,L.DIJKHUIZEN,B.W.DIJKSTRA
JRNL TITL STRUCTURE OF THE ALPHA-1,6/ALPHA-1,4-SPECIFIC GLUCANSUCRASE
JRNL TITL 2 GTFA FROM LACTOBACILLUS REUTERI 121
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 68 1448 2012
JRNL REFN ESSN 1744-3091
JRNL PMID 23192022
JRNL DOI 10.1107/S1744309112044168
REMARK 2
REMARK 2 RESOLUTION. 3.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 3.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 41820
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) : 0.240
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2218
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) : 3.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2716
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.3320
REMARK 3 BIN FREE R VALUE SET COUNT : 150
REMARK 3 BIN FREE R VALUE : 0.3420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8087
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 122.9
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.85000
REMARK 3 B22 (A**2) : 4.85000
REMARK 3 B33 (A**2) : -7.28000
REMARK 3 B12 (A**2) : 2.43000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.809
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.418
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.324
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 49.556
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.921
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.903
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8270 ; 0.005 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11241 ; 0.763 ; 1.927
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1018 ; 4.084 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 449 ;37.312 ;25.501
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1316 ;13.664 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;16.176 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1194 ; 0.054 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6533 ; 0.002 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 745 A 975
REMARK 3 ORIGIN FOR THE GROUP (A): 76.8080 -6.2240 -56.7880
REMARK 3 T TENSOR
REMARK 3 T11: 0.7120 T22: 0.3228
REMARK 3 T33: 0.0873 T12: -0.1711
REMARK 3 T13: -0.0865 T23: -0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 0.4025 L22: 1.5184
REMARK 3 L33: 1.3224 L12: 0.2306
REMARK 3 L13: 0.0026 L23: 1.3311
REMARK 3 S TENSOR
REMARK 3 S11: -0.0949 S12: 0.2037 S13: -0.0250
REMARK 3 S21: -0.0199 S22: 0.0035 S23: 0.0891
REMARK 3 S31: -0.0965 S32: -0.1361 S33: 0.0913
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 976 A 1153
REMARK 3 ORIGIN FOR THE GROUP (A): 75.6080 29.3120 -14.3170
REMARK 3 T TENSOR
REMARK 3 T11: 0.6154 T22: 0.1357
REMARK 3 T33: 0.2551 T12: 0.1538
REMARK 3 T13: -0.0032 T23: 0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 0.7407 L22: 0.6709
REMARK 3 L33: 0.7446 L12: 0.5675
REMARK 3 L13: 0.2586 L23: 0.0425
REMARK 3 S TENSOR
REMARK 3 S11: -0.0270 S12: 0.0495 S13: 0.0420
REMARK 3 S21: -0.0676 S22: 0.0473 S23: -0.0315
REMARK 3 S31: -0.3213 S32: -0.1708 S33: -0.0203
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1154 A 1484
REMARK 3 ORIGIN FOR THE GROUP (A): 68.5800 24.9950 3.4630
REMARK 3 T TENSOR
REMARK 3 T11: 0.4692 T22: 0.2387
REMARK 3 T33: 0.2739 T12: 0.1721
REMARK 3 T13: 0.0495 T23: 0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 0.7885 L22: 0.6165
REMARK 3 L33: 1.6922 L12: 0.2911
REMARK 3 L13: -0.2589 L23: 0.3369
REMARK 3 S TENSOR
REMARK 3 S11: 0.0790 S12: -0.0664 S13: 0.0500
REMARK 3 S21: 0.1072 S22: 0.0092 S23: 0.2226
REMARK 3 S31: -0.1655 S32: -0.4130 S33: -0.0882
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1485 A 1763
REMARK 3 ORIGIN FOR THE GROUP (A): 76.5380 -1.0410 -53.5940
REMARK 3 T TENSOR
REMARK 3 T11: 0.7233 T22: 0.3388
REMARK 3 T33: 0.1485 T12: -0.1560
REMARK 3 T13: -0.0193 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 0.1654 L22: 0.8455
REMARK 3 L33: 1.1579 L12: 0.0510
REMARK 3 L13: 0.0477 L23: 0.9037
REMARK 3 S TENSOR
REMARK 3 S11: -0.1487 S12: 0.1675 S13: -0.0480
REMARK 3 S21: -0.1862 S22: 0.1522 S23: 0.0590
REMARK 3 S31: -0.2154 S32: -0.0245 S33: -0.0034
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES WITH TLS ADDED
REMARK 4
REMARK 4 4AMC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1290051622.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUN-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44037
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.600
REMARK 200 RESOLUTION RANGE LOW (A) : 48.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.100
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.500
REMARK 200 R MERGE (I) : 0.22000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.60
REMARK 200 R MERGE FOR SHELL (I) : 0.95000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3KLK
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 85.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 8.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M (NH4)2SO4, 0.1 M SODIUM PHOSPHATE
REMARK 280 -CITRATE BUFFER PH 4.2
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 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 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+2/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,-Z+1/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 249.33600
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 124.66800
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 249.33600
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 124.66800
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 249.33600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 124.66800
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 249.33600
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 124.66800
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 739
REMARK 465 GLY A 740
REMARK 465 ILE A 741
REMARK 465 ASN A 742
REMARK 465 GLY A 743
REMARK 465 GLN A 744
REMARK 465 ALA A 1764
REMARK 465 GLU A 1765
REMARK 465 TYR A 1766
REMARK 465 PRO A 1767
REMARK 465 THR A 1768
REMARK 465 SER A 1769
REMARK 465 THR A 1770
REMARK 465 ASP A 1771
REMARK 465 VAL A 1772
REMARK 465 GLY A 1773
REMARK 465 LYS A 1774
REMARK 465 MET A 1775
REMARK 465 LEU A 1776
REMARK 465 ASP A 1777
REMARK 465 GLN A 1778
REMARK 465 ASN A 1779
REMARK 465 LYS A 1780
REMARK 465 LEU A 1781
REMARK 465 HIS A 1782
REMARK 465 HIS A 1783
REMARK 465 HIS A 1784
REMARK 465 HIS A 1785
REMARK 465 HIS A 1786
REMARK 465 HIS A 1787
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 758 72.41 57.96
REMARK 500 SER A 804 -156.45 -152.92
REMARK 500 ASN A 814 1.10 56.47
REMARK 500 ASP A 820 46.59 -94.07
REMARK 500 THR A 833 -46.16 -136.21
REMARK 500 TYR A 959 -103.91 -99.06
REMARK 500 ARG A 964 48.80 -95.89
REMARK 500 THR A 973 -146.20 -104.43
REMARK 500 LEU A 980 -63.28 -130.43
REMARK 500 ALA A 982 -138.02 46.68
REMARK 500 ALA A1016 31.57 -95.28
REMARK 500 ALA A1025 70.87 49.66
REMARK 500 GLU A1061 51.92 -105.76
REMARK 500 ASN A1076 60.13 36.51
REMARK 500 LEU A1093 -31.36 -131.49
REMARK 500 SER A1109 -178.69 -173.52
REMARK 500 SER A1136 -54.56 -151.05
REMARK 500 THR A1154 102.71 59.25
REMARK 500 THR A1156 160.77 64.62
REMARK 500 ASN A1172 35.72 -93.30
REMARK 500 SER A1244 72.48 -113.09
REMARK 500 ASN A1250 -160.29 -77.85
REMARK 500 ILE A1251 105.43 38.19
REMARK 500 THR A1269 -146.03 -87.69
REMARK 500 HIS A1303 62.69 -118.43
REMARK 500 ASP A1334 -158.40 -96.40
REMARK 500 ASN A1349 53.87 25.33
REMARK 500 GLU A1353 62.68 60.65
REMARK 500 ALA A1354 -128.19 36.84
REMARK 500 SER A1367 67.66 -112.11
REMARK 500 ASN A1396 59.51 -101.62
REMARK 500 THR A1401 47.11 -96.64
REMARK 500 ALA A1413 45.04 -86.61
REMARK 500 ASP A1467 66.99 67.47
REMARK 500 LEU A1478 70.97 -116.77
REMARK 500 ASN A1484 -169.76 -78.76
REMARK 500 ASN A1517 85.62 46.52
REMARK 500 ILE A1541 54.87 -104.97
REMARK 500 SER A1582 -50.33 101.39
REMARK 500 ALA A1617 -178.31 -69.72
REMARK 500 GLN A1643 -156.89 -163.79
REMARK 500 ASN A1645 -159.18 -156.39
REMARK 500 GLU A1646 128.20 61.84
REMARK 500 ASN A1652 -105.14 54.00
REMARK 500 ASN A1655 -135.82 63.81
REMARK 500 ASP A1682 -159.85 -74.83
REMARK 500 GLU A1689 44.05 -146.70
REMARK 500 LYS A1691 32.88 72.16
REMARK 500 SER A1698 -143.73 52.59
REMARK 500 ILE A1756 -65.65 -93.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2764 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 978 O
REMARK 620 2 GLU A 978 OE2 90.4
REMARK 620 3 ASP A 984 OD1 72.6 113.3
REMARK 620 4 ASN A1028 O 69.9 74.1 141.8
REMARK 620 5 ASP A1513 OD2 92.8 153.8 92.5 82.7
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2764
DBREF 4AMC A 741 1781 UNP Q5SBL9 Q5SBL9_LACRE 741 1781
SEQADV 4AMC MET A 739 UNP Q5SBL9 EXPRESSION TAG
SEQADV 4AMC GLY A 740 UNP Q5SBL9 EXPRESSION TAG
SEQADV 4AMC HIS A 1782 UNP Q5SBL9 EXPRESSION TAG
SEQADV 4AMC HIS A 1783 UNP Q5SBL9 EXPRESSION TAG
SEQADV 4AMC HIS A 1784 UNP Q5SBL9 EXPRESSION TAG
SEQADV 4AMC HIS A 1785 UNP Q5SBL9 EXPRESSION TAG
SEQADV 4AMC HIS A 1786 UNP Q5SBL9 EXPRESSION TAG
SEQADV 4AMC HIS A 1787 UNP Q5SBL9 EXPRESSION TAG
SEQRES 1 A 1049 MET GLY ILE ASN GLY GLN GLN TYR TYR ILE ASP PRO THR
SEQRES 2 A 1049 THR GLY GLN PRO ARG LYS ASN PHE LEU LEU GLN SER GLY
SEQRES 3 A 1049 ASN ASN TRP ILE TYR PHE ASP SER ASP THR GLY VAL GLY
SEQRES 4 A 1049 THR ASN ALA LEU GLU LEU GLN PHE ALA LYS GLY THR VAL
SEQRES 5 A 1049 SER SER ASN GLU GLN TYR ARG ASN GLY ASN ALA ALA TYR
SEQRES 6 A 1049 SER TYR ASP ASP LYS SER ILE GLU ASN VAL ASN GLY TYR
SEQRES 7 A 1049 LEU THR ALA ASP THR TRP TYR ARG PRO LYS GLN ILE LEU
SEQRES 8 A 1049 LYS ASP GLY THR THR TRP THR ASP SER LYS GLU THR ASP
SEQRES 9 A 1049 MET ARG PRO ILE LEU MET VAL TRP TRP PRO ASN THR LEU
SEQRES 10 A 1049 THR GLN ALA TYR TYR LEU ASN TYR MET LYS GLN HIS GLY
SEQRES 11 A 1049 ASN LEU LEU PRO SER ALA LEU PRO PHE PHE ASN ALA ASP
SEQRES 12 A 1049 ALA ASP PRO ALA GLU LEU ASN HIS TYR SER GLU ILE VAL
SEQRES 13 A 1049 GLN GLN ASN ILE GLU LYS ARG ILE SER GLU THR GLY ASN
SEQRES 14 A 1049 THR ASP TRP LEU ARG THR LEU MET HIS ASP PHE VAL THR
SEQRES 15 A 1049 ASN ASN PRO MET TRP ASN LYS ASP SER GLU ASN VAL ASN
SEQRES 16 A 1049 PHE SER GLY ILE GLN PHE GLN GLY GLY PHE LEU LYS TYR
SEQRES 17 A 1049 GLU ASN SER ASP LEU THR PRO TYR ALA ASN SER ASP TYR
SEQRES 18 A 1049 ARG LEU LEU GLY ARG MET PRO ILE ASN ILE LYS ASP GLN
SEQRES 19 A 1049 THR TYR ARG GLY GLN GLU PHE LEU LEU ALA ASN ASP ILE
SEQRES 20 A 1049 ASP ASN SER ASN PRO VAL VAL GLN ALA GLU GLN LEU ASN
SEQRES 21 A 1049 TRP LEU TYR TYR LEU LEU ASN PHE GLY THR ILE THR ALA
SEQRES 22 A 1049 ASN ASN ASP GLN ALA ASN PHE ASP SER VAL ARG VAL ASP
SEQRES 23 A 1049 ALA PRO ASP ASN ILE ASP ALA ASP LEU MET ASN ILE ALA
SEQRES 24 A 1049 GLN ASP TYR PHE ASN ALA ALA TYR GLY MET ASP SER ASP
SEQRES 25 A 1049 ALA VAL SER ASN LYS HIS ILE ASN ILE LEU GLU ASP TRP
SEQRES 26 A 1049 ASN HIS ALA ASP PRO GLU TYR PHE ASN LYS ILE GLY ASN
SEQRES 27 A 1049 PRO GLN LEU THR MET ASP ASP THR ILE LYS ASN SER LEU
SEQRES 28 A 1049 ASN HIS GLY LEU SER ASP ALA THR ASN ARG TRP GLY LEU
SEQRES 29 A 1049 ASP ALA ILE VAL HIS GLN SER LEU ALA ASP ARG GLU ASN
SEQRES 30 A 1049 ASN SER THR GLU ASN VAL VAL ILE PRO ASN TYR SER PHE
SEQRES 31 A 1049 VAL ARG ALA HIS ASP ASN ASN SER GLN ASP GLN ILE GLN
SEQRES 32 A 1049 ASN ALA ILE ARG ASP VAL THR GLY LYS ASP TYR HIS THR
SEQRES 33 A 1049 PHE THR PHE GLU ASP GLU GLN LYS GLY ILE ASP ALA TYR
SEQRES 34 A 1049 ILE GLN ASP GLN ASN SER THR VAL LYS LYS TYR ASN LEU
SEQRES 35 A 1049 TYR ASN ILE PRO ALA SER TYR ALA ILE LEU LEU THR ASN
SEQRES 36 A 1049 LYS ASP THR ILE PRO ARG VAL TYR TYR GLY ASP LEU TYR
SEQRES 37 A 1049 THR ASP GLY GLY GLN TYR MET GLU HIS GLN THR ARG TYR
SEQRES 38 A 1049 TYR ASP THR LEU THR ASN LEU LEU LYS SER ARG VAL LYS
SEQRES 39 A 1049 TYR VAL ALA GLY GLY GLN SER MET GLN THR MET SER VAL
SEQRES 40 A 1049 GLY GLY ASN ASN ASN ILE LEU THR SER VAL ARG TYR GLY
SEQRES 41 A 1049 LYS GLY ALA MET THR ALA THR ASP THR GLY THR ASP GLU
SEQRES 42 A 1049 THR ARG THR GLN GLY ILE GLY VAL VAL VAL SER ASN THR
SEQRES 43 A 1049 PRO ASN LEU LYS LEU GLY ALA ASN ASP LYS VAL VAL LEU
SEQRES 44 A 1049 HIS MET GLY ALA ALA HIS LYS ASN GLN GLN TYR ARG ALA
SEQRES 45 A 1049 ALA VAL LEU THR THR THR ASP GLY VAL ILE ASN TYR THR
SEQRES 46 A 1049 SER ASP GLN GLY ALA PRO VAL ALA MET THR ASP GLU ASN
SEQRES 47 A 1049 GLY ASP LEU TYR LEU SER SER HIS ASN LEU VAL VAL ASN
SEQRES 48 A 1049 GLY LYS GLU GLU ALA ASP THR ALA VAL GLN GLY TYR ALA
SEQRES 49 A 1049 ASN PRO ASP VAL SER GLY TYR LEU ALA VAL TRP VAL PRO
SEQRES 50 A 1049 VAL GLY ALA SER ASP ASN GLN ASP ALA ARG THR ALA PRO
SEQRES 51 A 1049 SER THR GLU LYS ASN SER GLY ASN SER ALA TYR ARG THR
SEQRES 52 A 1049 ASN ALA ALA PHE ASP SER ASN VAL ILE PHE GLU ALA PHE
SEQRES 53 A 1049 SER ASN PHE VAL TYR THR PRO THR LYS GLU SER GLU ARG
SEQRES 54 A 1049 ALA ASN VAL ARG ILE ALA GLN ASN ALA ASP PHE PHE ALA
SEQRES 55 A 1049 SER LEU GLY PHE THR SER PHE GLU MET ALA PRO GLN TYR
SEQRES 56 A 1049 ASN SER SER LYS ASP ARG THR PHE LEU ASP SER THR ILE
SEQRES 57 A 1049 ASP ASN GLY TYR ALA PHE THR ASP ARG TYR ASP LEU GLY
SEQRES 58 A 1049 MET SER GLU PRO ASN LYS TYR GLY THR ASP GLU ASP LEU
SEQRES 59 A 1049 ARG ASN ALA ILE GLN ALA LEU HIS LYS ALA GLY LEU GLN
SEQRES 60 A 1049 VAL MET ALA ASP TRP VAL PRO ASP GLN ILE TYR ASN LEU
SEQRES 61 A 1049 PRO GLY LYS GLU VAL ALA THR VAL THR ARG VAL ASP ASP
SEQRES 62 A 1049 ARG GLY ASN VAL TRP LYS ASP ALA ILE ILE ASN ASN ASN
SEQRES 63 A 1049 LEU TYR VAL VAL ASN THR ILE GLY GLY GLY GLU TYR GLN
SEQRES 64 A 1049 LYS LYS TYR GLY GLY ALA PHE LEU ASP LYS LEU GLN LYS
SEQRES 65 A 1049 LEU TYR PRO GLU ILE PHE THR LYS LYS GLN VAL SER THR
SEQRES 66 A 1049 GLY VAL ALA ILE ASP PRO SER GLN LYS ILE THR GLU TRP
SEQRES 67 A 1049 SER ALA LYS TYR PHE ASN GLY THR ASN ILE LEU HIS ARG
SEQRES 68 A 1049 GLY SER GLY TYR VAL LEU LYS ALA ASP GLY GLY GLN TYR
SEQRES 69 A 1049 TYR ASN LEU GLY THR THR THR LYS GLN PHE LEU PRO ILE
SEQRES 70 A 1049 GLN LEU THR GLY GLU LYS LYS GLN GLY ASN GLU GLY PHE
SEQRES 71 A 1049 VAL LYS GLY ASN ASP GLY ASN TYR TYR PHE TYR ASP LEU
SEQRES 72 A 1049 ALA GLY ASN MET VAL LYS ASN THR PHE ILE GLU ASP SER
SEQRES 73 A 1049 VAL GLY ASN TRP TYR PHE PHE ASP GLN ASP GLY LYS MET
SEQRES 74 A 1049 VAL GLU ASN LYS HIS PHE VAL ASP VAL ASP SER TYR GLY
SEQRES 75 A 1049 GLU LYS GLY THR TYR PHE PHE LEU LYS ASN GLY VAL SER
SEQRES 76 A 1049 PHE ARG GLY GLY LEU VAL GLN THR ASP ASN GLY THR TYR
SEQRES 77 A 1049 TYR PHE ASP ASN TYR GLY LYS MET VAL ARG ASN GLN THR
SEQRES 78 A 1049 ILE ASN ALA GLY ALA MET ILE TYR THR LEU ASP GLU ASN
SEQRES 79 A 1049 GLY LYS LEU ILE LYS ALA SER TYR ASN SER ASP ALA GLU
SEQRES 80 A 1049 TYR PRO THR SER THR ASP VAL GLY LYS MET LEU ASP GLN
SEQRES 81 A 1049 ASN LYS LEU HIS HIS HIS HIS HIS HIS
HET CA A2764 1
HETNAM CA CALCIUM ION
FORMUL 2 CA CA 2+
HELIX 1 1 LEU A 781 LEU A 783 5 3
HELIX 2 2 GLU A 794 ASN A 800 1 7
HELIX 3 3 ASP A 831 THR A 833 5 3
HELIX 4 4 LEU A 847 VAL A 849 5 3
HELIX 5 5 ASN A 853 HIS A 867 1 15
HELIX 6 6 ASP A 883 GLY A 906 1 24
HELIX 7 7 THR A 908 ASN A 922 1 15
HELIX 8 8 ASN A 926 GLU A 930 5 5
HELIX 9 9 MET A 965 ILE A 969 5 5
HELIX 10 10 ASN A 989 ASN A 1005 1 17
HELIX 11 11 ASN A 1005 ASN A 1012 1 8
HELIX 12 12 ALA A 1031 TYR A 1045 1 15
HELIX 13 13 SER A 1049 ASN A 1054 1 6
HELIX 14 14 ALA A 1066 ILE A 1074 1 9
HELIX 15 15 ASP A 1082 SER A 1094 1 13
HELIX 16 16 LEU A 1102 GLN A 1108 1 7
HELIX 17 17 SER A 1136 THR A 1148 1 13
HELIX 18 18 PHE A 1155 ASN A 1172 1 18
HELIX 19 19 ASN A 1182 LEU A 1191 1 10
HELIX 20 20 TYR A 1202 TYR A 1206 1 5
HELIX 21 21 TYR A 1219 TYR A 1233 1 15
HELIX 22 22 ASP A 1270 GLN A 1275 5 6
HELIX 23 23 LYS A 1423 GLU A 1426 5 4
HELIX 24 24 ARG A 1427 ASN A 1435 1 9
HELIX 25 25 ASN A 1435 LEU A 1442 1 8
HELIX 26 26 PHE A 1461 THR A 1465 5 5
HELIX 27 27 THR A 1488 ALA A 1502 1 15
HELIX 28 28 GLY A 1554 GLY A 1561 1 8
HELIX 29 29 PHE A 1564 TYR A 1572 1 9
HELIX 30 30 SER A 1597 LYS A 1599 5 3
HELIX 31 31 PRO A 1634 GLY A 1639 1 6
SHEET 1 AA 5 GLY A 777 ASN A 779 0
SHEET 2 AA 5 ASN A 766 PHE A 770 -1 O TYR A 769 N THR A 778
SHEET 3 AA 5 PHE A 759 SER A 763 -1 O PHE A 759 N PHE A 770
SHEET 4 AA 5 GLY A1717 THR A1721 1 O LEU A1718 N LEU A 760
SHEET 5 AA 5 GLY A1724 PHE A1728 -1 O GLY A1724 N THR A1721
SHEET 1 AB 2 TRP A 822 TYR A 823 0
SHEET 2 AB 2 ARG A 844 PRO A 845 -1 O ARG A 844 N TYR A 823
SHEET 1 AC 2 GLN A 827 LYS A 830 0
SHEET 2 AC 2 THR A 834 ASP A 837 -1 O THR A 834 N LYS A 830
SHEET 1 AD 6 GLN A1514 ILE A1515 0
SHEET 2 AD 6 ASN A 983 ILE A 985 -1 O ASN A 983 N ILE A1515
SHEET 3 AD 6 PHE A1601 ASN A1605 -1 N ASN A1602 O ASP A 984
SHEET 4 AD 6 PHE A 943 TYR A 946 -1 O LEU A 944 N THR A1604
SHEET 5 AD 6 GLY A1520 VAL A1529 -1 O THR A1527 N LYS A 945
SHEET 6 AD 6 ASN A1542 ILE A1551 -1 N ASN A1543 O VAL A1526
SHEET 1 AE 3 ILE A1059 LEU A1060 0
SHEET 2 AE 3 SER A1020 VAL A1023 1 O VAL A1021 N ILE A1059
SHEET 3 AE 3 MET A1507 TRP A1510 1 O ALA A1508 N ARG A1022
SHEET 1 AF 5 THR A1080 MET A1081 0
SHEET 2 AF 5 ASN A1125 PHE A1128 1 N TYR A1126 O THR A1080
SHEET 3 AF 5 ILE A1197 TYR A1201 1 O ILE A1197 N SER A1127
SHEET 4 AF 5 ILE A1410 GLU A1412 1 O ILE A1410 N VAL A1200
SHEET 5 AF 5 SER A1446 GLU A1448 1 O SER A1446 N PHE A1411
SHEET 1 AG 7 ASN A1115 ASN A1116 0
SHEET 2 AG 7 GLN A1238 THR A1242 -1 O GLN A1238 N ASN A1116
SHEET 3 AG 7 LEU A1252 ARG A1256 -1 O THR A1253 N GLN A1241
SHEET 4 AG 7 ILE A1277 SER A1282 -1 O ILE A1277 N ARG A1256
SHEET 5 AG 7 TYR A1369 PRO A1375 -1 O TYR A1369 N SER A1282
SHEET 6 AG 7 GLN A1307 THR A1314 -1 O ARG A1309 N VAL A1374
SHEET 7 AG 7 VAL A1319 ASN A1321 -1 O ILE A1320 N LEU A1313
SHEET 1 AH 7 ASN A1115 ASN A1116 0
SHEET 2 AH 7 GLN A1238 THR A1242 -1 O GLN A1238 N ASN A1116
SHEET 3 AH 7 LEU A1252 ARG A1256 -1 O THR A1253 N GLN A1241
SHEET 4 AH 7 ILE A1277 SER A1282 -1 O ILE A1277 N ARG A1256
SHEET 5 AH 7 TYR A1369 PRO A1375 -1 O TYR A1369 N SER A1282
SHEET 6 AH 7 GLN A1307 THR A1314 -1 O ARG A1309 N VAL A1374
SHEET 7 AH 7 VAL A1330 MET A1332 1 O ALA A1331 N TYR A1308
SHEET 1 AI 2 VAL A1319 ASN A1321 0
SHEET 2 AI 2 GLN A1307 THR A1314 -1 O LEU A1313 N ILE A1320
SHEET 1 AJ 2 LYS A1294 HIS A1298 0
SHEET 2 AJ 2 ASP A1338 SER A1342 -1 O LEU A1339 N LEU A1297
SHEET 1 AK 2 GLY A1647 LYS A1650 0
SHEET 2 AK 2 TYR A1656 TYR A1659 -1 O TYR A1657 N VAL A1649
SHEET 1 AL 2 THR A1669 GLU A1672 0
SHEET 2 AL 2 TRP A1678 PHE A1681 -1 O TYR A1679 N ILE A1671
SHEET 1 AM 2 PHE A1693 VAL A1696 0
SHEET 2 AM 2 GLY A1703 PHE A1706 -1 O GLY A1703 N VAL A1696
SHEET 1 AN 3 GLN A1738 ALA A1742 0
SHEET 2 AN 3 MET A1745 LEU A1749 -1 O MET A1745 N ALA A1742
SHEET 3 AN 3 LEU A1755 TYR A1760 -1 N ILE A1756 O THR A1748
LINK O GLU A 978 CA CA A2764 1555 1555 2.78
LINK OE2 GLU A 978 CA CA A2764 1555 1555 3.01
LINK OD1 ASP A 984 CA CA A2764 1555 1555 2.45
LINK O ASN A1028 CA CA A2764 1555 1555 2.66
LINK OD2 ASP A1513 CA CA A2764 1555 1555 3.01
SITE 1 AC1 4 GLU A 978 ASP A 984 ASN A1028 ASP A1513
CRYST1 183.871 183.871 374.004 90.00 90.00 120.00 P 62 2 2 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 0.005439 0.003140 0.000000 0.00000
SCALE2 0.000000 0.006280 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002674 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
