HEADER TRANSFERASE 30-MAY-13 4BQI
TITLE ARABIDOPSIS THALIANA CYTOSOLIC ALPHA-1,4-GLUCAN PHOSPHORYLASE (PHS2)
TITLE 2 IN COMPLEX WITH MALTOTRIOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-GLUCAN PHOSPHORYLASE 2, CYTOSOLIC;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ATPHS2, ALPHA-GLUCAN PHOSPHORYLASE, H ISOZYME, STARCH
COMPND 5 PHOSPHORYLASE H, PHS2;
COMPND 6 EC: 2.4.1.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA-2 LYSSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET151;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET151-PHS2
KEYWDS TRANSFERASE, CARBOHYDRATE METABOLISM, SELF-ASSEMBLY ON SURFACES
EXPDTA X-RAY DIFFRACTION
AUTHOR E.C.O'NEILL,A.M.RASHID,C.E.M.STEVENSON,A.C.HETRU,A.P.GUNNING,
AUTHOR 2 M.REJZEK,S.A.NEPOGODIEV,S.BORNEMANN,D.M.LAWSON,R.A.FIELD
REVDAT 4 20-DEC-23 4BQI 1 HETSYN
REVDAT 3 29-JUL-20 4BQI 1 COMPND REMARK HET HETNAM
REVDAT 3 2 1 HETSYN FORMUL LINK SITE
REVDAT 3 3 1 ATOM
REVDAT 2 08-MAY-19 4BQI 1 REMARK LINK
REVDAT 1 19-FEB-14 4BQI 0
JRNL AUTH E.C.O'NEILL,A.M.RASHID,C.E.M.STEVENSON,A.C.HETRU,
JRNL AUTH 2 A.P.GUNNING,M.REJZEK,S.A.NEPOGODIEV,S.BORNEMANN,D.M.LAWSON,
JRNL AUTH 3 R.A.FIELD
JRNL TITL SUGAR-COATED SENSOR CHIP AND NANOPARTICLE SURFACES FOR THE
JRNL TITL 2 IN VITRO ENZYMATIC SYNTHESIS OF STARCH-LIKE MATERIALS
JRNL REF CHEM.SCI. V. 5 341 2014
JRNL REFN ISSN 2041-6520
JRNL DOI 10.1039/C3SC51829A
REMARK 2
REMARK 2 RESOLUTION. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 52.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 126128
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6643
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) : 7793
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.2870
REMARK 3 BIN FREE R VALUE SET COUNT : 439
REMARK 3 BIN FREE R VALUE : 0.3520
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12957
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 111
REMARK 3 SOLVENT ATOMS : 919
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.95000
REMARK 3 B22 (A**2) : -0.81000
REMARK 3 B33 (A**2) : -0.75000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.171
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.157
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.122
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.076
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13472 ; 0.014 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 9079 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18330 ; 1.545 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): 22091 ; 1.155 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1674 ; 6.164 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 628 ;34.389 ;24.188
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2222 ;13.604 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 85 ;20.275 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2033 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 15035 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2786 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
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 15 A 47
REMARK 3 ORIGIN FOR THE GROUP (A): 41.4961 -43.8492 48.0936
REMARK 3 T TENSOR
REMARK 3 T11: 0.0782 T22: 0.0300
REMARK 3 T33: 0.1295 T12: 0.0093
REMARK 3 T13: -0.0241 T23: 0.0470
REMARK 3 L TENSOR
REMARK 3 L11: 3.6995 L22: 9.1062
REMARK 3 L33: 7.5451 L12: 1.6074
REMARK 3 L13: 1.8939 L23: 5.3712
REMARK 3 S TENSOR
REMARK 3 S11: 0.0286 S12: -0.0549 S13: -0.4014
REMARK 3 S21: -0.1763 S22: -0.0166 S23: 0.0311
REMARK 3 S31: 0.3290 S32: 0.0567 S33: -0.0120
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 48 A 108
REMARK 3 ORIGIN FOR THE GROUP (A): 41.7292 -34.6243 31.9267
REMARK 3 T TENSOR
REMARK 3 T11: 0.0533 T22: 0.0376
REMARK 3 T33: 0.0589 T12: 0.0307
REMARK 3 T13: -0.0243 T23: -0.0281
REMARK 3 L TENSOR
REMARK 3 L11: 1.4316 L22: 1.0450
REMARK 3 L33: 1.7313 L12: 0.2028
REMARK 3 L13: -0.7598 L23: -0.5344
REMARK 3 S TENSOR
REMARK 3 S11: -0.0034 S12: -0.0203 S13: -0.2064
REMARK 3 S21: 0.0685 S22: -0.0155 S23: -0.0240
REMARK 3 S31: 0.1926 S32: 0.1554 S33: 0.0189
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 109 A 253
REMARK 3 ORIGIN FOR THE GROUP (A): 42.6496 -23.0585 33.2448
REMARK 3 T TENSOR
REMARK 3 T11: 0.0263 T22: 0.0624
REMARK 3 T33: 0.0282 T12: 0.0076
REMARK 3 T13: -0.0110 T23: -0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 0.4049 L22: 1.2795
REMARK 3 L33: 0.6241 L12: -0.0174
REMARK 3 L13: 0.2157 L23: 0.0141
REMARK 3 S TENSOR
REMARK 3 S11: 0.0436 S12: -0.0277 S13: -0.0913
REMARK 3 S21: 0.1335 S22: -0.0368 S23: -0.0008
REMARK 3 S31: 0.0522 S32: 0.0466 S33: -0.0068
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 254 A 495
REMARK 3 ORIGIN FOR THE GROUP (A): 47.2737 -10.6548 17.7767
REMARK 3 T TENSOR
REMARK 3 T11: 0.0381 T22: 0.1166
REMARK 3 T33: 0.0411 T12: 0.0035
REMARK 3 T13: 0.0145 T23: 0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 0.3817 L22: 0.7639
REMARK 3 L33: 0.8414 L12: 0.3310
REMARK 3 L13: 0.2726 L23: -0.1252
REMARK 3 S TENSOR
REMARK 3 S11: -0.0440 S12: 0.1255 S13: 0.0536
REMARK 3 S21: -0.0776 S22: 0.0015 S23: -0.0273
REMARK 3 S31: -0.1062 S32: 0.1397 S33: 0.0424
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 496 A 573
REMARK 3 ORIGIN FOR THE GROUP (A): 15.3056 -36.1775 26.0384
REMARK 3 T TENSOR
REMARK 3 T11: 0.0730 T22: 0.0146
REMARK 3 T33: 0.0266 T12: -0.0070
REMARK 3 T13: 0.0077 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 1.3944 L22: 2.2265
REMARK 3 L33: 1.1516 L12: 0.0652
REMARK 3 L13: -0.1907 L23: 1.0074
REMARK 3 S TENSOR
REMARK 3 S11: 0.0546 S12: -0.1396 S13: -0.0764
REMARK 3 S21: 0.2706 S22: -0.0110 S23: 0.0660
REMARK 3 S31: 0.1969 S32: 0.0232 S33: -0.0436
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 574 A 767
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3519 -13.1240 25.5085
REMARK 3 T TENSOR
REMARK 3 T11: 0.0225 T22: 0.0255
REMARK 3 T33: 0.1109 T12: 0.0025
REMARK 3 T13: 0.0257 T23: -0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 0.9295 L22: 1.6570
REMARK 3 L33: 1.5813 L12: -0.0594
REMARK 3 L13: 0.3778 L23: -0.0819
REMARK 3 S TENSOR
REMARK 3 S11: -0.0074 S12: -0.0282 S13: 0.2176
REMARK 3 S21: 0.0863 S22: -0.0298 S23: 0.2620
REMARK 3 S31: -0.1308 S32: -0.1513 S33: 0.0372
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 768 A 805
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0690 -12.0668 19.2034
REMARK 3 T TENSOR
REMARK 3 T11: 0.0280 T22: 0.0450
REMARK 3 T33: 0.1169 T12: 0.0087
REMARK 3 T13: 0.0144 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 1.6369 L22: 10.6002
REMARK 3 L33: 1.1136 L12: 1.7852
REMARK 3 L13: -0.8121 L23: -1.3368
REMARK 3 S TENSOR
REMARK 3 S11: 0.1338 S12: 0.0595 S13: 0.3501
REMARK 3 S21: 0.2671 S22: -0.0959 S23: 0.5882
REMARK 3 S31: -0.1094 S32: -0.0328 S33: -0.0379
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 806 A 841
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6958 -32.8469 13.4053
REMARK 3 T TENSOR
REMARK 3 T11: 0.0949 T22: 0.1710
REMARK 3 T33: 0.0258 T12: 0.0763
REMARK 3 T13: -0.0105 T23: -0.0294
REMARK 3 L TENSOR
REMARK 3 L11: 3.1684 L22: 1.2068
REMARK 3 L33: 0.3849 L12: 1.9168
REMARK 3 L13: -0.9141 L23: -0.6282
REMARK 3 S TENSOR
REMARK 3 S11: -0.0359 S12: 0.3134 S13: 0.1461
REMARK 3 S21: -0.0814 S22: 0.1125 S23: 0.1067
REMARK 3 S31: 0.1007 S32: 0.0359 S33: -0.0766
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 15 B 63
REMARK 3 ORIGIN FOR THE GROUP (A): 57.5013 -40.7261 44.3816
REMARK 3 T TENSOR
REMARK 3 T11: 0.0671 T22: 0.0688
REMARK 3 T33: 0.1194 T12: 0.0296
REMARK 3 T13: -0.0178 T23: -0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 2.8938 L22: 3.6479
REMARK 3 L33: 4.4879 L12: -0.5733
REMARK 3 L13: 0.6310 L23: -0.1322
REMARK 3 S TENSOR
REMARK 3 S11: 0.0640 S12: 0.2961 S13: -0.1950
REMARK 3 S21: -0.1394 S22: -0.0552 S23: -0.0722
REMARK 3 S31: 0.1714 S32: 0.0578 S33: -0.0088
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 64 B 250
REMARK 3 ORIGIN FOR THE GROUP (A): 54.1301 -25.9289 60.8089
REMARK 3 T TENSOR
REMARK 3 T11: 0.0389 T22: 0.0529
REMARK 3 T33: 0.0515 T12: -0.0160
REMARK 3 T13: -0.0210 T23: 0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 0.4686 L22: 0.9251
REMARK 3 L33: 0.7821 L12: -0.0521
REMARK 3 L13: 0.0095 L23: 0.0819
REMARK 3 S TENSOR
REMARK 3 S11: 0.0363 S12: 0.0451 S13: -0.1263
REMARK 3 S21: -0.0746 S22: -0.0725 S23: -0.0491
REMARK 3 S31: 0.0228 S32: 0.1053 S33: 0.0362
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 251 B 278
REMARK 3 ORIGIN FOR THE GROUP (A): 39.1782 -6.2112 46.5491
REMARK 3 T TENSOR
REMARK 3 T11: 0.0889 T22: 0.0267
REMARK 3 T33: 0.0552 T12: -0.0104
REMARK 3 T13: 0.0357 T23: -0.0348
REMARK 3 L TENSOR
REMARK 3 L11: 4.5849 L22: 3.5227
REMARK 3 L33: 10.5050 L12: -1.8844
REMARK 3 L13: 6.1106 L23: -5.0372
REMARK 3 S TENSOR
REMARK 3 S11: -0.0855 S12: -0.1737 S13: 0.2309
REMARK 3 S21: 0.1789 S22: 0.0012 S23: 0.1135
REMARK 3 S31: -0.2931 S32: -0.1479 S33: 0.0843
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 279 B 430
REMARK 3 ORIGIN FOR THE GROUP (A): 45.7130 -11.7072 76.3993
REMARK 3 T TENSOR
REMARK 3 T11: 0.0349 T22: 0.0494
REMARK 3 T33: 0.0115 T12: -0.0123
REMARK 3 T13: -0.0011 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.9632 L22: 1.4510
REMARK 3 L33: 1.6910 L12: -0.3093
REMARK 3 L13: -0.1728 L23: 0.1447
REMARK 3 S TENSOR
REMARK 3 S11: -0.0139 S12: -0.1695 S13: 0.0461
REMARK 3 S21: 0.1916 S22: -0.0325 S23: 0.0188
REMARK 3 S31: -0.0886 S32: 0.0200 S33: 0.0465
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 431 B 571
REMARK 3 ORIGIN FOR THE GROUP (A): 71.5939 -25.3158 73.2261
REMARK 3 T TENSOR
REMARK 3 T11: 0.0825 T22: 0.1038
REMARK 3 T33: 0.0840 T12: -0.0386
REMARK 3 T13: -0.0401 T23: 0.0460
REMARK 3 L TENSOR
REMARK 3 L11: 0.9775 L22: 0.9433
REMARK 3 L33: 0.5295 L12: -0.4581
REMARK 3 L13: 0.0473 L23: 0.0845
REMARK 3 S TENSOR
REMARK 3 S11: -0.0243 S12: -0.0293 S13: -0.0892
REMARK 3 S21: 0.0075 S22: 0.0389 S23: -0.1133
REMARK 3 S31: 0.0626 S32: 0.1614 S33: -0.0145
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 572 B 767
REMARK 3 ORIGIN FOR THE GROUP (A): 85.1801 -11.3775 66.9893
REMARK 3 T TENSOR
REMARK 3 T11: 0.1160 T22: 0.2277
REMARK 3 T33: 0.1099 T12: -0.0987
REMARK 3 T13: -0.0147 T23: 0.0525
REMARK 3 L TENSOR
REMARK 3 L11: 1.0959 L22: 1.8424
REMARK 3 L33: 1.2263 L12: 0.2126
REMARK 3 L13: 0.6629 L23: 0.0984
REMARK 3 S TENSOR
REMARK 3 S11: -0.1256 S12: 0.0609 S13: 0.1241
REMARK 3 S21: -0.0724 S22: 0.0657 S23: -0.2207
REMARK 3 S31: -0.2780 S32: 0.2824 S33: 0.0599
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 768 B 806
REMARK 3 ORIGIN FOR THE GROUP (A): 89.5773 -11.7173 72.8191
REMARK 3 T TENSOR
REMARK 3 T11: 0.0977 T22: 0.2589
REMARK 3 T33: 0.0941 T12: -0.1110
REMARK 3 T13: -0.0388 T23: 0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 1.9877 L22: 10.0564
REMARK 3 L33: 1.8368 L12: -2.1502
REMARK 3 L13: 0.0673 L23: 1.1576
REMARK 3 S TENSOR
REMARK 3 S11: -0.1137 S12: -0.0371 S13: 0.2908
REMARK 3 S21: 0.0001 S22: 0.1108 S23: -0.5573
REMARK 3 S31: -0.2409 S32: 0.1769 S33: 0.0030
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 807 B 841
REMARK 3 ORIGIN FOR THE GROUP (A): 65.8113 -32.7990 78.8667
REMARK 3 T TENSOR
REMARK 3 T11: 0.1338 T22: 0.1528
REMARK 3 T33: 0.0998 T12: -0.0246
REMARK 3 T13: -0.0494 T23: 0.0893
REMARK 3 L TENSOR
REMARK 3 L11: 2.0853 L22: 1.3332
REMARK 3 L33: 0.7354 L12: -1.5722
REMARK 3 L13: -0.7543 L23: 0.8269
REMARK 3 S TENSOR
REMARK 3 S11: -0.0845 S12: -0.3808 S13: 0.0061
REMARK 3 S21: 0.1582 S22: 0.2135 S23: -0.0843
REMARK 3 S31: 0.2034 S32: 0.0552 S33: -0.1290
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 ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 4BQI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1290057082.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JAN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.25
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) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 132861
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 65.810
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
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) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.56000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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 1GPB
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLISED FROM APPROXIMATELY 20%
REMARK 280 PEG3350, 100 MM AMMONIUM CITRATE PH 8.25, 10% GLYCEROL USING THE
REMARK 280 HANGING DROP VAPOUR DIFFUSION METHOD AT 20 DEG C. 1 MICROLITRE
REMARK 280 OF PROTEIN AT 10 MG PER ML IN 12.5 MM HEPES PH 7.5, 25 MM NACL
REMARK 280 WAS MIXED WITH 1 MICROLITRE OF THE WELL SOLUTION TO GIVE THE
REMARK 280 FINAL DROP, VAPOR DIFFUSION, HANGING DROP, 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 58.03600
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 -32
REMARK 465 HIS A -31
REMARK 465 HIS A -30
REMARK 465 HIS A -29
REMARK 465 HIS A -28
REMARK 465 HIS A -27
REMARK 465 HIS A -26
REMARK 465 GLY A -25
REMARK 465 LYS A -24
REMARK 465 PRO A -23
REMARK 465 ILE A -22
REMARK 465 PRO A -21
REMARK 465 ASN A -20
REMARK 465 PRO A -19
REMARK 465 LEU A -18
REMARK 465 LEU A -17
REMARK 465 GLY A -16
REMARK 465 LEU A -15
REMARK 465 ASP A -14
REMARK 465 SER A -13
REMARK 465 THR A -12
REMARK 465 GLU A -11
REMARK 465 ASN A -10
REMARK 465 LEU A -9
REMARK 465 TYR A -8
REMARK 465 PHE A -7
REMARK 465 GLN A -6
REMARK 465 GLY A -5
REMARK 465 ILE A -4
REMARK 465 ASP A -3
REMARK 465 PRO A -2
REMARK 465 PHE A -1
REMARK 465 THR A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ASN A 3
REMARK 465 ALA A 4
REMARK 465 ASN A 5
REMARK 465 GLY A 6
REMARK 465 LYS A 7
REMARK 465 ALA A 8
REMARK 465 ALA A 9
REMARK 465 THR A 10
REMARK 465 SER A 11
REMARK 465 LEU A 12
REMARK 465 PRO A 13
REMARK 465 GLU A 14
REMARK 465 GLU A 323
REMARK 465 GLY A 324
REMARK 465 SER A 325
REMARK 465 MET B -32
REMARK 465 HIS B -31
REMARK 465 HIS B -30
REMARK 465 HIS B -29
REMARK 465 HIS B -28
REMARK 465 HIS B -27
REMARK 465 HIS B -26
REMARK 465 GLY B -25
REMARK 465 LYS B -24
REMARK 465 PRO B -23
REMARK 465 ILE B -22
REMARK 465 PRO B -21
REMARK 465 ASN B -20
REMARK 465 PRO B -19
REMARK 465 LEU B -18
REMARK 465 LEU B -17
REMARK 465 GLY B -16
REMARK 465 LEU B -15
REMARK 465 ASP B -14
REMARK 465 SER B -13
REMARK 465 THR B -12
REMARK 465 GLU B -11
REMARK 465 ASN B -10
REMARK 465 LEU B -9
REMARK 465 TYR B -8
REMARK 465 PHE B -7
REMARK 465 GLN B -6
REMARK 465 GLY B -5
REMARK 465 ILE B -4
REMARK 465 ASP B -3
REMARK 465 PRO B -2
REMARK 465 PHE B -1
REMARK 465 THR B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ASN B 3
REMARK 465 ALA B 4
REMARK 465 ASN B 5
REMARK 465 GLY B 6
REMARK 465 LYS B 7
REMARK 465 ALA B 8
REMARK 465 ALA B 9
REMARK 465 THR B 10
REMARK 465 SER B 11
REMARK 465 LEU B 12
REMARK 465 PRO B 13
REMARK 465 GLU B 14
REMARK 465 GLU B 323
REMARK 465 GLY B 324
REMARK 465 SER B 325
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 LYS A 15 CG CD CE NZ
REMARK 470 LYS A 19 CE NZ
REMARK 470 LEU A 47 CG CD1 CD2
REMARK 470 LYS A 48 CG CD CE NZ
REMARK 470 LYS A 79 CD CE NZ
REMARK 470 GLU A 123 CG CD OE1 OE2
REMARK 470 LYS A 170 CE NZ
REMARK 470 LYS A 175 CG CD CE NZ
REMARK 470 LYS A 176 CG CD CE NZ
REMARK 470 LYS A 251 CE NZ
REMARK 470 GLU A 255 CG CD OE1 OE2
REMARK 470 LYS A 327 CG CD CE NZ
REMARK 470 LEU A 382 CG CD1 CD2
REMARK 470 GLU A 384 CG CD OE1 OE2
REMARK 470 LYS A 396 CE NZ
REMARK 470 GLU A 424 CG CD OE1 OE2
REMARK 470 GLN A 438 CG CD OE1 NE2
REMARK 470 LYS A 439 CG CD CE NZ
REMARK 470 LYS A 467 CE NZ
REMARK 470 LYS A 514 CE NZ
REMARK 470 ARG A 590 NE CZ NH1 NH2
REMARK 470 LYS A 598 CD CE NZ
REMARK 470 GLU A 600 CG CD OE1 OE2
REMARK 470 LYS A 603 CG CD CE NZ
REMARK 470 LYS A 604 CG CD CE NZ
REMARK 470 PHE A 617 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 712 CD OE1 OE2
REMARK 470 LYS A 730 CE NZ
REMARK 470 GLU A 733 CG CD OE1 OE2
REMARK 470 GLN A 748 CD OE1 NE2
REMARK 470 ARG A 802 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 830 CD CE NZ
REMARK 470 LYS B 15 CG CD CE NZ
REMARK 470 LEU B 47 CG CD1 CD2
REMARK 470 LYS B 48 CD CE NZ
REMARK 470 ARG B 65 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 79 CD CE NZ
REMARK 470 GLU B 123 CG CD OE1 OE2
REMARK 470 LYS B 170 CE NZ
REMARK 470 LYS B 175 CG CD CE NZ
REMARK 470 LYS B 176 CG CD CE NZ
REMARK 470 LYS B 208 CE NZ
REMARK 470 LYS B 327 CD CE NZ
REMARK 470 VAL B 381 CG1 CG2
REMARK 470 GLU B 384 CG CD OE1 OE2
REMARK 470 ARG B 417 CD NE CZ NH1 NH2
REMARK 470 VAL B 421 CG1 CG2
REMARK 470 GLU B 424 CG CD OE1 OE2
REMARK 470 ASP B 425 CG OD1 OD2
REMARK 470 GLU B 469 CD OE1 OE2
REMARK 470 LYS B 508 CE NZ
REMARK 470 LYS B 511 CD CE NZ
REMARK 470 LYS B 547 CE NZ
REMARK 470 ARG B 573 NE CZ NH1 NH2
REMARK 470 LYS B 592 CE NZ
REMARK 470 LYS B 595 CG CD CE NZ
REMARK 470 LYS B 598 CG CD CE NZ
REMARK 470 GLU B 600 CG CD OE1 OE2
REMARK 470 GLU B 601 CG CD OE1 OE2
REMARK 470 LYS B 603 CG CD CE NZ
REMARK 470 LYS B 604 CG CD CE NZ
REMARK 470 PHE B 617 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 642 CG CD OE1 OE2
REMARK 470 GLU B 712 CG CD OE1 OE2
REMARK 470 GLU B 733 CD OE1 OE2
REMARK 470 LYS B 738 CE NZ
REMARK 470 ASP B 765 CG OD1 OD2
REMARK 470 THR B 771 OG1 CG2
REMARK 470 PHE B 773 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 803 CG CD CE NZ
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 OE1 GLU A 268 OE1 GLU B 268 2.17
REMARK 500 O HOH A 2095 O HOH A 2230 2.17
REMARK 500 O VAL B 75 O HOH B 2035 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP B 367 CE2 TRP B 367 CD2 0.073
REMARK 500
REMARK 500 REMARK: NULL
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 493 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 96 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 443 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 443 NE - CZ - NH2 ANGL. DEV. = -3.0 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 ASN A 136 -57.11 -128.20
REMARK 500 LEU A 168 -65.40 -96.30
REMARK 500 LYS A 188 -82.83 -102.63
REMARK 500 PHE A 206 -135.00 67.71
REMARK 500 ASP A 221 -160.98 64.62
REMARK 500 ASP A 341 -170.88 69.52
REMARK 500 LYS A 439 76.86 -153.77
REMARK 500 GLU A 469 -69.64 -125.30
REMARK 500 ARG A 492 -72.81 -79.66
REMARK 500 LEU A 495 -65.91 -154.27
REMARK 500 SER A 681 -104.18 -146.22
REMARK 500 ASN B 136 -57.02 -128.65
REMARK 500 LEU B 168 -66.34 -91.33
REMARK 500 LYS B 188 -82.76 -101.92
REMARK 500 PHE B 206 -136.03 66.16
REMARK 500 ASP B 221 -158.67 64.67
REMARK 500 ASP B 341 -171.29 68.52
REMARK 500 ASP B 418 56.67 -100.39
REMARK 500 THR B 419 -25.15 169.39
REMARK 500 ASN B 435 31.08 -95.50
REMARK 500 ASN B 436 124.63 -39.52
REMARK 500 GLU B 469 -70.41 -126.08
REMARK 500 ASN B 487 166.20 -49.66
REMARK 500 ARG B 492 -73.68 -76.21
REMARK 500 LEU B 495 -62.34 -153.49
REMARK 500 SER B 681 -108.01 -150.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 MALTOTRIOSE (MLR): CRYSTAL WAS SOAKED FOR 1 WEEK IN A 1
REMARK 600 MILLIMOLAR SOLUTION OF MALTOTRIOSE MADE UP IN
REMARK 600 CRYSTALLIZATION WELL SOLUTION
REMARK 600 PYRIDOXAL-5'-PHOSPHATE (PLP): COVALENTLY LINKED TO LYS 687
REMARK 600 OF CORRESPONDING PROTEIN CHAIN
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BQE RELATED DB: PDB
REMARK 900 SENSOR CHIP AND NANOPARTICLE SURFACES FOR THE IN VITRO ENZYMATIC
REMARK 900 SYNTHESIS OF STARCH-LIKE MATERIALS
REMARK 900 RELATED ID: 4BQF RELATED DB: PDB
REMARK 900 ARABIDOPSIS THALIANA CYTOSOLIC ALPHA-1,4-GLUCAN PHOSPHORYLASE (PHS2)
REMARK 900 IN COMPLEX WITH ACARBOSE
DBREF 4BQI A 1 841 UNP Q9SD76 PHS2_ARATH 1 841
DBREF 4BQI B 1 841 UNP Q9SD76 PHS2_ARATH 1 841
SEQADV 4BQI MET A -32 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI HIS A -31 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI HIS A -30 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI HIS A -29 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI HIS A -28 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI HIS A -27 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI HIS A -26 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI GLY A -25 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI LYS A -24 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI PRO A -23 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI ILE A -22 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI PRO A -21 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI ASN A -20 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI PRO A -19 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI LEU A -18 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI LEU A -17 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI GLY A -16 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI LEU A -15 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI ASP A -14 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI SER A -13 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI THR A -12 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI GLU A -11 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI ASN A -10 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI LEU A -9 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI TYR A -8 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI PHE A -7 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI GLN A -6 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI GLY A -5 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI ILE A -4 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI ASP A -3 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI PRO A -2 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI PHE A -1 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI THR A 0 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI MET B -32 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI HIS B -31 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI HIS B -30 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI HIS B -29 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI HIS B -28 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI HIS B -27 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI HIS B -26 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI GLY B -25 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI LYS B -24 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI PRO B -23 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI ILE B -22 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI PRO B -21 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI ASN B -20 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI PRO B -19 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI LEU B -18 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI LEU B -17 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI GLY B -16 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI LEU B -15 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI ASP B -14 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI SER B -13 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI THR B -12 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI GLU B -11 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI ASN B -10 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI LEU B -9 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI TYR B -8 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI PHE B -7 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI GLN B -6 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI GLY B -5 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI ILE B -4 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI ASP B -3 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI PRO B -2 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI PHE B -1 UNP Q9SD76 EXPRESSION TAG
SEQADV 4BQI THR B 0 UNP Q9SD76 EXPRESSION TAG
SEQRES 1 A 874 MET HIS HIS HIS HIS HIS HIS GLY LYS PRO ILE PRO ASN
SEQRES 2 A 874 PRO LEU LEU GLY LEU ASP SER THR GLU ASN LEU TYR PHE
SEQRES 3 A 874 GLN GLY ILE ASP PRO PHE THR MET ALA ASN ALA ASN GLY
SEQRES 4 A 874 LYS ALA ALA THR SER LEU PRO GLU LYS ILE SER ALA LYS
SEQRES 5 A 874 ALA ASN PRO GLU ALA ASP ASP ALA THR GLU ILE ALA GLY
SEQRES 6 A 874 ASN ILE VAL TYR HIS ALA LYS TYR SER PRO HIS PHE SER
SEQRES 7 A 874 PRO LEU LYS PHE GLY PRO GLU GLN ALA LEU TYR ALA THR
SEQRES 8 A 874 ALA GLU SER LEU ARG ASP ARG LEU ILE GLN LEU TRP ASN
SEQRES 9 A 874 GLU THR TYR VAL HIS PHE ASN LYS VAL ASP PRO LYS GLN
SEQRES 10 A 874 THR TYR TYR LEU SER MET GLU TYR LEU GLN GLY ARG ALA
SEQRES 11 A 874 LEU THR ASN ALA ILE GLY ASN LEU ASN LEU GLN GLY PRO
SEQRES 12 A 874 TYR ALA ASP ALA LEU ARG THR LEU GLY TYR GLU LEU GLU
SEQRES 13 A 874 GLU ILE ALA GLU GLN GLU LYS ASP ALA ALA LEU GLY ASN
SEQRES 14 A 874 GLY GLY LEU GLY ARG LEU ALA SER CYS PHE LEU ASP SER
SEQRES 15 A 874 MET ALA THR LEU ASN LEU PRO ALA TRP GLY TYR GLY LEU
SEQRES 16 A 874 ARG TYR ARG HIS GLY LEU PHE LYS GLN ILE ILE THR LYS
SEQRES 17 A 874 LYS GLY GLN GLU GLU ILE PRO GLU ASP TRP LEU GLU LYS
SEQRES 18 A 874 PHE SER PRO TRP GLU ILE VAL ARG HIS ASP VAL VAL PHE
SEQRES 19 A 874 PRO VAL ARG PHE PHE GLY LYS VAL GLN VAL ASN PRO ASP
SEQRES 20 A 874 GLY SER ARG LYS TRP VAL ASP GLY ASP VAL VAL GLN ALA
SEQRES 21 A 874 LEU ALA TYR ASP VAL PRO ILE PRO GLY TYR GLY THR LYS
SEQRES 22 A 874 ASN THR ILE SER LEU ARG LEU TRP GLU ALA LYS ALA ARG
SEQRES 23 A 874 ALA GLU ASP LEU ASP LEU PHE GLN PHE ASN GLU GLY GLU
SEQRES 24 A 874 TYR GLU LEU ALA ALA GLN LEU HIS SER ARG ALA GLN GLN
SEQRES 25 A 874 ILE CYS THR VAL LEU TYR PRO GLY ASP ALA THR GLU ASN
SEQRES 26 A 874 GLY LYS LEU LEU ARG LEU LYS GLN GLN PHE PHE LEU CYS
SEQRES 27 A 874 SER ALA SER LEU GLN ASP ILE ILE SER ARG PHE HIS GLU
SEQRES 28 A 874 ARG SER THR THR GLU GLY SER ARG LYS TRP SER GLU PHE
SEQRES 29 A 874 PRO SER LYS VAL ALA VAL GLN MET ASN ASP THR HIS PRO
SEQRES 30 A 874 THR LEU ALA ILE PRO GLU LEU MET ARG LEU LEU MET ASP
SEQRES 31 A 874 ASP ASN GLY LEU GLY TRP ASP GLU ALA TRP ASP VAL THR
SEQRES 32 A 874 SER LYS THR VAL ALA TYR THR ASN HIS THR VAL LEU PRO
SEQRES 33 A 874 GLU ALA LEU GLU LYS TRP SER GLN SER LEU MET TRP LYS
SEQRES 34 A 874 LEU LEU PRO ARG HIS MET GLU ILE ILE GLU GLU ILE ASP
SEQRES 35 A 874 LYS ARG PHE VAL GLN THR ILE ARG ASP THR ARG VAL ASP
SEQRES 36 A 874 LEU GLU ASP LYS ILE SER SER LEU SER ILE LEU ASP ASN
SEQRES 37 A 874 ASN PRO GLN LYS PRO VAL VAL ARG MET ALA ASN LEU CYS
SEQRES 38 A 874 VAL VAL SER SER HIS THR VAL ASN GLY VAL ALA GLN LEU
SEQRES 39 A 874 HIS SER ASP ILE LEU LYS ALA GLU LEU PHE ALA ASP TYR
SEQRES 40 A 874 VAL SER ILE TRP PRO ASN LYS PHE GLN ASN LYS THR ASN
SEQRES 41 A 874 GLY ILE THR PRO ARG ARG TRP LEU ARG PHE CYS SER PRO
SEQRES 42 A 874 GLU LEU SER ASP ILE ILE THR LYS TRP LEU LYS THR ASP
SEQRES 43 A 874 LYS TRP ILE THR ASP LEU ASP LEU LEU THR GLY LEU ARG
SEQRES 44 A 874 GLN PHE ALA ASP ASN GLU GLU LEU GLN SER GLU TRP ALA
SEQRES 45 A 874 SER ALA LYS THR ALA ASN LYS LYS ARG LEU ALA GLN TYR
SEQRES 46 A 874 ILE GLU ARG VAL THR GLY VAL SER ILE ASP PRO THR SER
SEQRES 47 A 874 LEU PHE ASP ILE GLN VAL LYS ARG ILE HIS GLU TYR LYS
SEQRES 48 A 874 ARG GLN LEU MET ASN ILE LEU GLY VAL VAL TYR ARG PHE
SEQRES 49 A 874 LYS LYS LEU LYS GLU MET LYS PRO GLU GLU ARG LYS LYS
SEQRES 50 A 874 THR VAL PRO ARG THR VAL MET ILE GLY GLY LYS ALA PHE
SEQRES 51 A 874 ALA THR TYR THR ASN ALA LYS ARG ILE VAL LYS LEU VAL
SEQRES 52 A 874 ASN ASP VAL GLY ASP VAL VAL ASN SER ASP PRO GLU VAL
SEQRES 53 A 874 ASN GLU TYR LEU LYS VAL VAL PHE VAL PRO ASN TYR ASN
SEQRES 54 A 874 VAL THR VAL ALA GLU MET LEU ILE PRO GLY SER GLU LEU
SEQRES 55 A 874 SER GLN HIS ILE SER THR ALA GLY MET GLU ALA SER GLY
SEQRES 56 A 874 THR SER ASN MET LYS PHE ALA LEU ASN GLY CYS LEU ILE
SEQRES 57 A 874 ILE GLY THR LEU ASP GLY ALA ASN VAL GLU ILE ARG GLU
SEQRES 58 A 874 GLU VAL GLY GLU GLU ASN PHE PHE LEU PHE GLY ALA THR
SEQRES 59 A 874 ALA ASP GLN VAL PRO ARG LEU ARG LYS GLU ARG GLU ASP
SEQRES 60 A 874 GLY LEU PHE LYS PRO ASP PRO ARG PHE GLU GLU ALA LYS
SEQRES 61 A 874 GLN PHE VAL LYS SER GLY VAL PHE GLY SER TYR ASP TYR
SEQRES 62 A 874 GLY PRO LEU LEU ASP SER LEU GLU GLY ASN THR GLY PHE
SEQRES 63 A 874 GLY ARG GLY ASP TYR PHE LEU VAL GLY TYR ASP PHE PRO
SEQRES 64 A 874 SER TYR MET ASP ALA GLN ALA LYS VAL ASP GLU ALA TYR
SEQRES 65 A 874 LYS ASP ARG LYS GLY TRP LEU LYS MET SER ILE LEU SER
SEQRES 66 A 874 THR ALA GLY SER GLY LYS PHE SER SER ASP ARG THR ILE
SEQRES 67 A 874 ALA GLN TYR ALA LYS GLU ILE TRP ASN ILE GLU ALA CYS
SEQRES 68 A 874 PRO VAL PRO
SEQRES 1 B 874 MET HIS HIS HIS HIS HIS HIS GLY LYS PRO ILE PRO ASN
SEQRES 2 B 874 PRO LEU LEU GLY LEU ASP SER THR GLU ASN LEU TYR PHE
SEQRES 3 B 874 GLN GLY ILE ASP PRO PHE THR MET ALA ASN ALA ASN GLY
SEQRES 4 B 874 LYS ALA ALA THR SER LEU PRO GLU LYS ILE SER ALA LYS
SEQRES 5 B 874 ALA ASN PRO GLU ALA ASP ASP ALA THR GLU ILE ALA GLY
SEQRES 6 B 874 ASN ILE VAL TYR HIS ALA LYS TYR SER PRO HIS PHE SER
SEQRES 7 B 874 PRO LEU LYS PHE GLY PRO GLU GLN ALA LEU TYR ALA THR
SEQRES 8 B 874 ALA GLU SER LEU ARG ASP ARG LEU ILE GLN LEU TRP ASN
SEQRES 9 B 874 GLU THR TYR VAL HIS PHE ASN LYS VAL ASP PRO LYS GLN
SEQRES 10 B 874 THR TYR TYR LEU SER MET GLU TYR LEU GLN GLY ARG ALA
SEQRES 11 B 874 LEU THR ASN ALA ILE GLY ASN LEU ASN LEU GLN GLY PRO
SEQRES 12 B 874 TYR ALA ASP ALA LEU ARG THR LEU GLY TYR GLU LEU GLU
SEQRES 13 B 874 GLU ILE ALA GLU GLN GLU LYS ASP ALA ALA LEU GLY ASN
SEQRES 14 B 874 GLY GLY LEU GLY ARG LEU ALA SER CYS PHE LEU ASP SER
SEQRES 15 B 874 MET ALA THR LEU ASN LEU PRO ALA TRP GLY TYR GLY LEU
SEQRES 16 B 874 ARG TYR ARG HIS GLY LEU PHE LYS GLN ILE ILE THR LYS
SEQRES 17 B 874 LYS GLY GLN GLU GLU ILE PRO GLU ASP TRP LEU GLU LYS
SEQRES 18 B 874 PHE SER PRO TRP GLU ILE VAL ARG HIS ASP VAL VAL PHE
SEQRES 19 B 874 PRO VAL ARG PHE PHE GLY LYS VAL GLN VAL ASN PRO ASP
SEQRES 20 B 874 GLY SER ARG LYS TRP VAL ASP GLY ASP VAL VAL GLN ALA
SEQRES 21 B 874 LEU ALA TYR ASP VAL PRO ILE PRO GLY TYR GLY THR LYS
SEQRES 22 B 874 ASN THR ILE SER LEU ARG LEU TRP GLU ALA LYS ALA ARG
SEQRES 23 B 874 ALA GLU ASP LEU ASP LEU PHE GLN PHE ASN GLU GLY GLU
SEQRES 24 B 874 TYR GLU LEU ALA ALA GLN LEU HIS SER ARG ALA GLN GLN
SEQRES 25 B 874 ILE CYS THR VAL LEU TYR PRO GLY ASP ALA THR GLU ASN
SEQRES 26 B 874 GLY LYS LEU LEU ARG LEU LYS GLN GLN PHE PHE LEU CYS
SEQRES 27 B 874 SER ALA SER LEU GLN ASP ILE ILE SER ARG PHE HIS GLU
SEQRES 28 B 874 ARG SER THR THR GLU GLY SER ARG LYS TRP SER GLU PHE
SEQRES 29 B 874 PRO SER LYS VAL ALA VAL GLN MET ASN ASP THR HIS PRO
SEQRES 30 B 874 THR LEU ALA ILE PRO GLU LEU MET ARG LEU LEU MET ASP
SEQRES 31 B 874 ASP ASN GLY LEU GLY TRP ASP GLU ALA TRP ASP VAL THR
SEQRES 32 B 874 SER LYS THR VAL ALA TYR THR ASN HIS THR VAL LEU PRO
SEQRES 33 B 874 GLU ALA LEU GLU LYS TRP SER GLN SER LEU MET TRP LYS
SEQRES 34 B 874 LEU LEU PRO ARG HIS MET GLU ILE ILE GLU GLU ILE ASP
SEQRES 35 B 874 LYS ARG PHE VAL GLN THR ILE ARG ASP THR ARG VAL ASP
SEQRES 36 B 874 LEU GLU ASP LYS ILE SER SER LEU SER ILE LEU ASP ASN
SEQRES 37 B 874 ASN PRO GLN LYS PRO VAL VAL ARG MET ALA ASN LEU CYS
SEQRES 38 B 874 VAL VAL SER SER HIS THR VAL ASN GLY VAL ALA GLN LEU
SEQRES 39 B 874 HIS SER ASP ILE LEU LYS ALA GLU LEU PHE ALA ASP TYR
SEQRES 40 B 874 VAL SER ILE TRP PRO ASN LYS PHE GLN ASN LYS THR ASN
SEQRES 41 B 874 GLY ILE THR PRO ARG ARG TRP LEU ARG PHE CYS SER PRO
SEQRES 42 B 874 GLU LEU SER ASP ILE ILE THR LYS TRP LEU LYS THR ASP
SEQRES 43 B 874 LYS TRP ILE THR ASP LEU ASP LEU LEU THR GLY LEU ARG
SEQRES 44 B 874 GLN PHE ALA ASP ASN GLU GLU LEU GLN SER GLU TRP ALA
SEQRES 45 B 874 SER ALA LYS THR ALA ASN LYS LYS ARG LEU ALA GLN TYR
SEQRES 46 B 874 ILE GLU ARG VAL THR GLY VAL SER ILE ASP PRO THR SER
SEQRES 47 B 874 LEU PHE ASP ILE GLN VAL LYS ARG ILE HIS GLU TYR LYS
SEQRES 48 B 874 ARG GLN LEU MET ASN ILE LEU GLY VAL VAL TYR ARG PHE
SEQRES 49 B 874 LYS LYS LEU LYS GLU MET LYS PRO GLU GLU ARG LYS LYS
SEQRES 50 B 874 THR VAL PRO ARG THR VAL MET ILE GLY GLY LYS ALA PHE
SEQRES 51 B 874 ALA THR TYR THR ASN ALA LYS ARG ILE VAL LYS LEU VAL
SEQRES 52 B 874 ASN ASP VAL GLY ASP VAL VAL ASN SER ASP PRO GLU VAL
SEQRES 53 B 874 ASN GLU TYR LEU LYS VAL VAL PHE VAL PRO ASN TYR ASN
SEQRES 54 B 874 VAL THR VAL ALA GLU MET LEU ILE PRO GLY SER GLU LEU
SEQRES 55 B 874 SER GLN HIS ILE SER THR ALA GLY MET GLU ALA SER GLY
SEQRES 56 B 874 THR SER ASN MET LYS PHE ALA LEU ASN GLY CYS LEU ILE
SEQRES 57 B 874 ILE GLY THR LEU ASP GLY ALA ASN VAL GLU ILE ARG GLU
SEQRES 58 B 874 GLU VAL GLY GLU GLU ASN PHE PHE LEU PHE GLY ALA THR
SEQRES 59 B 874 ALA ASP GLN VAL PRO ARG LEU ARG LYS GLU ARG GLU ASP
SEQRES 60 B 874 GLY LEU PHE LYS PRO ASP PRO ARG PHE GLU GLU ALA LYS
SEQRES 61 B 874 GLN PHE VAL LYS SER GLY VAL PHE GLY SER TYR ASP TYR
SEQRES 62 B 874 GLY PRO LEU LEU ASP SER LEU GLU GLY ASN THR GLY PHE
SEQRES 63 B 874 GLY ARG GLY ASP TYR PHE LEU VAL GLY TYR ASP PHE PRO
SEQRES 64 B 874 SER TYR MET ASP ALA GLN ALA LYS VAL ASP GLU ALA TYR
SEQRES 65 B 874 LYS ASP ARG LYS GLY TRP LEU LYS MET SER ILE LEU SER
SEQRES 66 B 874 THR ALA GLY SER GLY LYS PHE SER SER ASP ARG THR ILE
SEQRES 67 B 874 ALA GLN TYR ALA LYS GLU ILE TRP ASN ILE GLU ALA CYS
SEQRES 68 B 874 PRO VAL PRO
HET GLC C 1 12
HET GLC C 2 11
HET GLC C 3 11
HET GLC D 1 12
HET GLC D 2 11
HET GLC D 3 11
HET PLP A 901 15
HET PEG A1842 7
HET PLP B 901 15
HET GOL B1842 6
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM GOL GLYCEROL
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN PLP VITAMIN B6 PHOSPHATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GLC 6(C6 H12 O6)
FORMUL 5 PLP 2(C8 H10 N O6 P)
FORMUL 6 PEG C4 H10 O3
FORMUL 8 GOL C3 H8 O3
FORMUL 9 HOH *919(H2 O)
HELIX 1 1 ASP A 26 SER A 41 1 16
HELIX 2 2 GLY A 50 ASP A 81 1 32
HELIX 3 3 ALA A 97 LEU A 105 1 9
HELIX 4 4 LEU A 107 LEU A 118 1 12
HELIX 5 5 GLU A 121 GLN A 128 1 8
HELIX 6 6 GLY A 137 LEU A 153 1 17
HELIX 7 7 ARG A 253 LEU A 257 5 5
HELIX 8 8 ASP A 258 GLU A 264 1 7
HELIX 9 9 GLU A 266 ALA A 271 1 6
HELIX 10 10 ALA A 271 CYS A 281 1 11
HELIX 11 11 THR A 290 ARG A 319 1 30
HELIX 12 12 LYS A 327 SER A 329 5 3
HELIX 13 13 GLU A 330 LYS A 334 1 5
HELIX 14 14 LEU A 346 ASP A 357 1 12
HELIX 15 15 GLY A 362 THR A 373 1 12
HELIX 16 16 LEU A 382 LEU A 386 5 5
HELIX 17 17 GLN A 391 LEU A 398 1 8
HELIX 18 18 LEU A 398 ARG A 420 1 23
HELIX 19 19 VAL A 421 ASP A 425 5 5
HELIX 20 20 LYS A 426 SER A 431 1 6
HELIX 21 21 MET A 444 SER A 452 1 9
HELIX 22 22 ALA A 459 GLU A 469 1 11
HELIX 23 23 PHE A 471 TRP A 478 1 8
HELIX 24 24 PRO A 491 CYS A 498 1 8
HELIX 25 25 SER A 499 LYS A 511 1 13
HELIX 26 26 ASP A 513 THR A 517 5 5
HELIX 27 27 ASP A 518 ALA A 529 5 12
HELIX 28 28 ASN A 531 GLY A 558 1 28
HELIX 29 29 ARG A 579 MET A 597 1 19
HELIX 30 30 LYS A 598 LYS A 603 1 6
HELIX 31 31 TYR A 620 SER A 639 1 20
HELIX 32 32 ASN A 656 ILE A 664 1 9
HELIX 33 33 GLY A 682 ASN A 691 1 10
HELIX 34 34 ALA A 702 GLY A 711 1 10
HELIX 35 35 GLU A 712 PHE A 715 5 4
HELIX 36 36 GLN A 724 ASP A 734 1 11
HELIX 37 37 ASP A 740 SER A 752 1 13
HELIX 38 38 TYR A 760 ASP A 765 1 6
HELIX 39 39 SER A 766 GLU A 768 5 3
HELIX 40 40 LEU A 780 GLY A 815 1 36
HELIX 41 41 SER A 816 PHE A 819 5 4
HELIX 42 42 SER A 820 ILE A 832 1 13
HELIX 43 43 ASP B 26 SER B 41 1 16
HELIX 44 44 GLY B 50 ASP B 81 1 32
HELIX 45 45 ALA B 97 LEU B 105 1 9
HELIX 46 46 LEU B 107 LEU B 118 1 12
HELIX 47 47 GLU B 121 GLN B 128 1 8
HELIX 48 48 GLY B 137 LEU B 153 1 17
HELIX 49 49 ARG B 253 LEU B 257 5 5
HELIX 50 50 ASP B 258 GLU B 264 1 7
HELIX 51 51 GLU B 266 ALA B 271 1 6
HELIX 52 52 ALA B 271 CYS B 281 1 11
HELIX 53 53 THR B 290 ARG B 319 1 30
HELIX 54 54 LYS B 327 SER B 329 5 3
HELIX 55 55 GLU B 330 LYS B 334 1 5
HELIX 56 56 LEU B 346 ASP B 357 1 12
HELIX 57 57 GLY B 362 THR B 373 1 12
HELIX 58 58 LEU B 382 LEU B 386 5 5
HELIX 59 59 GLN B 391 LEU B 398 1 8
HELIX 60 60 LEU B 398 ASP B 418 1 21
HELIX 61 61 ARG B 420 ASP B 425 5 6
HELIX 62 62 LYS B 426 SER B 431 1 6
HELIX 63 63 MET B 444 SER B 452 1 9
HELIX 64 64 ALA B 459 GLU B 469 1 11
HELIX 65 65 PHE B 471 TRP B 478 1 8
HELIX 66 66 PRO B 491 CYS B 498 1 8
HELIX 67 67 SER B 499 LYS B 511 1 13
HELIX 68 68 ASP B 513 THR B 517 5 5
HELIX 69 69 ASP B 518 ALA B 529 5 12
HELIX 70 70 ASN B 531 GLY B 558 1 28
HELIX 71 71 HIS B 575 LYS B 578 5 4
HELIX 72 72 ARG B 579 MET B 597 1 19
HELIX 73 73 LYS B 598 LYS B 603 1 6
HELIX 74 74 TYR B 620 SER B 639 1 20
HELIX 75 75 ASN B 656 SER B 667 1 12
HELIX 76 76 GLY B 682 ASN B 691 1 10
HELIX 77 77 ALA B 702 GLY B 711 1 10
HELIX 78 78 GLU B 712 PHE B 715 5 4
HELIX 79 79 GLN B 724 ASP B 734 1 11
HELIX 80 80 ASP B 740 SER B 752 1 13
HELIX 81 81 TYR B 760 ASP B 765 1 6
HELIX 82 82 SER B 766 GLU B 768 5 3
HELIX 83 83 LEU B 780 GLY B 815 1 36
HELIX 84 84 SER B 816 PHE B 819 5 4
HELIX 85 85 SER B 820 ILE B 832 1 13
SHEET 1 AA 9 ILE A 194 PHE A 205 0
SHEET 2 AA 9 ASP A 223 PRO A 235 -1 O ASP A 223 N PHE A 205
SHEET 3 AA 9 THR A 242 LYS A 251 -1 O ILE A 243 N ILE A 234
SHEET 4 AA 9 ALA A 157 LEU A 162 1 O GLY A 159 N ARG A 246
SHEET 5 AA 9 GLN A 84 LEU A 88 1 O THR A 85 N TRP A 158
SHEET 6 AA 9 VAL A 335 ASN A 340 1 O ALA A 336 N TYR A 86
SHEET 7 AA 9 VAL A 374 THR A 377 1 O ALA A 375 N MET A 339
SHEET 8 AA 9 THR A 454 GLY A 457 1 O THR A 454 N TYR A 376
SHEET 9 AA 9 PHE A 482 ASN A 484 1 O GLN A 483 N GLY A 457
SHEET 1 AB 2 LYS A 170 THR A 174 0
SHEET 2 AB 2 GLY A 177 ILE A 181 -1 O GLY A 177 N THR A 174
SHEET 1 AC 2 LYS A 208 VAL A 211 0
SHEET 2 AC 2 ARG A 217 VAL A 220 -1 O LYS A 218 N GLN A 210
SHEET 1 AD 3 LYS A 388 SER A 390 0
SHEET 2 AD 3 VAL A 441 ARG A 443 -1 O VAL A 442 N TRP A 389
SHEET 3 AD 3 LEU A 433 ASP A 434 -1 O ASP A 434 N VAL A 441
SHEET 1 AE 6 LEU A 647 VAL A 652 0
SHEET 2 AE 6 ARG A 608 GLY A 613 1 O ARG A 608 N LYS A 648
SHEET 3 AE 6 LEU A 566 VAL A 571 1 O LEU A 566 N THR A 609
SHEET 4 AE 6 LEU A 669 HIS A 672 1 O LEU A 669 N ILE A 569
SHEET 5 AE 6 LEU A 694 GLY A 697 1 O LEU A 694 N SER A 670
SHEET 6 AE 6 PHE A 716 LEU A 717 1 O PHE A 716 N GLY A 697
SHEET 1 BA 9 ILE B 194 PHE B 205 0
SHEET 2 BA 9 ASP B 223 PRO B 235 -1 O ASP B 223 N PHE B 205
SHEET 3 BA 9 THR B 242 LYS B 251 -1 O ILE B 243 N ILE B 234
SHEET 4 BA 9 ALA B 157 LEU B 162 1 O GLY B 159 N ARG B 246
SHEET 5 BA 9 GLN B 84 LEU B 88 1 O THR B 85 N TRP B 158
SHEET 6 BA 9 VAL B 335 ASN B 340 1 O ALA B 336 N TYR B 86
SHEET 7 BA 9 VAL B 374 THR B 377 1 O ALA B 375 N MET B 339
SHEET 8 BA 9 THR B 454 GLY B 457 1 O THR B 454 N TYR B 376
SHEET 9 BA 9 PHE B 482 ASN B 484 1 O GLN B 483 N GLY B 457
SHEET 1 BB 2 LYS B 170 THR B 174 0
SHEET 2 BB 2 GLY B 177 ILE B 181 -1 O GLY B 177 N THR B 174
SHEET 1 BC 2 LYS B 208 VAL B 211 0
SHEET 2 BC 2 ARG B 217 VAL B 220 -1 O LYS B 218 N GLN B 210
SHEET 1 BD 3 LYS B 388 SER B 390 0
SHEET 2 BD 3 VAL B 441 ARG B 443 -1 O VAL B 442 N TRP B 389
SHEET 3 BD 3 LEU B 433 ASP B 434 -1 O ASP B 434 N VAL B 441
SHEET 1 BE 6 LEU B 647 VAL B 652 0
SHEET 2 BE 6 ARG B 608 GLY B 613 1 O ARG B 608 N LYS B 648
SHEET 3 BE 6 LEU B 566 VAL B 571 1 O LEU B 566 N THR B 609
SHEET 4 BE 6 LEU B 669 HIS B 672 1 O LEU B 669 N ILE B 569
SHEET 5 BE 6 LEU B 694 GLY B 697 1 O LEU B 694 N SER B 670
SHEET 6 BE 6 PHE B 716 LEU B 717 1 O PHE B 716 N GLY B 697
LINK NZ LYS A 687 C4A PLP A 901 1555 1555 1.51
LINK NZ LYS B 687 C4A PLP B 901 1555 1555 1.25
LINK O4 GLC C 1 C1 GLC C 2 1555 1555 1.42
LINK O4 GLC C 2 C1 GLC C 3 1555 1555 1.42
LINK O4 GLC D 1 C1 GLC D 2 1555 1555 1.43
LINK O4 GLC D 2 C1 GLC D 3 1555 1555 1.43
CRYST1 83.713 116.072 94.342 90.00 107.38 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011946 0.000000 0.003739 0.00000
SCALE2 0.000000 0.008615 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011107 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
