HEADER TRANSFERASE 12-NOV-07 2VGB
TITLE HUMAN ERYTHROCYTE PYRUVATE KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRUVATE KINASE ISOZYMES R/L;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: RESIDUES 47-574;
COMPND 5 SYNONYM: R-TYPE/L-TYPE PYRUVATE KINASE, RED CELL/LIVER PYRUVATE
COMPND 6 KINASE, PYRUVATE KINASE 1, PYRUVATE KINASE;
COMPND 7 EC: 2.7.1.40;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS METAL-BINDING, PHOSPHORYLATION, PYRUVATE KINASE IN THE ACTIVE R-
KEYWDS 2 STATE, KINASE, PYRUVATE, MAGNESIUM, GLYCOLYSIS, TRANSFERASE, DISEASE
KEYWDS 3 MUTATION
EXPDTA X-RAY DIFFRACTION
AUTHOR G.VALENTINI,L.CHIARELLI,R.FORTIN,M.DOLZAN,A.GALIZZI,D.J.ABRAHAM,
AUTHOR 2 C.WANG,P.BIANCHI,A.ZANELLA,A.MATTEVI
REVDAT 7 13-DEC-23 2VGB 1 HETSYN
REVDAT 6 29-JUL-20 2VGB 1 COMPND REMARK HETNAM LINK
REVDAT 6 2 1 SITE
REVDAT 5 08-MAY-19 2VGB 1 REMARK
REVDAT 4 16-MAY-18 2VGB 1 REMARK
REVDAT 3 13-JUL-11 2VGB 1 VERSN
REVDAT 2 24-FEB-09 2VGB 1 VERSN
REVDAT 1 20-NOV-07 2VGB 0
SPRSDE 20-NOV-07 2VGB 1LIU
JRNL AUTH G.VALENTINI,L.R.CHIARELLI,R.FORTIN,M.DOLZAN,A.GALIZZI,
JRNL AUTH 2 D.J.ABRAHAM,C.WANG,P.BIANCHI,A.ZANELLA,A.MATTEVI
JRNL TITL STRUCTURE AND FUNCTION OF HUMAN ERYTHROCYTE PYRUVATE KINASE.
JRNL TITL 2 MOLECULAR BASIS OF NONSPHEROCYTIC HEMOLYTIC ANEMIA.
JRNL REF J.BIOL.CHEM. V. 277 23807 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11960989
JRNL DOI 10.1074/JBC.M202107200
REMARK 2
REMARK 2 RESOLUTION. 2.73 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.73
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 52174
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) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2780
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.73
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.79
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3194
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3340
REMARK 3 BIN FREE R VALUE SET COUNT : 151
REMARK 3 BIN FREE R VALUE : 0.3840
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15423
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 124
REMARK 3 SOLVENT ATOMS : 65
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.14000
REMARK 3 B22 (A**2) : 0.20000
REMARK 3 B33 (A**2) : -0.05000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.12000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.416
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.332
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 35.492
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.915
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.881
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15782 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 21409 ; 1.513 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2029 ; 5.423 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 657 ;36.011 ;23.014
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2668 ;20.809 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 158 ;23.116 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2490 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11775 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 7652 ; 0.257 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 10829 ; 0.322 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 658 ; 0.163 ; 0.200
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): 116 ; 0.540 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.315 ; 0.200
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): 10104 ; 0.399 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16275 ; 0.785 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5710 ; 1.546 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5134 ; 2.564 ; 4.500
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 : 3
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 57 A 161 1
REMARK 3 1 B 57 B 161 1
REMARK 3 1 C 57 C 161 1
REMARK 3 1 D 57 D 161 1
REMARK 3 2 A 261 A 430 1
REMARK 3 2 B 261 B 430 1
REMARK 3 2 C 261 C 430 1
REMARK 3 2 D 261 D 430 1
REMARK 3 3 A 580 A 580 4
REMARK 3 3 B 580 B 580 4
REMARK 3 3 C 580 C 580 4
REMARK 3 3 D 580 D 580 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 2066 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 2066 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 2066 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 2066 ; 0.05 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 A (A): 20 ; 0.28 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 20 ; 0.62 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 20 ; 0.43 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 D (A): 20 ; 0.35 ; 0.50
REMARK 3 TIGHT THERMAL 1 A (A**2): 2066 ; 0.09 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 2066 ; 0.09 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 2066 ; 0.10 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 2066 ; 0.10 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 20 ; 0.83 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 20 ; 1.25 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 20 ; 1.17 ; 2.00
REMARK 3 MEDIUM THERMAL 1 D (A**2): 20 ; 0.81 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 162 A 260 4
REMARK 3 1 B 162 B 260 4
REMARK 3 1 C 162 C 260 4
REMARK 3 1 D 162 D 260 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 541 ; 0.40 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 B (A): 541 ; 0.30 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 C (A): 541 ; 0.23 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 D (A): 541 ; 0.25 ; 0.50
REMARK 3 MEDIUM THERMAL 2 A (A**2): 541 ; 0.41 ; 2.00
REMARK 3 MEDIUM THERMAL 2 B (A**2): 541 ; 0.36 ; 2.00
REMARK 3 MEDIUM THERMAL 2 C (A**2): 541 ; 0.44 ; 2.00
REMARK 3 MEDIUM THERMAL 2 D (A**2): 541 ; 0.46 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 431 A 573 1
REMARK 3 1 B 431 B 573 1
REMARK 3 1 C 431 C 573 1
REMARK 3 1 D 431 D 573 1
REMARK 3 2 A 581 A 581 4
REMARK 3 2 B 581 B 581 4
REMARK 3 2 C 581 C 581 4
REMARK 3 2 D 581 D 581 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 A (A): 1112 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 3 B (A): 1112 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 3 C (A): 1112 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 3 D (A): 1112 ; 0.05 ; 0.05
REMARK 3 MEDIUM POSITIONAL 3 A (A): 9 ; 0.26 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 B (A): 9 ; 0.24 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 C (A): 9 ; 0.19 ; 0.50
REMARK 3 MEDIUM POSITIONAL 3 D (A): 9 ; 0.35 ; 0.50
REMARK 3 TIGHT THERMAL 3 A (A**2): 1112 ; 0.08 ; 0.50
REMARK 3 TIGHT THERMAL 3 B (A**2): 1112 ; 0.07 ; 0.50
REMARK 3 TIGHT THERMAL 3 C (A**2): 1112 ; 0.09 ; 0.50
REMARK 3 TIGHT THERMAL 3 D (A**2): 1112 ; 0.08 ; 0.50
REMARK 3 MEDIUM THERMAL 3 A (A**2): 9 ; 0.28 ; 2.00
REMARK 3 MEDIUM THERMAL 3 B (A**2): 9 ; 0.46 ; 2.00
REMARK 3 MEDIUM THERMAL 3 C (A**2): 9 ; 0.31 ; 2.00
REMARK 3 MEDIUM THERMAL 3 D (A**2): 9 ; 0.38 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 57 A 160
REMARK 3 RESIDUE RANGE : A 261 A 573
REMARK 3 ORIGIN FOR THE GROUP (A): 27.9022 -6.5686 37.3360
REMARK 3 T TENSOR
REMARK 3 T11: -0.1639 T22: 0.0030
REMARK 3 T33: -0.1044 T12: 0.0735
REMARK 3 T13: 0.0277 T23: -0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 1.8780 L22: 1.8684
REMARK 3 L33: 1.5789 L12: 0.1428
REMARK 3 L13: 1.0719 L23: 0.4468
REMARK 3 S TENSOR
REMARK 3 S11: 0.2209 S12: 0.1550 S13: -0.3718
REMARK 3 S21: -0.0067 S22: -0.0333 S23: -0.0336
REMARK 3 S31: 0.3819 S32: 0.1085 S33: -0.1876
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 161 A 260
REMARK 3 ORIGIN FOR THE GROUP (A): 49.9273 24.1544 33.9283
REMARK 3 T TENSOR
REMARK 3 T11: -0.0942 T22: 0.2678
REMARK 3 T33: 0.5202 T12: -0.0302
REMARK 3 T13: 0.0805 T23: 0.1469
REMARK 3 L TENSOR
REMARK 3 L11: 10.1872 L22: 11.6732
REMARK 3 L33: 10.7703 L12: -0.0612
REMARK 3 L13: -0.3443 L23: 1.7381
REMARK 3 S TENSOR
REMARK 3 S11: 0.2367 S12: 0.7691 S13: 1.2113
REMARK 3 S21: -0.0518 S22: 0.1215 S23: -1.7249
REMARK 3 S31: -0.1413 S32: 0.2198 S33: -0.3582
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 57 B 160
REMARK 3 RESIDUE RANGE : B 261 B 573
REMARK 3 ORIGIN FOR THE GROUP (A): -6.8293 -27.9279 12.4788
REMARK 3 T TENSOR
REMARK 3 T11: -0.0210 T22: -0.1004
REMARK 3 T33: -0.0433 T12: -0.0130
REMARK 3 T13: 0.0600 T23: 0.0735
REMARK 3 L TENSOR
REMARK 3 L11: 2.2121 L22: 1.8136
REMARK 3 L33: 2.1907 L12: 0.3638
REMARK 3 L13: 1.1439 L23: -0.3382
REMARK 3 S TENSOR
REMARK 3 S11: 0.1057 S12: -0.3222 S13: -0.3799
REMARK 3 S21: 0.4001 S22: 0.0935 S23: -0.1703
REMARK 3 S31: 0.1305 S32: -0.0997 S33: -0.1991
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 : B 161 B 260
REMARK 3 ORIGIN FOR THE GROUP (A): -40.3889 -19.5393 2.0063
REMARK 3 T TENSOR
REMARK 3 T11: 0.0613 T22: 0.7433
REMARK 3 T33: 0.6573 T12: -0.0942
REMARK 3 T13: 0.1766 T23: 0.3164
REMARK 3 L TENSOR
REMARK 3 L11: 13.7967 L22: 9.8383
REMARK 3 L33: 17.6017 L12: -0.4967
REMARK 3 L13: -0.4898 L23: -1.9484
REMARK 3 S TENSOR
REMARK 3 S11: -1.0607 S12: -0.0025 S13: 0.3386
REMARK 3 S21: -0.0812 S22: 1.2946 S23: 1.9249
REMARK 3 S31: -0.3117 S32: -2.5602 S33: -0.2339
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 57 C 160
REMARK 3 RESIDUE RANGE : C 261 C 573
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0178 27.2882 30.8966
REMARK 3 T TENSOR
REMARK 3 T11: -0.1885 T22: -0.1358
REMARK 3 T33: -0.1258 T12: 0.0013
REMARK 3 T13: 0.0353 T23: -0.0331
REMARK 3 L TENSOR
REMARK 3 L11: 1.1948 L22: 1.3700
REMARK 3 L33: 2.1764 L12: -0.2406
REMARK 3 L13: 0.6342 L23: -0.2900
REMARK 3 S TENSOR
REMARK 3 S11: -0.0375 S12: 0.0208 S13: 0.1438
REMARK 3 S21: -0.0874 S22: -0.0253 S23: 0.0986
REMARK 3 S31: -0.1245 S32: -0.0410 S33: 0.0628
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 : C 161 C 260
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5615 21.1803 67.4129
REMARK 3 T TENSOR
REMARK 3 T11: 0.1113 T22: 0.0140
REMARK 3 T33: -0.1175 T12: -0.0393
REMARK 3 T13: 0.0336 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 7.3704 L22: 6.4412
REMARK 3 L33: 5.9273 L12: 0.0833
REMARK 3 L13: -0.0582 L23: 0.7559
REMARK 3 S TENSOR
REMARK 3 S11: 0.0701 S12: -0.4608 S13: -0.4480
REMARK 3 S21: 0.6801 S22: 0.1267 S23: -0.0665
REMARK 3 S31: 0.3466 S32: -0.0560 S33: -0.1968
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 57 D 160
REMARK 3 RESIDUE RANGE : D 261 D 573
REMARK 3 ORIGIN FOR THE GROUP (A): -11.0003 6.2724 -6.7195
REMARK 3 T TENSOR
REMARK 3 T11: -0.1963 T22: -0.1063
REMARK 3 T33: -0.1328 T12: -0.0021
REMARK 3 T13: 0.0132 T23: 0.0236
REMARK 3 L TENSOR
REMARK 3 L11: 1.1383 L22: 2.7547
REMARK 3 L33: 0.8158 L12: 0.3273
REMARK 3 L13: 0.2816 L23: 0.5332
REMARK 3 S TENSOR
REMARK 3 S11: -0.0934 S12: -0.0438 S13: 0.2294
REMARK 3 S21: 0.1680 S22: -0.0084 S23: 0.1378
REMARK 3 S31: -0.1126 S32: -0.0377 S33: 0.1018
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 : D 161 D 260
REMARK 3 ORIGIN FOR THE GROUP (A): -4.3537 -22.6928 -29.6628
REMARK 3 T TENSOR
REMARK 3 T11: 0.1643 T22: -0.0110
REMARK 3 T33: -0.0480 T12: -0.0416
REMARK 3 T13: 0.0659 T23: -0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 5.6513 L22: 8.0690
REMARK 3 L33: 6.4676 L12: 1.9334
REMARK 3 L13: -0.6495 L23: -1.3336
REMARK 3 S TENSOR
REMARK 3 S11: 0.0244 S12: 0.3304 S13: -0.2735
REMARK 3 S21: -1.1082 S22: 0.0727 S23: -0.2886
REMARK 3 S31: 0.5538 S32: 0.2116 S33: -0.0971
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 2VGB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1290034402.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 1.
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55091
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 2.100
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.24000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1PKN
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RECOMBINANT WILD-TYPE RPK WAS
REMARK 280 CRYSTALLIZED USING THE VAPOR DIFFUSION METHOD AT 22 C. WELL
REMARK 280 SOLUTIONS CONSISTED OF 50 MM MES/KOH, PH 6.4, 10 MM MNSO4, AND
REMARK 280 10-14% W/V PEG8000. HANGING DROPS WERE FORMED BY MIXING EQUAL
REMARK 280 VOLUMES OF 12 MG/ML PROTEIN IN 50 MM KCL, 5 MM FBP, 5 MM
REMARK 280 PHOSPHOGLYCOLATE, 20 MM POTASSIUM PHOSPHATE, PH 7.0, AND WELL
REMARK 280 SOLUTIONS., PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 295K
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 86.02900
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 21560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 89210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.1 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 LEU A 47
REMARK 465 THR A 48
REMARK 465 GLN A 49
REMARK 465 GLU A 50
REMARK 465 LEU A 51
REMARK 465 GLY A 52
REMARK 465 THR A 53
REMARK 465 ALA A 54
REMARK 465 PHE A 55
REMARK 465 PHE A 56
REMARK 465 SER A 574
REMARK 465 LEU B 47
REMARK 465 THR B 48
REMARK 465 GLN B 49
REMARK 465 GLU B 50
REMARK 465 LEU B 51
REMARK 465 GLY B 52
REMARK 465 THR B 53
REMARK 465 ALA B 54
REMARK 465 PHE B 55
REMARK 465 PHE B 56
REMARK 465 LEU B 167
REMARK 465 GLN B 168
REMARK 465 GLY B 169
REMARK 465 GLY B 170
REMARK 465 PRO B 171
REMARK 465 GLU B 172
REMARK 465 SER B 173
REMARK 465 GLU B 174
REMARK 465 VAL B 187
REMARK 465 ASP B 188
REMARK 465 PRO B 189
REMARK 465 ALA B 190
REMARK 465 PHE B 191
REMARK 465 ARG B 192
REMARK 465 THR B 193
REMARK 465 ARG B 194
REMARK 465 GLY B 195
REMARK 465 ASN B 196
REMARK 465 GLN B 229
REMARK 465 LYS B 230
REMARK 465 ILE B 231
REMARK 465 GLY B 232
REMARK 465 PRO B 233
REMARK 465 GLU B 234
REMARK 465 GLY B 235
REMARK 465 LEU B 236
REMARK 465 SER B 574
REMARK 465 LEU C 47
REMARK 465 THR C 48
REMARK 465 GLN C 49
REMARK 465 GLU C 50
REMARK 465 LEU C 51
REMARK 465 GLY C 52
REMARK 465 THR C 53
REMARK 465 ALA C 54
REMARK 465 PHE C 55
REMARK 465 PHE C 56
REMARK 465 SER C 574
REMARK 465 LEU D 47
REMARK 465 THR D 48
REMARK 465 GLN D 49
REMARK 465 GLU D 50
REMARK 465 LEU D 51
REMARK 465 GLY D 52
REMARK 465 THR D 53
REMARK 465 ALA D 54
REMARK 465 PHE D 55
REMARK 465 PHE D 56
REMARK 465 LEU D 167
REMARK 465 GLN D 168
REMARK 465 GLY D 169
REMARK 465 GLY D 170
REMARK 465 PRO D 171
REMARK 465 SER D 574
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 OG SER B 89 O HOH B 2001 2.06
REMARK 500 O SER B 144 O HOH B 2004 2.14
REMARK 500 OE2 GLU D 315 OD2 ASP D 339 2.17
REMARK 500 OG SER C 89 O HOH C 2001 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CE1 HIS A 306 NH1 ARG B 322 1655 1.57
REMARK 500 CE1 HIS A 306 NH2 ARG B 322 1655 1.63
REMARK 500 NE2 HIS A 306 NH1 ARG B 322 1655 1.65
REMARK 500 CE1 HIS A 306 CZ ARG B 322 1655 1.67
REMARK 500 NE2 HIS A 306 CZ ARG B 322 1655 2.09
REMARK 500 NE2 GLN C 258 O ARG D 298 1556 2.17
REMARK 500 ND1 HIS A 306 NH2 ARG B 322 1655 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 LYS A 410 CD LYS A 410 CE -0.161
REMARK 500 LYS A 410 CE LYS A 410 NZ 0.338
REMARK 500 SER B 144 CB SER B 144 OG 0.360
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 VAL A 473 CB - CA - C ANGL. DEV. = -12.7 DEGREES
REMARK 500 VAL B 473 CB - CA - C ANGL. DEV. = -11.9 DEGREES
REMARK 500 VAL C 473 CB - CA - C ANGL. DEV. = -14.0 DEGREES
REMARK 500 LEU D 374 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 VAL D 473 CB - CA - C ANGL. DEV. = -12.1 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 VAL A 83 79.17 -158.49
REMARK 500 ALA A 84 148.77 174.10
REMARK 500 SER A 98 42.19 -142.40
REMARK 500 GLN A 168 99.87 -66.27
REMARK 500 ARG A 192 -14.66 -47.94
REMARK 500 ARG A 194 48.58 -99.23
REMARK 500 ASP A 220 78.29 53.54
REMARK 500 GLU A 234 -3.85 -152.42
REMARK 500 THR A 371 120.33 88.40
REMARK 500 LEU A 374 38.78 -146.41
REMARK 500 SER A 405 -97.90 -126.90
REMARK 500 LEU A 447 164.40 -49.94
REMARK 500 ARG A 486 -38.04 -33.69
REMARK 500 ASN A 566 16.29 -169.82
REMARK 500 GLN B 59 16.07 59.31
REMARK 500 VAL B 83 81.88 -160.49
REMARK 500 ALA B 84 150.75 170.94
REMARK 500 VAL B 213 119.39 -36.74
REMARK 500 ASP B 220 93.75 67.17
REMARK 500 ARG B 249 72.50 47.12
REMARK 500 GLU B 304 1.08 -61.30
REMARK 500 THR B 371 118.79 86.34
REMARK 500 LEU B 374 37.30 -152.58
REMARK 500 SER B 405 -96.30 -125.20
REMARK 500 PHE B 413 51.84 -141.65
REMARK 500 LEU B 447 169.02 -49.21
REMARK 500 ARG B 486 -37.44 -39.11
REMARK 500 THR B 556 -158.87 -134.88
REMARK 500 ASN B 566 14.34 -167.37
REMARK 500 VAL C 83 73.60 -159.17
REMARK 500 PHE C 119 1.00 -69.91
REMARK 500 ASP C 220 82.14 68.39
REMARK 500 THR C 371 119.97 86.19
REMARK 500 LEU C 374 40.89 -147.05
REMARK 500 SER C 405 -92.67 -126.84
REMARK 500 LEU C 447 167.50 -47.43
REMARK 500 ASN C 566 14.48 -169.51
REMARK 500 VAL D 83 79.76 -162.43
REMARK 500 ALA D 84 149.77 172.56
REMARK 500 PRO D 160 59.17 -69.56
REMARK 500 ASP D 220 82.42 61.76
REMARK 500 LYS D 230 133.97 -172.71
REMARK 500 THR D 371 123.28 90.82
REMARK 500 LEU D 374 36.00 -148.35
REMARK 500 SER D 405 -95.46 -127.35
REMARK 500 PHE D 413 55.67 -143.01
REMARK 500 THR D 556 -158.32 -134.04
REMARK 500 ASN D 566 11.48 -166.81
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 K A 582 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 118 OD1
REMARK 620 2 SER A 120 OG 73.9
REMARK 620 3 ASP A 156 OD1 88.5 147.7
REMARK 620 4 THR A 157 O 112.1 104.2 57.2
REMARK 620 5 PGA A 581 O2P 94.5 114.4 93.4 138.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 583 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 315 OE2
REMARK 620 2 ASP A 339 OD2 88.3
REMARK 620 3 PGA A 581 O1P 100.1 165.2
REMARK 620 4 PGA A 581 O1 94.0 94.5 72.9
REMARK 620 5 PGA A 581 O4P 165.9 104.1 69.5 92.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 586 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 118 OD1
REMARK 620 2 ASP B 156 OD1 94.1
REMARK 620 3 THR B 157 O 114.3 61.5
REMARK 620 4 PGA B 581 O2P 93.2 95.7 144.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 587 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 315 OE2
REMARK 620 2 ASP B 339 OD2 80.9
REMARK 620 3 PGA B 581 O1 94.5 94.2
REMARK 620 4 PGA B 581 O4P 153.0 117.4 103.1
REMARK 620 5 PGA B 581 O1P 101.1 169.8 75.8 64.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C 590 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 118 OD1
REMARK 620 2 ASP C 156 OD1 101.0
REMARK 620 3 THR C 157 O 121.6 61.7
REMARK 620 4 PGA C 581 O2P 98.4 100.1 137.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C 591 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 315 OE2
REMARK 620 2 ASP C 339 OD2 83.8
REMARK 620 3 PGA C 581 O1 88.4 91.1
REMARK 620 4 PGA C 581 O4P 166.0 108.3 84.3
REMARK 620 5 PGA C 581 O1P 99.8 159.0 68.5 66.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K D 594 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN D 118 OD1
REMARK 620 2 ASP D 156 OD1 100.8
REMARK 620 3 THR D 157 O 119.7 63.3
REMARK 620 4 PGA D 581 O2P 95.3 99.5 142.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN D 595 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 315 OE2
REMARK 620 2 ASP D 339 OD2 80.2
REMARK 620 3 PGA D 581 O1 90.5 86.5
REMARK 620 4 PGA D 581 O1P 111.9 155.8 73.0
REMARK 620 N 1 2 3
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 9-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "DA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LIY RELATED DB: PDB
REMARK 900 HUMAN ERYTHROCYTE PYRUVATE KINASE: ARG479HIS MUTANT
REMARK 900 RELATED ID: 1LIU RELATED DB: PDB
REMARK 900 HUMAN ERYTHROCYTE PYRUVATE KINASE
REMARK 900 RELATED ID: 1LIW RELATED DB: PDB
REMARK 900 HUMAN ERYTHROCYTE PYRUVATE KINASE: THR384MET MUTANT
REMARK 900 RELATED ID: 1LIX RELATED DB: PDB
REMARK 900 HUMAN ERYTHROCYTE PYRUVATE KINASE: ARG486TRP MUTANT
DBREF 2VGB A 47 574 UNP P30613 KPYR_HUMAN 47 574
DBREF 2VGB B 47 574 UNP P30613 KPYR_HUMAN 47 574
DBREF 2VGB C 47 574 UNP P30613 KPYR_HUMAN 47 574
DBREF 2VGB D 47 574 UNP P30613 KPYR_HUMAN 47 574
SEQRES 1 A 528 LEU THR GLN GLU LEU GLY THR ALA PHE PHE GLN GLN GLN
SEQRES 2 A 528 GLN LEU PRO ALA ALA MET ALA ASP THR PHE LEU GLU HIS
SEQRES 3 A 528 LEU CYS LEU LEU ASP ILE ASP SER GLU PRO VAL ALA ALA
SEQRES 4 A 528 ARG SER THR SER ILE ILE ALA THR ILE GLY PRO ALA SER
SEQRES 5 A 528 ARG SER VAL GLU ARG LEU LYS GLU MET ILE LYS ALA GLY
SEQRES 6 A 528 MET ASN ILE ALA ARG LEU ASN PHE SER HIS GLY SER HIS
SEQRES 7 A 528 GLU TYR HIS ALA GLU SER ILE ALA ASN VAL ARG GLU ALA
SEQRES 8 A 528 VAL GLU SER PHE ALA GLY SER PRO LEU SER TYR ARG PRO
SEQRES 9 A 528 VAL ALA ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG
SEQRES 10 A 528 THR GLY ILE LEU GLN GLY GLY PRO GLU SER GLU VAL GLU
SEQRES 11 A 528 LEU VAL LYS GLY SER GLN VAL LEU VAL THR VAL ASP PRO
SEQRES 12 A 528 ALA PHE ARG THR ARG GLY ASN ALA ASN THR VAL TRP VAL
SEQRES 13 A 528 ASP TYR PRO ASN ILE VAL ARG VAL VAL PRO VAL GLY GLY
SEQRES 14 A 528 ARG ILE TYR ILE ASP ASP GLY LEU ILE SER LEU VAL VAL
SEQRES 15 A 528 GLN LYS ILE GLY PRO GLU GLY LEU VAL THR GLN VAL GLU
SEQRES 16 A 528 ASN GLY GLY VAL LEU GLY SER ARG LYS GLY VAL ASN LEU
SEQRES 17 A 528 PRO GLY ALA GLN VAL ASP LEU PRO GLY LEU SER GLU GLN
SEQRES 18 A 528 ASP VAL ARG ASP LEU ARG PHE GLY VAL GLU HIS GLY VAL
SEQRES 19 A 528 ASP ILE VAL PHE ALA SER PHE VAL ARG LYS ALA SER ASP
SEQRES 20 A 528 VAL ALA ALA VAL ARG ALA ALA LEU GLY PRO GLU GLY HIS
SEQRES 21 A 528 GLY ILE LYS ILE ILE SER LYS ILE GLU ASN HIS GLU GLY
SEQRES 22 A 528 VAL LYS ARG PHE ASP GLU ILE LEU GLU VAL SER ASP GLY
SEQRES 23 A 528 ILE MET VAL ALA ARG GLY ASP LEU GLY ILE GLU ILE PRO
SEQRES 24 A 528 ALA GLU LYS VAL PHE LEU ALA GLN LYS MET MET ILE GLY
SEQRES 25 A 528 ARG CYS ASN LEU ALA GLY LYS PRO VAL VAL CYS ALA THR
SEQRES 26 A 528 GLN MET LEU GLU SER MET ILE THR LYS PRO ARG PRO THR
SEQRES 27 A 528 ARG ALA GLU THR SER ASP VAL ALA ASN ALA VAL LEU ASP
SEQRES 28 A 528 GLY ALA ASP CYS ILE MET LEU SER GLY GLU THR ALA LYS
SEQRES 29 A 528 GLY ASN PHE PRO VAL GLU ALA VAL LYS MET GLN HIS ALA
SEQRES 30 A 528 ILE ALA ARG GLU ALA GLU ALA ALA VAL TYR HIS ARG GLN
SEQRES 31 A 528 LEU PHE GLU GLU LEU ARG ARG ALA ALA PRO LEU SER ARG
SEQRES 32 A 528 ASP PRO THR GLU VAL THR ALA ILE GLY ALA VAL GLU ALA
SEQRES 33 A 528 ALA PHE LYS CYS CYS ALA ALA ALA ILE ILE VAL LEU THR
SEQRES 34 A 528 THR THR GLY ARG SER ALA GLN LEU LEU SER ARG TYR ARG
SEQRES 35 A 528 PRO ARG ALA ALA VAL ILE ALA VAL THR ARG SER ALA GLN
SEQRES 36 A 528 ALA ALA ARG GLN VAL HIS LEU CYS ARG GLY VAL PHE PRO
SEQRES 37 A 528 LEU LEU TYR ARG GLU PRO PRO GLU ALA ILE TRP ALA ASP
SEQRES 38 A 528 ASP VAL ASP ARG ARG VAL GLN PHE GLY ILE GLU SER GLY
SEQRES 39 A 528 LYS LEU ARG GLY PHE LEU ARG VAL GLY ASP LEU VAL ILE
SEQRES 40 A 528 VAL VAL THR GLY TRP ARG PRO GLY SER GLY TYR THR ASN
SEQRES 41 A 528 ILE MET ARG VAL LEU SER ILE SER
SEQRES 1 B 528 LEU THR GLN GLU LEU GLY THR ALA PHE PHE GLN GLN GLN
SEQRES 2 B 528 GLN LEU PRO ALA ALA MET ALA ASP THR PHE LEU GLU HIS
SEQRES 3 B 528 LEU CYS LEU LEU ASP ILE ASP SER GLU PRO VAL ALA ALA
SEQRES 4 B 528 ARG SER THR SER ILE ILE ALA THR ILE GLY PRO ALA SER
SEQRES 5 B 528 ARG SER VAL GLU ARG LEU LYS GLU MET ILE LYS ALA GLY
SEQRES 6 B 528 MET ASN ILE ALA ARG LEU ASN PHE SER HIS GLY SER HIS
SEQRES 7 B 528 GLU TYR HIS ALA GLU SER ILE ALA ASN VAL ARG GLU ALA
SEQRES 8 B 528 VAL GLU SER PHE ALA GLY SER PRO LEU SER TYR ARG PRO
SEQRES 9 B 528 VAL ALA ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG
SEQRES 10 B 528 THR GLY ILE LEU GLN GLY GLY PRO GLU SER GLU VAL GLU
SEQRES 11 B 528 LEU VAL LYS GLY SER GLN VAL LEU VAL THR VAL ASP PRO
SEQRES 12 B 528 ALA PHE ARG THR ARG GLY ASN ALA ASN THR VAL TRP VAL
SEQRES 13 B 528 ASP TYR PRO ASN ILE VAL ARG VAL VAL PRO VAL GLY GLY
SEQRES 14 B 528 ARG ILE TYR ILE ASP ASP GLY LEU ILE SER LEU VAL VAL
SEQRES 15 B 528 GLN LYS ILE GLY PRO GLU GLY LEU VAL THR GLN VAL GLU
SEQRES 16 B 528 ASN GLY GLY VAL LEU GLY SER ARG LYS GLY VAL ASN LEU
SEQRES 17 B 528 PRO GLY ALA GLN VAL ASP LEU PRO GLY LEU SER GLU GLN
SEQRES 18 B 528 ASP VAL ARG ASP LEU ARG PHE GLY VAL GLU HIS GLY VAL
SEQRES 19 B 528 ASP ILE VAL PHE ALA SER PHE VAL ARG LYS ALA SER ASP
SEQRES 20 B 528 VAL ALA ALA VAL ARG ALA ALA LEU GLY PRO GLU GLY HIS
SEQRES 21 B 528 GLY ILE LYS ILE ILE SER LYS ILE GLU ASN HIS GLU GLY
SEQRES 22 B 528 VAL LYS ARG PHE ASP GLU ILE LEU GLU VAL SER ASP GLY
SEQRES 23 B 528 ILE MET VAL ALA ARG GLY ASP LEU GLY ILE GLU ILE PRO
SEQRES 24 B 528 ALA GLU LYS VAL PHE LEU ALA GLN LYS MET MET ILE GLY
SEQRES 25 B 528 ARG CYS ASN LEU ALA GLY LYS PRO VAL VAL CYS ALA THR
SEQRES 26 B 528 GLN MET LEU GLU SER MET ILE THR LYS PRO ARG PRO THR
SEQRES 27 B 528 ARG ALA GLU THR SER ASP VAL ALA ASN ALA VAL LEU ASP
SEQRES 28 B 528 GLY ALA ASP CYS ILE MET LEU SER GLY GLU THR ALA LYS
SEQRES 29 B 528 GLY ASN PHE PRO VAL GLU ALA VAL LYS MET GLN HIS ALA
SEQRES 30 B 528 ILE ALA ARG GLU ALA GLU ALA ALA VAL TYR HIS ARG GLN
SEQRES 31 B 528 LEU PHE GLU GLU LEU ARG ARG ALA ALA PRO LEU SER ARG
SEQRES 32 B 528 ASP PRO THR GLU VAL THR ALA ILE GLY ALA VAL GLU ALA
SEQRES 33 B 528 ALA PHE LYS CYS CYS ALA ALA ALA ILE ILE VAL LEU THR
SEQRES 34 B 528 THR THR GLY ARG SER ALA GLN LEU LEU SER ARG TYR ARG
SEQRES 35 B 528 PRO ARG ALA ALA VAL ILE ALA VAL THR ARG SER ALA GLN
SEQRES 36 B 528 ALA ALA ARG GLN VAL HIS LEU CYS ARG GLY VAL PHE PRO
SEQRES 37 B 528 LEU LEU TYR ARG GLU PRO PRO GLU ALA ILE TRP ALA ASP
SEQRES 38 B 528 ASP VAL ASP ARG ARG VAL GLN PHE GLY ILE GLU SER GLY
SEQRES 39 B 528 LYS LEU ARG GLY PHE LEU ARG VAL GLY ASP LEU VAL ILE
SEQRES 40 B 528 VAL VAL THR GLY TRP ARG PRO GLY SER GLY TYR THR ASN
SEQRES 41 B 528 ILE MET ARG VAL LEU SER ILE SER
SEQRES 1 C 528 LEU THR GLN GLU LEU GLY THR ALA PHE PHE GLN GLN GLN
SEQRES 2 C 528 GLN LEU PRO ALA ALA MET ALA ASP THR PHE LEU GLU HIS
SEQRES 3 C 528 LEU CYS LEU LEU ASP ILE ASP SER GLU PRO VAL ALA ALA
SEQRES 4 C 528 ARG SER THR SER ILE ILE ALA THR ILE GLY PRO ALA SER
SEQRES 5 C 528 ARG SER VAL GLU ARG LEU LYS GLU MET ILE LYS ALA GLY
SEQRES 6 C 528 MET ASN ILE ALA ARG LEU ASN PHE SER HIS GLY SER HIS
SEQRES 7 C 528 GLU TYR HIS ALA GLU SER ILE ALA ASN VAL ARG GLU ALA
SEQRES 8 C 528 VAL GLU SER PHE ALA GLY SER PRO LEU SER TYR ARG PRO
SEQRES 9 C 528 VAL ALA ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG
SEQRES 10 C 528 THR GLY ILE LEU GLN GLY GLY PRO GLU SER GLU VAL GLU
SEQRES 11 C 528 LEU VAL LYS GLY SER GLN VAL LEU VAL THR VAL ASP PRO
SEQRES 12 C 528 ALA PHE ARG THR ARG GLY ASN ALA ASN THR VAL TRP VAL
SEQRES 13 C 528 ASP TYR PRO ASN ILE VAL ARG VAL VAL PRO VAL GLY GLY
SEQRES 14 C 528 ARG ILE TYR ILE ASP ASP GLY LEU ILE SER LEU VAL VAL
SEQRES 15 C 528 GLN LYS ILE GLY PRO GLU GLY LEU VAL THR GLN VAL GLU
SEQRES 16 C 528 ASN GLY GLY VAL LEU GLY SER ARG LYS GLY VAL ASN LEU
SEQRES 17 C 528 PRO GLY ALA GLN VAL ASP LEU PRO GLY LEU SER GLU GLN
SEQRES 18 C 528 ASP VAL ARG ASP LEU ARG PHE GLY VAL GLU HIS GLY VAL
SEQRES 19 C 528 ASP ILE VAL PHE ALA SER PHE VAL ARG LYS ALA SER ASP
SEQRES 20 C 528 VAL ALA ALA VAL ARG ALA ALA LEU GLY PRO GLU GLY HIS
SEQRES 21 C 528 GLY ILE LYS ILE ILE SER LYS ILE GLU ASN HIS GLU GLY
SEQRES 22 C 528 VAL LYS ARG PHE ASP GLU ILE LEU GLU VAL SER ASP GLY
SEQRES 23 C 528 ILE MET VAL ALA ARG GLY ASP LEU GLY ILE GLU ILE PRO
SEQRES 24 C 528 ALA GLU LYS VAL PHE LEU ALA GLN LYS MET MET ILE GLY
SEQRES 25 C 528 ARG CYS ASN LEU ALA GLY LYS PRO VAL VAL CYS ALA THR
SEQRES 26 C 528 GLN MET LEU GLU SER MET ILE THR LYS PRO ARG PRO THR
SEQRES 27 C 528 ARG ALA GLU THR SER ASP VAL ALA ASN ALA VAL LEU ASP
SEQRES 28 C 528 GLY ALA ASP CYS ILE MET LEU SER GLY GLU THR ALA LYS
SEQRES 29 C 528 GLY ASN PHE PRO VAL GLU ALA VAL LYS MET GLN HIS ALA
SEQRES 30 C 528 ILE ALA ARG GLU ALA GLU ALA ALA VAL TYR HIS ARG GLN
SEQRES 31 C 528 LEU PHE GLU GLU LEU ARG ARG ALA ALA PRO LEU SER ARG
SEQRES 32 C 528 ASP PRO THR GLU VAL THR ALA ILE GLY ALA VAL GLU ALA
SEQRES 33 C 528 ALA PHE LYS CYS CYS ALA ALA ALA ILE ILE VAL LEU THR
SEQRES 34 C 528 THR THR GLY ARG SER ALA GLN LEU LEU SER ARG TYR ARG
SEQRES 35 C 528 PRO ARG ALA ALA VAL ILE ALA VAL THR ARG SER ALA GLN
SEQRES 36 C 528 ALA ALA ARG GLN VAL HIS LEU CYS ARG GLY VAL PHE PRO
SEQRES 37 C 528 LEU LEU TYR ARG GLU PRO PRO GLU ALA ILE TRP ALA ASP
SEQRES 38 C 528 ASP VAL ASP ARG ARG VAL GLN PHE GLY ILE GLU SER GLY
SEQRES 39 C 528 LYS LEU ARG GLY PHE LEU ARG VAL GLY ASP LEU VAL ILE
SEQRES 40 C 528 VAL VAL THR GLY TRP ARG PRO GLY SER GLY TYR THR ASN
SEQRES 41 C 528 ILE MET ARG VAL LEU SER ILE SER
SEQRES 1 D 528 LEU THR GLN GLU LEU GLY THR ALA PHE PHE GLN GLN GLN
SEQRES 2 D 528 GLN LEU PRO ALA ALA MET ALA ASP THR PHE LEU GLU HIS
SEQRES 3 D 528 LEU CYS LEU LEU ASP ILE ASP SER GLU PRO VAL ALA ALA
SEQRES 4 D 528 ARG SER THR SER ILE ILE ALA THR ILE GLY PRO ALA SER
SEQRES 5 D 528 ARG SER VAL GLU ARG LEU LYS GLU MET ILE LYS ALA GLY
SEQRES 6 D 528 MET ASN ILE ALA ARG LEU ASN PHE SER HIS GLY SER HIS
SEQRES 7 D 528 GLU TYR HIS ALA GLU SER ILE ALA ASN VAL ARG GLU ALA
SEQRES 8 D 528 VAL GLU SER PHE ALA GLY SER PRO LEU SER TYR ARG PRO
SEQRES 9 D 528 VAL ALA ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG
SEQRES 10 D 528 THR GLY ILE LEU GLN GLY GLY PRO GLU SER GLU VAL GLU
SEQRES 11 D 528 LEU VAL LYS GLY SER GLN VAL LEU VAL THR VAL ASP PRO
SEQRES 12 D 528 ALA PHE ARG THR ARG GLY ASN ALA ASN THR VAL TRP VAL
SEQRES 13 D 528 ASP TYR PRO ASN ILE VAL ARG VAL VAL PRO VAL GLY GLY
SEQRES 14 D 528 ARG ILE TYR ILE ASP ASP GLY LEU ILE SER LEU VAL VAL
SEQRES 15 D 528 GLN LYS ILE GLY PRO GLU GLY LEU VAL THR GLN VAL GLU
SEQRES 16 D 528 ASN GLY GLY VAL LEU GLY SER ARG LYS GLY VAL ASN LEU
SEQRES 17 D 528 PRO GLY ALA GLN VAL ASP LEU PRO GLY LEU SER GLU GLN
SEQRES 18 D 528 ASP VAL ARG ASP LEU ARG PHE GLY VAL GLU HIS GLY VAL
SEQRES 19 D 528 ASP ILE VAL PHE ALA SER PHE VAL ARG LYS ALA SER ASP
SEQRES 20 D 528 VAL ALA ALA VAL ARG ALA ALA LEU GLY PRO GLU GLY HIS
SEQRES 21 D 528 GLY ILE LYS ILE ILE SER LYS ILE GLU ASN HIS GLU GLY
SEQRES 22 D 528 VAL LYS ARG PHE ASP GLU ILE LEU GLU VAL SER ASP GLY
SEQRES 23 D 528 ILE MET VAL ALA ARG GLY ASP LEU GLY ILE GLU ILE PRO
SEQRES 24 D 528 ALA GLU LYS VAL PHE LEU ALA GLN LYS MET MET ILE GLY
SEQRES 25 D 528 ARG CYS ASN LEU ALA GLY LYS PRO VAL VAL CYS ALA THR
SEQRES 26 D 528 GLN MET LEU GLU SER MET ILE THR LYS PRO ARG PRO THR
SEQRES 27 D 528 ARG ALA GLU THR SER ASP VAL ALA ASN ALA VAL LEU ASP
SEQRES 28 D 528 GLY ALA ASP CYS ILE MET LEU SER GLY GLU THR ALA LYS
SEQRES 29 D 528 GLY ASN PHE PRO VAL GLU ALA VAL LYS MET GLN HIS ALA
SEQRES 30 D 528 ILE ALA ARG GLU ALA GLU ALA ALA VAL TYR HIS ARG GLN
SEQRES 31 D 528 LEU PHE GLU GLU LEU ARG ARG ALA ALA PRO LEU SER ARG
SEQRES 32 D 528 ASP PRO THR GLU VAL THR ALA ILE GLY ALA VAL GLU ALA
SEQRES 33 D 528 ALA PHE LYS CYS CYS ALA ALA ALA ILE ILE VAL LEU THR
SEQRES 34 D 528 THR THR GLY ARG SER ALA GLN LEU LEU SER ARG TYR ARG
SEQRES 35 D 528 PRO ARG ALA ALA VAL ILE ALA VAL THR ARG SER ALA GLN
SEQRES 36 D 528 ALA ALA ARG GLN VAL HIS LEU CYS ARG GLY VAL PHE PRO
SEQRES 37 D 528 LEU LEU TYR ARG GLU PRO PRO GLU ALA ILE TRP ALA ASP
SEQRES 38 D 528 ASP VAL ASP ARG ARG VAL GLN PHE GLY ILE GLU SER GLY
SEQRES 39 D 528 LYS LEU ARG GLY PHE LEU ARG VAL GLY ASP LEU VAL ILE
SEQRES 40 D 528 VAL VAL THR GLY TRP ARG PRO GLY SER GLY TYR THR ASN
SEQRES 41 D 528 ILE MET ARG VAL LEU SER ILE SER
HET FBP A 580 20
HET PGA A 581 9
HET K A 582 1
HET MN A 583 1
HET FBP B 580 20
HET PGA B 581 9
HET K B 586 1
HET MN B 587 1
HET FBP C 580 20
HET PGA C 581 9
HET K C 590 1
HET MN C 591 1
HET FBP D 580 20
HET PGA D 581 9
HET K D 594 1
HET MN D 595 1
HETNAM FBP 1,6-DI-O-PHOSPHONO-BETA-D-FRUCTOFURANOSE
HETNAM PGA 2-PHOSPHOGLYCOLIC ACID
HETNAM K POTASSIUM ION
HETNAM MN MANGANESE (II) ION
HETSYN FBP BETA-FRUCTOSE-1,6-DIPHOSPHATE; FRUCTOSE-1,6-
HETSYN 2 FBP BISPHOSPHATE; 1,6-DI-O-PHOSPHONO-BETA-D-FRUCTOSE; 1,6-
HETSYN 3 FBP DI-O-PHOSPHONO-D-FRUCTOSE; 1,6-DI-O-PHOSPHONO-FRUCTOSE
FORMUL 5 FBP 4(C6 H14 O12 P2)
FORMUL 6 PGA 4(C2 H5 O6 P)
FORMUL 7 K 4(K 1+)
FORMUL 8 MN 4(MN 2+)
FORMUL 21 HOH *65(H2 O)
HELIX 1 1 GLN A 60 MET A 65 1 6
HELIX 2 2 THR A 68 CYS A 74 1 7
HELIX 3 3 GLY A 95 ARG A 99 5 5
HELIX 4 4 SER A 100 GLY A 111 1 12
HELIX 5 5 SER A 123 SER A 140 1 18
HELIX 6 6 ASP A 188 THR A 193 5 6
HELIX 7 7 ASN A 206 VAL A 211 1 6
HELIX 8 8 SER A 265 HIS A 278 1 14
HELIX 9 9 LYS A 290 GLY A 302 1 13
HELIX 10 10 PRO A 303 HIS A 306 5 4
HELIX 11 11 ASN A 316 ARG A 322 1 7
HELIX 12 12 ARG A 322 SER A 330 1 9
HELIX 13 13 ARG A 337 ILE A 344 1 8
HELIX 14 14 PRO A 345 GLU A 347 5 3
HELIX 15 15 LYS A 348 GLY A 364 1 17
HELIX 16 16 LEU A 374 THR A 379 5 6
HELIX 17 17 THR A 384 GLY A 398 1 15
HELIX 18 18 SER A 405 LYS A 410 1 6
HELIX 19 19 PHE A 413 VAL A 432 1 20
HELIX 20 20 TYR A 433 ALA A 445 1 13
HELIX 21 21 ASP A 450 CYS A 466 1 17
HELIX 22 22 GLY A 478 ARG A 486 1 9
HELIX 23 23 SER A 499 VAL A 506 1 8
HELIX 24 24 HIS A 507 CYS A 509 5 3
HELIX 25 25 ILE A 524 ARG A 543 1 20
HELIX 26 26 GLN B 60 MET B 65 1 6
HELIX 27 27 THR B 68 CYS B 74 1 7
HELIX 28 28 GLY B 95 ARG B 99 5 5
HELIX 29 29 SER B 100 GLY B 111 1 12
HELIX 30 30 SER B 123 SER B 140 1 18
HELIX 31 31 ASN B 206 VAL B 211 1 6
HELIX 32 32 SER B 265 HIS B 278 1 14
HELIX 33 33 LYS B 290 GLY B 302 1 13
HELIX 34 34 PRO B 303 HIS B 306 5 4
HELIX 35 35 ASN B 316 ARG B 322 1 7
HELIX 36 36 ARG B 322 SER B 330 1 9
HELIX 37 37 ARG B 337 ILE B 344 1 8
HELIX 38 38 PRO B 345 GLU B 347 5 3
HELIX 39 39 LYS B 348 GLY B 364 1 17
HELIX 40 40 LEU B 374 THR B 379 5 6
HELIX 41 41 THR B 384 GLY B 398 1 15
HELIX 42 42 SER B 405 LYS B 410 1 6
HELIX 43 43 PHE B 413 ALA B 431 1 19
HELIX 44 44 TYR B 433 ALA B 445 1 13
HELIX 45 45 ASP B 450 CYS B 466 1 17
HELIX 46 46 GLY B 478 TYR B 487 1 10
HELIX 47 47 SER B 499 VAL B 506 1 8
HELIX 48 48 HIS B 507 CYS B 509 5 3
HELIX 49 49 ILE B 524 ARG B 543 1 20
HELIX 50 50 GLN C 60 MET C 65 1 6
HELIX 51 51 THR C 68 CYS C 74 1 7
HELIX 52 52 GLY C 95 ARG C 99 5 5
HELIX 53 53 SER C 100 GLY C 111 1 12
HELIX 54 54 SER C 123 SER C 140 1 18
HELIX 55 55 ASP C 188 ARG C 192 5 5
HELIX 56 56 ASN C 206 VAL C 211 1 6
HELIX 57 57 SER C 265 HIS C 278 1 14
HELIX 58 58 LYS C 290 GLY C 302 1 13
HELIX 59 59 PRO C 303 HIS C 306 5 4
HELIX 60 60 ASN C 316 ARG C 322 1 7
HELIX 61 61 ARG C 322 SER C 330 1 9
HELIX 62 62 ARG C 337 ILE C 344 1 8
HELIX 63 63 PRO C 345 GLU C 347 5 3
HELIX 64 64 LYS C 348 GLY C 364 1 17
HELIX 65 65 LEU C 374 THR C 379 5 6
HELIX 66 66 THR C 384 GLY C 398 1 15
HELIX 67 67 SER C 405 LYS C 410 1 6
HELIX 68 68 PHE C 413 VAL C 432 1 20
HELIX 69 69 TYR C 433 ALA C 445 1 13
HELIX 70 70 ASP C 450 CYS C 467 1 18
HELIX 71 71 GLY C 478 ARG C 486 1 9
HELIX 72 72 SER C 499 VAL C 506 1 8
HELIX 73 73 HIS C 507 CYS C 509 5 3
HELIX 74 74 ILE C 524 ARG C 543 1 20
HELIX 75 75 GLN D 60 MET D 65 1 6
HELIX 76 76 THR D 68 CYS D 74 1 7
HELIX 77 77 GLY D 95 ARG D 99 5 5
HELIX 78 78 SER D 100 GLY D 111 1 12
HELIX 79 79 SER D 123 SER D 140 1 18
HELIX 80 80 ASP D 188 THR D 193 5 6
HELIX 81 81 ASN D 206 VAL D 211 1 6
HELIX 82 82 SER D 265 HIS D 278 1 14
HELIX 83 83 LYS D 290 GLY D 302 1 13
HELIX 84 84 PRO D 303 HIS D 306 5 4
HELIX 85 85 ASN D 316 ARG D 322 1 7
HELIX 86 86 ARG D 322 SER D 330 1 9
HELIX 87 87 ARG D 337 ILE D 344 1 8
HELIX 88 88 LYS D 348 GLY D 364 1 17
HELIX 89 89 LEU D 374 THR D 379 5 6
HELIX 90 90 THR D 384 GLY D 398 1 15
HELIX 91 91 SER D 405 LYS D 410 1 6
HELIX 92 92 PHE D 413 ALA D 431 1 19
HELIX 93 93 TYR D 433 ALA D 445 1 13
HELIX 94 94 ASP D 450 CYS D 466 1 17
HELIX 95 95 GLY D 478 ARG D 486 1 9
HELIX 96 96 SER D 499 VAL D 506 1 8
HELIX 97 97 HIS D 507 CYS D 509 5 3
HELIX 98 98 ILE D 524 ARG D 543 1 20
SHEET 1 AA10 SER A 89 THR A 93 0
SHEET 2 AA10 CYS A 401 LEU A 404 1 O ILE A 402 N ILE A 91
SHEET 3 AA10 VAL A 367 ALA A 370 1 O CYS A 369 N MET A 403
SHEET 4 AA10 GLY A 332 ALA A 336 1 O ILE A 333 N VAL A 368
SHEET 5 AA10 LYS A 309 ILE A 314 1 O SER A 312 N MET A 334
SHEET 6 AA10 ILE A 282 ALA A 285 1 O VAL A 283 N ILE A 311
SHEET 7 AA10 ALA A 152 ASP A 156 1 O LEU A 155 N PHE A 284
SHEET 8 AA10 MET A 112 ASN A 118 1 O ASN A 113 N ALA A 152
SHEET 9 AA10 SER A 89 THR A 93 1 O ILE A 90 N ASN A 113
SHEET 10 AA10 SER A 89 THR A 93 0
SHEET 1 AB 2 VAL A 175 LEU A 177 0
SHEET 2 AB 2 GLY A 244 LEU A 246 -1 O GLY A 244 N LEU A 177
SHEET 1 AC 6 THR A 199 TRP A 201 0
SHEET 2 AC 6 GLN A 182 THR A 186 1 O LEU A 184 N VAL A 200
SHEET 3 AC 6 GLY A 235 ASN A 242 -1 O LEU A 236 N VAL A 185
SHEET 4 AC 6 ILE A 224 ILE A 231 -1 O SER A 225 N GLU A 241
SHEET 5 AC 6 ARG A 216 ILE A 219 -1 O ILE A 217 N LEU A 226
SHEET 6 AC 6 VAL A 252 ASN A 253 -1 O ASN A 253 N TYR A 218
SHEET 1 AD10 VAL A 512 LEU A 516 0
SHEET 2 AD10 ALA A 492 THR A 497 1 O VAL A 493 N PHE A 513
SHEET 3 AD10 ALA A 470 LEU A 474 1 O ILE A 471 N ILE A 494
SHEET 4 AD10 LEU A 551 GLY A 557 1 O ILE A 553 N ILE A 472
SHEET 5 AD10 THR A 565 SER A 572 -1 N ASN A 566 O THR A 556
SHEET 6 AD10 THR B 565 SER B 572 -1 O ASN B 566 N VAL A 570
SHEET 7 AD10 LEU B 551 GLY B 557 -1 O VAL B 552 N LEU B 571
SHEET 8 AD10 ALA B 470 LEU B 474 1 O ALA B 470 N ILE B 553
SHEET 9 AD10 ALA B 492 THR B 497 1 O ALA B 492 N ILE B 471
SHEET 10 AD10 VAL B 512 LEU B 516 1 O PHE B 513 N ALA B 495
SHEET 1 BA 9 SER B 89 THR B 93 0
SHEET 2 BA 9 CYS B 401 LEU B 404 1 O ILE B 402 N ILE B 91
SHEET 3 BA 9 VAL B 367 ALA B 370 1 O CYS B 369 N MET B 403
SHEET 4 BA 9 GLY B 332 ALA B 336 1 O ILE B 333 N VAL B 368
SHEET 5 BA 9 LYS B 309 ILE B 314 1 O SER B 312 N MET B 334
SHEET 6 BA 9 ILE B 282 ALA B 285 1 O VAL B 283 N ILE B 311
SHEET 7 BA 9 ALA B 152 ASP B 156 1 O LEU B 155 N PHE B 284
SHEET 8 BA 9 MET B 112 ASN B 118 1 O ASN B 113 N ALA B 152
SHEET 9 BA 9 SER B 89 THR B 93 1 O ILE B 90 N ASN B 113
SHEET 1 BB 2 GLU B 176 LEU B 177 0
SHEET 2 BB 2 GLY B 244 VAL B 245 -1 O GLY B 244 N LEU B 177
SHEET 1 BC 6 THR B 199 TRP B 201 0
SHEET 2 BC 6 GLN B 182 THR B 186 1 O LEU B 184 N VAL B 200
SHEET 3 BC 6 THR B 238 ASN B 242 -1 O THR B 238 N VAL B 183
SHEET 4 BC 6 ILE B 224 VAL B 227 -1 O SER B 225 N GLU B 241
SHEET 5 BC 6 ARG B 216 ILE B 219 -1 O ILE B 217 N LEU B 226
SHEET 6 BC 6 VAL B 252 ASN B 253 -1 O ASN B 253 N TYR B 218
SHEET 1 CA 9 SER C 89 THR C 93 0
SHEET 2 CA 9 CYS C 401 LEU C 404 1 O ILE C 402 N ILE C 91
SHEET 3 CA 9 VAL C 367 ALA C 370 1 O CYS C 369 N MET C 403
SHEET 4 CA 9 GLY C 332 ALA C 336 1 O ILE C 333 N VAL C 368
SHEET 5 CA 9 LYS C 309 ILE C 314 1 O SER C 312 N MET C 334
SHEET 6 CA 9 ILE C 282 ALA C 285 1 O VAL C 283 N ILE C 311
SHEET 7 CA 9 ALA C 152 ASP C 156 1 O LEU C 155 N PHE C 284
SHEET 8 CA 9 MET C 112 ASN C 118 1 O ASN C 113 N ALA C 152
SHEET 9 CA 9 SER C 89 THR C 93 1 O ILE C 90 N ASN C 113
SHEET 1 CB 2 VAL C 175 LEU C 177 0
SHEET 2 CB 2 GLY C 244 LEU C 246 -1 O GLY C 244 N LEU C 177
SHEET 1 CC 6 THR C 199 TRP C 201 0
SHEET 2 CC 6 GLN C 182 THR C 186 1 O LEU C 184 N VAL C 200
SHEET 3 CC 6 GLY C 235 ASN C 242 -1 O LEU C 236 N VAL C 185
SHEET 4 CC 6 ILE C 224 GLY C 232 -1 O SER C 225 N GLU C 241
SHEET 5 CC 6 ARG C 216 ILE C 219 -1 O ILE C 217 N LEU C 226
SHEET 6 CC 6 VAL C 252 ASN C 253 -1 O ASN C 253 N TYR C 218
SHEET 1 CD10 VAL C 512 LEU C 516 0
SHEET 2 CD10 ALA C 492 THR C 497 1 O VAL C 493 N PHE C 513
SHEET 3 CD10 ALA C 470 LEU C 474 1 O ILE C 471 N ILE C 494
SHEET 4 CD10 LEU C 551 GLY C 557 1 O ILE C 553 N ILE C 472
SHEET 5 CD10 THR C 565 SER C 572 -1 N ASN C 566 O THR C 556
SHEET 6 CD10 THR D 565 SER D 572 -1 O ASN D 566 N VAL C 570
SHEET 7 CD10 LEU D 551 GLY D 557 -1 O VAL D 552 N LEU D 571
SHEET 8 CD10 ALA D 470 LEU D 474 1 O ALA D 470 N ILE D 553
SHEET 9 CD10 ALA D 492 THR D 497 1 O ALA D 492 N ILE D 471
SHEET 10 CD10 VAL D 512 LEU D 516 1 O PHE D 513 N ALA D 495
SHEET 1 DA17 SER D 89 THR D 93 0
SHEET 2 DA17 CYS D 401 LEU D 404 1 O ILE D 402 N ILE D 91
SHEET 3 DA17 VAL D 367 ALA D 370 1 O CYS D 369 N MET D 403
SHEET 4 DA17 MET D 112 ASN D 118 0
SHEET 5 DA17 SER D 89 THR D 93 1 O ILE D 90 N ASN D 113
SHEET 6 DA17 ALA D 152 ASP D 156 0
SHEET 7 DA17 MET D 112 ASN D 118 1 O ASN D 113 N ALA D 152
SHEET 8 DA17 ILE D 282 ALA D 285 0
SHEET 9 DA17 ALA D 152 ASP D 156 1 O LEU D 155 N PHE D 284
SHEET 10 DA17 LYS D 309 ILE D 314 0
SHEET 11 DA17 ILE D 282 ALA D 285 1 O VAL D 283 N ILE D 311
SHEET 12 DA17 GLY D 332 ALA D 336 0
SHEET 13 DA17 LYS D 309 ILE D 314 1 O SER D 312 N MET D 334
SHEET 14 DA17 VAL D 367 ALA D 370 0
SHEET 15 DA17 GLY D 332 ALA D 336 1 O ILE D 333 N VAL D 368
SHEET 16 DA17 CYS D 401 LEU D 404 0
SHEET 17 DA17 SER D 89 THR D 93 1 O SER D 89 N ILE D 402
SHEET 1 DB 2 VAL D 175 LEU D 177 0
SHEET 2 DB 2 GLY D 244 LEU D 246 -1 O GLY D 244 N LEU D 177
SHEET 1 DC 6 THR D 199 TRP D 201 0
SHEET 2 DC 6 GLN D 182 THR D 186 1 O LEU D 184 N VAL D 200
SHEET 3 DC 6 GLY D 235 ASN D 242 -1 O LEU D 236 N VAL D 185
SHEET 4 DC 6 ILE D 224 GLY D 232 -1 O SER D 225 N GLU D 241
SHEET 5 DC 6 ARG D 216 ILE D 219 -1 O ILE D 217 N LEU D 226
SHEET 6 DC 6 VAL D 252 ASN D 253 -1 O ASN D 253 N TYR D 218
LINK OD1 ASN A 118 K K A 582 1555 1555 3.15
LINK OG SER A 120 K K A 582 1555 1555 3.44
LINK OD1 ASP A 156 K K A 582 1555 1555 2.95
LINK O THR A 157 K K A 582 1555 1555 3.03
LINK OE2 GLU A 315 MN MN A 583 1555 1555 1.61
LINK OD2 ASP A 339 MN MN A 583 1555 1555 1.87
LINK O2P PGA A 581 K K A 582 1555 1555 3.14
LINK O1P PGA A 581 MN MN A 583 1555 1555 2.09
LINK O1 PGA A 581 MN MN A 583 1555 1555 2.27
LINK O4P PGA A 581 MN MN A 583 1555 1555 2.37
LINK OD1 ASN B 118 K K B 586 1555 1555 3.21
LINK OD1 ASP B 156 K K B 586 1555 1555 2.62
LINK O THR B 157 K K B 586 1555 1555 2.87
LINK OE2 GLU B 315 MN MN B 587 1555 1555 1.75
LINK OD2 ASP B 339 MN MN B 587 1555 1555 1.79
LINK O2P PGA B 581 K K B 586 1555 1555 2.92
LINK O1 PGA B 581 MN MN B 587 1555 1555 2.07
LINK O4P PGA B 581 MN MN B 587 1555 1555 2.50
LINK O1P PGA B 581 MN MN B 587 1555 1555 2.19
LINK OD1 ASN C 118 K K C 590 1555 1555 2.90
LINK OD1 ASP C 156 K K C 590 1555 1555 2.67
LINK O THR C 157 K K C 590 1555 1555 2.90
LINK OE2 GLU C 315 MN MN C 591 1555 1555 1.57
LINK OD2 ASP C 339 MN MN C 591 1555 1555 1.72
LINK O2P PGA C 581 K K C 590 1555 1555 2.97
LINK O1 PGA C 581 MN MN C 591 1555 1555 2.15
LINK O4P PGA C 581 MN MN C 591 1555 1555 2.26
LINK O1P PGA C 581 MN MN C 591 1555 1555 2.32
LINK OD1 ASN D 118 K K D 594 1555 1555 2.97
LINK OD1 ASP D 156 K K D 594 1555 1555 2.63
LINK O THR D 157 K K D 594 1555 1555 3.04
LINK OE2 GLU D 315 MN MN D 595 1555 1555 1.52
LINK OD2 ASP D 339 MN MN D 595 1555 1555 1.83
LINK O2P PGA D 581 K K D 594 1555 1555 2.89
LINK O1 PGA D 581 MN MN D 595 1555 1555 1.97
LINK O1P PGA D 581 MN MN D 595 1555 1555 2.38
CRYST1 74.413 172.058 85.512 90.00 92.46 90.00 P 1 21 1 8
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 0.013439 0.000000 0.000577 0.00000
SCALE2 0.000000 0.005812 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011705 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
