HEADER TRANSFERASE 31-JUL-09 3II0
TITLE CRYSTAL STRUCTURE OF HUMAN GLUTAMATE OXALOACETATE TRANSAMINASE 1
TITLE 2 (GOT1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTATE AMINOTRANSFERASE, CYTOPLASMIC;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 14-412;
COMPND 5 SYNONYM: TRANSAMINASE A, GLUTAMATE OXALOACETATE TRANSAMINASE 1;
COMPND 6 EC: 2.6.1.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GOT1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PNIC-CTHF
KEYWDS GLUTAMATE OXALOACETATE TRANSAMINASE 1, ASPARTATE AMINOTRANSFERASE 1,
KEYWDS 2 PYRIDOXAL PHOSPHATE-DEPENDENT ENZYME, AMINO ACID METABOLISM, UREA
KEYWDS 3 AND TRICARBOXYLIC ACID CYCLES, STRUCTURAL GENOMICS, STRUCTURAL
KEYWDS 4 GENOMICS CONSORTIUM, SGC, AMINOTRANSFERASE, PHOSPHOPROTEIN,
KEYWDS 5 PYRIDOXAL PHOSPHATE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.UGOCHUKWU,E.PILKA,C.COOPER,J.E.BRAY,W.W.YUE,J.MUNIZ,A.CHAIKUAD,
AUTHOR 2 F.VON DELFT,C.BOUNTRA,C.H.ARROWSMITH,J.WEIGELT,A.EDWARDS,
AUTHOR 3 K.L.KAVANAGH,U.OPPERMANN,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 4 06-SEP-23 3II0 1 REMARK SEQADV
REVDAT 3 01-NOV-17 3II0 1 REMARK
REVDAT 2 13-JUL-11 3II0 1 VERSN
REVDAT 1 11-AUG-09 3II0 0
JRNL AUTH E.UGOCHUKWU,E.PILKA,C.COOPER,J.E.BRAY,W.W.YUE,J.MUNIZ,
JRNL AUTH 2 A.CHAIKUAD,K.L.KAVANAGH,U.OPPERMANN
JRNL TITL CRYSTAL STRUCTURE OF HUMAN GLUTAMATE OXALOACETATE
JRNL TITL 2 TRANSAMINASE 1 (GOT1)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0089
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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.04
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 121312
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6417
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) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8782
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.32
REMARK 3 BIN R VALUE (WORKING SET) : 0.2870
REMARK 3 BIN FREE R VALUE SET COUNT : 483
REMARK 3 BIN FREE R VALUE : 0.3290
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12745
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 156
REMARK 3 SOLVENT ATOMS : 733
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) : 16.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.62000
REMARK 3 B22 (A**2) : -1.70000
REMARK 3 B33 (A**2) : 0.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED 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): 0.114
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.293
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13312 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 8977 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18105 ; 1.444 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): 21769 ; 0.937 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1648 ; 5.624 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 623 ;35.614 ;23.756
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2088 ;13.419 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 87 ;18.796 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1965 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14943 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2820 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 8133 ; 0.932 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3293 ; 0.330 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13119 ; 1.607 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5179 ; 2.789 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4973 ; 4.002 ; 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 : 4
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 14 A 213 5
REMARK 3 1 B 14 B 213 5
REMARK 3 2 A 215 A 410 5
REMARK 3 2 B 215 B 410 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 2321 ; 0.060 ; 0.500
REMARK 3 LOOSE POSITIONAL 1 A (A): 2879 ; 0.160 ; 5.000
REMARK 3 MEDIUM THERMAL 1 A (A**2): 2321 ; 0.570 ; 2.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 2879 ; 0.690 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 14 C 213 5
REMARK 3 1 D 14 D 213 5
REMARK 3 2 C 215 C 410 5
REMARK 3 2 D 215 D 410 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 2323 ; 0.080 ; 0.500
REMARK 3 LOOSE POSITIONAL 2 A (A): 2899 ; 0.160 ; 5.000
REMARK 3 MEDIUM THERMAL 2 A (A**2): 2323 ; 0.590 ; 2.000
REMARK 3 LOOSE THERMAL 2 A (A**2): 2899 ; 0.690 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 411 A 417 6
REMARK 3 1 B 411 B 417 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 3 A (A): 84 ; 0.570 ; 5.000
REMARK 3 LOOSE THERMAL 3 A (A**2): 84 ; 3.230 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 411 C 417 6
REMARK 3 1 D 411 D 417 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 4 A (A): 81 ; 0.220 ; 5.000
REMARK 3 LOOSE THERMAL 4 A (A**2): 81 ; 1.690 ;10.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
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 409
REMARK 3 ORIGIN FOR THE GROUP (A): 37.2199 -6.0572 -30.2947
REMARK 3 T TENSOR
REMARK 3 T11: 0.1004 T22: 0.0507
REMARK 3 T33: 0.0153 T12: 0.0622
REMARK 3 T13: -0.0043 T23: 0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 0.8685 L22: 1.2868
REMARK 3 L33: 0.2902 L12: -0.3872
REMARK 3 L13: -0.2702 L23: 0.1982
REMARK 3 S TENSOR
REMARK 3 S11: -0.0418 S12: -0.0398 S13: 0.0109
REMARK 3 S21: 0.2009 S22: 0.0373 S23: -0.1169
REMARK 3 S31: 0.0369 S32: 0.0374 S33: 0.0045
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 410 A 418
REMARK 3 ORIGIN FOR THE GROUP (A): 53.9761 -14.0687 -60.7858
REMARK 3 T TENSOR
REMARK 3 T11: 0.1984 T22: 0.2037
REMARK 3 T33: 0.0646 T12: -0.0137
REMARK 3 T13: 0.0905 T23: -0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 2.5121 L22: 6.6180
REMARK 3 L33: 10.0031 L12: 2.3339
REMARK 3 L13: -3.8771 L23: -7.8300
REMARK 3 S TENSOR
REMARK 3 S11: -0.1556 S12: -0.5391 S13: -0.0856
REMARK 3 S21: 0.0471 S22: 0.0203 S23: -0.0939
REMARK 3 S31: 0.0395 S32: 0.3439 S33: 0.1353
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 : B 15 B 409
REMARK 3 ORIGIN FOR THE GROUP (A): 3.0813 -48.9168 -30.7671
REMARK 3 T TENSOR
REMARK 3 T11: 0.0594 T22: 0.0421
REMARK 3 T33: 0.0313 T12: 0.0453
REMARK 3 T13: 0.0179 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 1.0646 L22: 1.1033
REMARK 3 L33: 0.4445 L12: -0.3260
REMARK 3 L13: 0.2981 L23: -0.1709
REMARK 3 S TENSOR
REMARK 3 S11: -0.0763 S12: -0.0642 S13: 0.0011
REMARK 3 S21: 0.1488 S22: 0.0425 S23: 0.1575
REMARK 3 S31: -0.0792 S32: -0.0725 S33: 0.0338
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 410 B 418
REMARK 3 ORIGIN FOR THE GROUP (A): -14.4420 -41.9148 -62.0321
REMARK 3 T TENSOR
REMARK 3 T11: 0.1600 T22: 0.1831
REMARK 3 T33: 0.1609 T12: 0.0256
REMARK 3 T13: -0.0143 T23: 0.0182
REMARK 3 L TENSOR
REMARK 3 L11: 1.3309 L22: 4.8137
REMARK 3 L33: 9.6771 L12: 2.3989
REMARK 3 L13: 3.5065 L23: 6.7798
REMARK 3 S TENSOR
REMARK 3 S11: -0.0127 S12: -0.0730 S13: 0.0094
REMARK 3 S21: 0.2436 S22: -0.0747 S23: 0.1207
REMARK 3 S31: 0.2367 S32: -0.1084 S33: 0.0874
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 : C 13 C 17
REMARK 3 ORIGIN FOR THE GROUP (A): 27.0279 -71.3159 -23.6763
REMARK 3 T TENSOR
REMARK 3 T11: 0.1288 T22: 0.1342
REMARK 3 T33: 0.1548 T12: 0.0583
REMARK 3 T13: 0.0387 T23: 0.0436
REMARK 3 L TENSOR
REMARK 3 L11: 4.4382 L22: 7.9112
REMARK 3 L33: 9.6362 L12: 2.6880
REMARK 3 L13: 6.5231 L23: 3.5286
REMARK 3 S TENSOR
REMARK 3 S11: 0.1034 S12: -0.0470 S13: -0.1932
REMARK 3 S21: -0.0725 S22: 0.1303 S23: -0.0479
REMARK 3 S31: 0.1853 S32: -0.0523 S33: -0.2336
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 18 C 274
REMARK 3 ORIGIN FOR THE GROUP (A): 34.1005 -62.1761 -38.0092
REMARK 3 T TENSOR
REMARK 3 T11: 0.0185 T22: 0.0456
REMARK 3 T33: 0.0737 T12: 0.0157
REMARK 3 T13: 0.0146 T23: 0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 0.7324 L22: 1.5090
REMARK 3 L33: 0.6497 L12: -0.1339
REMARK 3 L13: -0.0074 L23: 0.3634
REMARK 3 S TENSOR
REMARK 3 S11: -0.0094 S12: -0.0054 S13: 0.0639
REMARK 3 S21: -0.0444 S22: 0.0132 S23: -0.3017
REMARK 3 S31: -0.0204 S32: 0.1242 S33: -0.0038
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 : C 275 C 409
REMARK 3 ORIGIN FOR THE GROUP (A): 40.3174 -61.9064 -26.5362
REMARK 3 T TENSOR
REMARK 3 T11: 0.0539 T22: 0.0989
REMARK 3 T33: 0.1442 T12: 0.0355
REMARK 3 T13: -0.0553 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 1.1706 L22: 1.3924
REMARK 3 L33: 0.7431 L12: -0.0303
REMARK 3 L13: 0.2219 L23: -0.0708
REMARK 3 S TENSOR
REMARK 3 S11: 0.0295 S12: -0.0819 S13: 0.0386
REMARK 3 S21: 0.1556 S22: -0.0392 S23: -0.4451
REMARK 3 S31: 0.0535 S32: 0.2120 S33: 0.0097
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 : C 410 C 418
REMARK 3 ORIGIN FOR THE GROUP (A): 42.4318 -87.7292 -16.6056
REMARK 3 T TENSOR
REMARK 3 T11: 0.3883 T22: 0.3289
REMARK 3 T33: 0.2557 T12: -0.0074
REMARK 3 T13: -0.0844 T23: 0.0326
REMARK 3 L TENSOR
REMARK 3 L11: 3.7500 L22: 5.4933
REMARK 3 L33: 10.5400 L12: 4.5195
REMARK 3 L13: 6.2803 L23: 7.5808
REMARK 3 S TENSOR
REMARK 3 S11: -0.2219 S12: -0.0020 S13: 0.1911
REMARK 3 S21: -0.1203 S22: -0.0542 S23: 0.1922
REMARK 3 S31: -0.2927 S32: 0.0606 S33: 0.2761
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 : D 13 D 19
REMARK 3 ORIGIN FOR THE GROUP (A): 13.4112 14.9692 -21.3539
REMARK 3 T TENSOR
REMARK 3 T11: 0.1742 T22: 0.0899
REMARK 3 T33: 0.3518 T12: 0.0063
REMARK 3 T13: -0.0667 T23: -0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 1.7388 L22: 6.5563
REMARK 3 L33: 9.1446 L12: 0.3695
REMARK 3 L13: -3.2646 L23: -4.9488
REMARK 3 S TENSOR
REMARK 3 S11: 0.0005 S12: -0.1500 S13: 0.1652
REMARK 3 S21: 0.1247 S22: 0.0567 S23: 0.0689
REMARK 3 S31: -0.1500 S32: 0.2258 S33: -0.0572
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 : D 20 D 274
REMARK 3 ORIGIN FOR THE GROUP (A): 5.5842 6.6543 -36.5784
REMARK 3 T TENSOR
REMARK 3 T11: 0.0604 T22: 0.0469
REMARK 3 T33: 0.0894 T12: 0.0208
REMARK 3 T13: 0.0192 T23: -0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 0.9188 L22: 1.3225
REMARK 3 L33: 0.6538 L12: -0.1715
REMARK 3 L13: -0.1888 L23: -0.3030
REMARK 3 S TENSOR
REMARK 3 S11: 0.0074 S12: 0.0740 S13: -0.0859
REMARK 3 S21: -0.0162 S22: -0.0322 S23: 0.3068
REMARK 3 S31: 0.0772 S32: -0.1069 S33: 0.0248
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 : D 275 D 411
REMARK 3 ORIGIN FOR THE GROUP (A): -0.0830 7.3888 -24.3127
REMARK 3 T TENSOR
REMARK 3 T11: 0.1229 T22: 0.0662
REMARK 3 T33: 0.1291 T12: 0.0371
REMARK 3 T13: 0.0924 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 1.4541 L22: 1.3395
REMARK 3 L33: 0.7446 L12: -0.1139
REMARK 3 L13: -0.4228 L23: -0.0008
REMARK 3 S TENSOR
REMARK 3 S11: 0.0353 S12: -0.0552 S13: -0.0580
REMARK 3 S21: 0.2196 S22: -0.0428 S23: 0.4001
REMARK 3 S31: -0.0413 S32: -0.1477 S33: 0.0076
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 : D 412 D 418
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3394 35.3822 -19.0069
REMARK 3 T TENSOR
REMARK 3 T11: 0.4735 T22: 0.3211
REMARK 3 T33: 0.4081 T12: 0.0219
REMARK 3 T13: 0.0490 T23: 0.1770
REMARK 3 L TENSOR
REMARK 3 L11: 5.7992 L22: 1.3970
REMARK 3 L33: 8.9942 L12: -1.1086
REMARK 3 L13: -0.2042 L23: 3.2941
REMARK 3 S TENSOR
REMARK 3 S11: 0.0420 S12: -0.7645 S13: -1.1689
REMARK 3 S21: 0.4541 S22: -0.1630 S23: 0.2521
REMARK 3 S31: 1.1509 S32: -0.9008 S33: 0.1211
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 3II0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-09.
REMARK 100 THE DEPOSITION ID IS D_1000054435.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97630
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 127732
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 56.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.10800
REMARK 200 R SYM (I) : 0.10800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.78000
REMARK 200 R SYM FOR SHELL (I) : 0.78000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
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 1AJS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.25M NA_K_TARTRATE; 15W/V PEG_3350,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K, PH 0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 39.26550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 119.99850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.67350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 119.99850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.26550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.67350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 13
REMARK 465 GLN A 14
REMARK 465 SER A 420
REMARK 465 HIS A 421
REMARK 465 HIS A 422
REMARK 465 HIS A 423
REMARK 465 HIS A 424
REMARK 465 HIS A 425
REMARK 465 HIS A 426
REMARK 465 ASP A 427
REMARK 465 TYR A 428
REMARK 465 LYS A 429
REMARK 465 ASP A 430
REMARK 465 ASP A 431
REMARK 465 ASP A 432
REMARK 465 ASP A 433
REMARK 465 LYS A 434
REMARK 465 MET B 13
REMARK 465 GLN B 14
REMARK 465 SER B 420
REMARK 465 HIS B 421
REMARK 465 HIS B 422
REMARK 465 HIS B 423
REMARK 465 HIS B 424
REMARK 465 HIS B 425
REMARK 465 HIS B 426
REMARK 465 ASP B 427
REMARK 465 TYR B 428
REMARK 465 LYS B 429
REMARK 465 ASP B 430
REMARK 465 ASP B 431
REMARK 465 ASP B 432
REMARK 465 ASP B 433
REMARK 465 LYS B 434
REMARK 465 SER C 420
REMARK 465 HIS C 421
REMARK 465 HIS C 422
REMARK 465 HIS C 423
REMARK 465 HIS C 424
REMARK 465 HIS C 425
REMARK 465 HIS C 426
REMARK 465 ASP C 427
REMARK 465 TYR C 428
REMARK 465 LYS C 429
REMARK 465 ASP C 430
REMARK 465 ASP C 431
REMARK 465 ASP C 432
REMARK 465 ASP C 433
REMARK 465 LYS C 434
REMARK 465 SER D 420
REMARK 465 HIS D 421
REMARK 465 HIS D 422
REMARK 465 HIS D 423
REMARK 465 HIS D 424
REMARK 465 HIS D 425
REMARK 465 HIS D 426
REMARK 465 ASP D 427
REMARK 465 TYR D 428
REMARK 465 LYS D 429
REMARK 465 ASP D 430
REMARK 465 ASP D 431
REMARK 465 ASP D 432
REMARK 465 ASP D 433
REMARK 465 LYS D 434
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 ARG A 26 CZ NH1 NH2
REMARK 470 GLU A 27 CD OE1 OE2
REMARK 470 LYS A 99 CD CE NZ
REMARK 470 GLU A 165 CG CD OE1 OE2
REMARK 470 LYS A 166 CE NZ
REMARK 470 LYS A 214 CD CE NZ
REMARK 470 GLU A 277 CD OE1 OE2
REMARK 470 GLU A 279 CG CD OE1 OE2
REMARK 470 LYS A 290 CD CE NZ
REMARK 470 GLU A 315 CD OE1 OE2
REMARK 470 LYS A 369 CG CD CE NZ
REMARK 470 LYS A 396 CE NZ
REMARK 470 GLN A 419 CG CD OE1 NE2
REMARK 470 ARG B 26 CZ NH1 NH2
REMARK 470 GLU B 27 CD OE1 OE2
REMARK 470 GLU B 165 CG CD OE1 OE2
REMARK 470 LYS B 166 CG CD CE NZ
REMARK 470 GLU B 179 CD OE1 OE2
REMARK 470 LYS B 214 CD CE NZ
REMARK 470 PHE B 217 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 277 CD OE1 OE2
REMARK 470 GLU B 279 CG CD OE1 OE2
REMARK 470 GLN B 283 CD OE1 NE2
REMARK 470 LYS B 290 CD CE NZ
REMARK 470 LYS B 369 CE NZ
REMARK 470 LYS B 396 CE NZ
REMARK 470 GLU B 414 CG CD OE1 OE2
REMARK 470 GLN B 419 CG CD OE1 NE2
REMARK 470 ARG C 26 CZ NH1 NH2
REMARK 470 GLU C 27 CD OE1 OE2
REMARK 470 LYS C 55 CE NZ
REMARK 470 LYS C 60 CE NZ
REMARK 470 LYS C 97 CE NZ
REMARK 470 LYS C 166 CE NZ
REMARK 470 LYS C 214 CD CE NZ
REMARK 470 GLU C 277 CD OE1 OE2
REMARK 470 LYS C 290 NZ
REMARK 470 GLU C 315 CD OE1 OE2
REMARK 470 ASN C 352 OD1 ND2
REMARK 470 LYS C 369 CE NZ
REMARK 470 LYS C 396 CE NZ
REMARK 470 GLU C 414 CG CD OE1 OE2
REMARK 470 ASN C 415 CG OD1 ND2
REMARK 470 ARG D 26 CZ NH1 NH2
REMARK 470 GLU D 27 CD OE1 OE2
REMARK 470 LYS D 55 CE NZ
REMARK 470 ASP D 92 OD1 OD2
REMARK 470 LYS D 166 CG CD CE NZ
REMARK 470 ILE D 199 CD1
REMARK 470 LYS D 214 CD CE NZ
REMARK 470 GLU D 277 CD OE1 OE2
REMARK 470 GLU D 315 CD OE1 OE2
REMARK 470 LYS D 369 CE NZ
REMARK 470 GLU D 414 CG CD OE1 OE2
REMARK 470 ASN D 415 CG OD1 ND2
REMARK 470 LEU D 416 CG CD1 CD2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 122 CA CB CG CD NE CZ NH1
REMARK 480 ARG A 122 NH2
REMARK 480 GLU B 79 CA CB CG CD OE1 OE2
REMARK 480 ARG B 122 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU D 79 CA CB CG CD OE1 OE2
REMARK 480 HIS D 215 CA CB CG ND1 CD2 CE1 NE2
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 O HOH A 467 O HOH C 466 1.97
REMARK 500 NZ LYS C 378 O HOH C 635 2.16
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 HIS D 215 N HIS D 215 CA -0.184
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 42 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 122 CB - CA - C ANGL. DEV. = -13.0 DEGREES
REMARK 500 ARG B 122 N - CA - CB ANGL. DEV. = 11.9 DEGREES
REMARK 500 HIS D 215 N - CA - CB ANGL. DEV. = -11.6 DEGREES
REMARK 500 HIS D 215 N - CA - C ANGL. DEV. = 20.7 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 TYR A 161 -68.38 -140.15
REMARK 500 LEU A 263 42.16 -101.51
REMARK 500 SER A 297 -58.48 77.70
REMARK 500 PHE A 418 9.52 83.08
REMARK 500 TYR B 161 -66.98 -146.08
REMARK 500 LEU B 263 39.02 -98.27
REMARK 500 SER B 297 -56.67 79.39
REMARK 500 TYR C 161 -62.60 -152.78
REMARK 500 PHE C 184 0.32 83.14
REMARK 500 ARG C 267 61.18 61.91
REMARK 500 SER C 297 -56.98 72.56
REMARK 500 TYR D 161 -63.82 -149.33
REMARK 500 PHE D 184 -0.50 77.97
REMARK 500 LEU D 263 40.70 -103.82
REMARK 500 THR D 295 -67.64 -107.68
REMARK 500 SER D 297 -58.53 74.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR A 435
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 11
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 436
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR B 435
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 436
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP C 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR C 435
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 12
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 436
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP D 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR D 435
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 9
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AJS RELATED DB: PDB
REMARK 900 REFINEMENT AND COMPARISONS OF THE CRYSTAL STRUCTURES OF PIG
REMARK 900 CYTOSOLIC ASPARTATE AMINOTRANSFERASE AND ITS COMPLEX WITH 2-
REMARK 900 METHYLASPARTATE
DBREF 3II0 A 14 412 UNP P17174 AATC_HUMAN 14 412
DBREF 3II0 B 14 412 UNP P17174 AATC_HUMAN 14 412
DBREF 3II0 C 14 412 UNP P17174 AATC_HUMAN 14 412
DBREF 3II0 D 14 412 UNP P17174 AATC_HUMAN 14 412
SEQADV 3II0 MET A 13 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ALA A 413 UNP P17174 EXPRESSION TAG
SEQADV 3II0 GLU A 414 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASN A 415 UNP P17174 EXPRESSION TAG
SEQADV 3II0 LEU A 416 UNP P17174 EXPRESSION TAG
SEQADV 3II0 TYR A 417 UNP P17174 EXPRESSION TAG
SEQADV 3II0 PHE A 418 UNP P17174 EXPRESSION TAG
SEQADV 3II0 GLN A 419 UNP P17174 EXPRESSION TAG
SEQADV 3II0 SER A 420 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS A 421 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS A 422 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS A 423 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS A 424 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS A 425 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS A 426 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASP A 427 UNP P17174 EXPRESSION TAG
SEQADV 3II0 TYR A 428 UNP P17174 EXPRESSION TAG
SEQADV 3II0 LYS A 429 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASP A 430 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASP A 431 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASP A 432 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASP A 433 UNP P17174 EXPRESSION TAG
SEQADV 3II0 LYS A 434 UNP P17174 EXPRESSION TAG
SEQADV 3II0 MET B 13 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ALA B 413 UNP P17174 EXPRESSION TAG
SEQADV 3II0 GLU B 414 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASN B 415 UNP P17174 EXPRESSION TAG
SEQADV 3II0 LEU B 416 UNP P17174 EXPRESSION TAG
SEQADV 3II0 TYR B 417 UNP P17174 EXPRESSION TAG
SEQADV 3II0 PHE B 418 UNP P17174 EXPRESSION TAG
SEQADV 3II0 GLN B 419 UNP P17174 EXPRESSION TAG
SEQADV 3II0 SER B 420 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS B 421 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS B 422 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS B 423 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS B 424 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS B 425 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS B 426 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASP B 427 UNP P17174 EXPRESSION TAG
SEQADV 3II0 TYR B 428 UNP P17174 EXPRESSION TAG
SEQADV 3II0 LYS B 429 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASP B 430 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASP B 431 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASP B 432 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASP B 433 UNP P17174 EXPRESSION TAG
SEQADV 3II0 LYS B 434 UNP P17174 EXPRESSION TAG
SEQADV 3II0 MET C 13 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ALA C 413 UNP P17174 EXPRESSION TAG
SEQADV 3II0 GLU C 414 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASN C 415 UNP P17174 EXPRESSION TAG
SEQADV 3II0 LEU C 416 UNP P17174 EXPRESSION TAG
SEQADV 3II0 TYR C 417 UNP P17174 EXPRESSION TAG
SEQADV 3II0 PHE C 418 UNP P17174 EXPRESSION TAG
SEQADV 3II0 GLN C 419 UNP P17174 EXPRESSION TAG
SEQADV 3II0 SER C 420 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS C 421 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS C 422 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS C 423 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS C 424 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS C 425 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS C 426 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASP C 427 UNP P17174 EXPRESSION TAG
SEQADV 3II0 TYR C 428 UNP P17174 EXPRESSION TAG
SEQADV 3II0 LYS C 429 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASP C 430 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASP C 431 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASP C 432 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASP C 433 UNP P17174 EXPRESSION TAG
SEQADV 3II0 LYS C 434 UNP P17174 EXPRESSION TAG
SEQADV 3II0 MET D 13 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ALA D 413 UNP P17174 EXPRESSION TAG
SEQADV 3II0 GLU D 414 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASN D 415 UNP P17174 EXPRESSION TAG
SEQADV 3II0 LEU D 416 UNP P17174 EXPRESSION TAG
SEQADV 3II0 TYR D 417 UNP P17174 EXPRESSION TAG
SEQADV 3II0 PHE D 418 UNP P17174 EXPRESSION TAG
SEQADV 3II0 GLN D 419 UNP P17174 EXPRESSION TAG
SEQADV 3II0 SER D 420 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS D 421 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS D 422 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS D 423 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS D 424 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS D 425 UNP P17174 EXPRESSION TAG
SEQADV 3II0 HIS D 426 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASP D 427 UNP P17174 EXPRESSION TAG
SEQADV 3II0 TYR D 428 UNP P17174 EXPRESSION TAG
SEQADV 3II0 LYS D 429 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASP D 430 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASP D 431 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASP D 432 UNP P17174 EXPRESSION TAG
SEQADV 3II0 ASP D 433 UNP P17174 EXPRESSION TAG
SEQADV 3II0 LYS D 434 UNP P17174 EXPRESSION TAG
SEQRES 1 A 422 MET GLN PRO VAL LEU VAL PHE LYS LEU THR ALA ASP PHE
SEQRES 2 A 422 ARG GLU ASP PRO ASP PRO ARG LYS VAL ASN LEU GLY VAL
SEQRES 3 A 422 GLY ALA TYR ARG THR ASP ASP CYS HIS PRO TRP VAL LEU
SEQRES 4 A 422 PRO VAL VAL LYS LYS VAL GLU GLN LYS ILE ALA ASN ASP
SEQRES 5 A 422 ASN SER LEU ASN HIS GLU TYR LEU PRO ILE LEU GLY LEU
SEQRES 6 A 422 ALA GLU PHE ARG SER CYS ALA SER ARG LEU ALA LEU GLY
SEQRES 7 A 422 ASP ASP SER PRO ALA LEU LYS GLU LYS ARG VAL GLY GLY
SEQRES 8 A 422 VAL GLN SER LEU GLY GLY THR GLY ALA LEU ARG ILE GLY
SEQRES 9 A 422 ALA ASP PHE LEU ALA ARG TRP TYR ASN GLY THR ASN ASN
SEQRES 10 A 422 LYS ASN THR PRO VAL TYR VAL SER SER PRO THR TRP GLU
SEQRES 11 A 422 ASN HIS ASN ALA VAL PHE SER ALA ALA GLY PHE LYS ASP
SEQRES 12 A 422 ILE ARG SER TYR ARG TYR TRP ASP ALA GLU LYS ARG GLY
SEQRES 13 A 422 LEU ASP LEU GLN GLY PHE LEU ASN ASP LEU GLU ASN ALA
SEQRES 14 A 422 PRO GLU PHE SER ILE VAL VAL LEU HIS ALA CYS ALA HIS
SEQRES 15 A 422 ASN PRO THR GLY ILE ASP PRO THR PRO GLU GLN TRP LYS
SEQRES 16 A 422 GLN ILE ALA SER VAL MET LYS HIS ARG PHE LEU PHE PRO
SEQRES 17 A 422 PHE PHE ASP SER ALA TYR GLN GLY PHE ALA SER GLY ASN
SEQRES 18 A 422 LEU GLU ARG ASP ALA TRP ALA ILE ARG TYR PHE VAL SER
SEQRES 19 A 422 GLU GLY PHE GLU PHE PHE CYS ALA GLN SER PHE SER LYS
SEQRES 20 A 422 ASN PHE GLY LEU TYR ASN GLU ARG VAL GLY ASN LEU THR
SEQRES 21 A 422 VAL VAL GLY LYS GLU PRO GLU SER ILE LEU GLN VAL LEU
SEQRES 22 A 422 SER GLN MET GLU LYS ILE VAL ARG ILE THR TRP SER ASN
SEQRES 23 A 422 PRO PRO ALA GLN GLY ALA ARG ILE VAL ALA SER THR LEU
SEQRES 24 A 422 SER ASN PRO GLU LEU PHE GLU GLU TRP THR GLY ASN VAL
SEQRES 25 A 422 LYS THR MET ALA ASP ARG ILE LEU THR MET ARG SER GLU
SEQRES 26 A 422 LEU ARG ALA ARG LEU GLU ALA LEU LYS THR PRO GLY THR
SEQRES 27 A 422 TRP ASN HIS ILE THR ASP GLN ILE GLY MET PHE SER PHE
SEQRES 28 A 422 THR GLY LEU ASN PRO LYS GLN VAL GLU TYR LEU VAL ASN
SEQRES 29 A 422 GLU LYS HIS ILE TYR LEU LEU PRO SER GLY ARG ILE ASN
SEQRES 30 A 422 VAL SER GLY LEU THR THR LYS ASN LEU ASP TYR VAL ALA
SEQRES 31 A 422 THR SER ILE HIS GLU ALA VAL THR LYS ILE ALA GLU ASN
SEQRES 32 A 422 LEU TYR PHE GLN SER HIS HIS HIS HIS HIS HIS ASP TYR
SEQRES 33 A 422 LYS ASP ASP ASP ASP LYS
SEQRES 1 B 422 MET GLN PRO VAL LEU VAL PHE LYS LEU THR ALA ASP PHE
SEQRES 2 B 422 ARG GLU ASP PRO ASP PRO ARG LYS VAL ASN LEU GLY VAL
SEQRES 3 B 422 GLY ALA TYR ARG THR ASP ASP CYS HIS PRO TRP VAL LEU
SEQRES 4 B 422 PRO VAL VAL LYS LYS VAL GLU GLN LYS ILE ALA ASN ASP
SEQRES 5 B 422 ASN SER LEU ASN HIS GLU TYR LEU PRO ILE LEU GLY LEU
SEQRES 6 B 422 ALA GLU PHE ARG SER CYS ALA SER ARG LEU ALA LEU GLY
SEQRES 7 B 422 ASP ASP SER PRO ALA LEU LYS GLU LYS ARG VAL GLY GLY
SEQRES 8 B 422 VAL GLN SER LEU GLY GLY THR GLY ALA LEU ARG ILE GLY
SEQRES 9 B 422 ALA ASP PHE LEU ALA ARG TRP TYR ASN GLY THR ASN ASN
SEQRES 10 B 422 LYS ASN THR PRO VAL TYR VAL SER SER PRO THR TRP GLU
SEQRES 11 B 422 ASN HIS ASN ALA VAL PHE SER ALA ALA GLY PHE LYS ASP
SEQRES 12 B 422 ILE ARG SER TYR ARG TYR TRP ASP ALA GLU LYS ARG GLY
SEQRES 13 B 422 LEU ASP LEU GLN GLY PHE LEU ASN ASP LEU GLU ASN ALA
SEQRES 14 B 422 PRO GLU PHE SER ILE VAL VAL LEU HIS ALA CYS ALA HIS
SEQRES 15 B 422 ASN PRO THR GLY ILE ASP PRO THR PRO GLU GLN TRP LYS
SEQRES 16 B 422 GLN ILE ALA SER VAL MET LYS HIS ARG PHE LEU PHE PRO
SEQRES 17 B 422 PHE PHE ASP SER ALA TYR GLN GLY PHE ALA SER GLY ASN
SEQRES 18 B 422 LEU GLU ARG ASP ALA TRP ALA ILE ARG TYR PHE VAL SER
SEQRES 19 B 422 GLU GLY PHE GLU PHE PHE CYS ALA GLN SER PHE SER LYS
SEQRES 20 B 422 ASN PHE GLY LEU TYR ASN GLU ARG VAL GLY ASN LEU THR
SEQRES 21 B 422 VAL VAL GLY LYS GLU PRO GLU SER ILE LEU GLN VAL LEU
SEQRES 22 B 422 SER GLN MET GLU LYS ILE VAL ARG ILE THR TRP SER ASN
SEQRES 23 B 422 PRO PRO ALA GLN GLY ALA ARG ILE VAL ALA SER THR LEU
SEQRES 24 B 422 SER ASN PRO GLU LEU PHE GLU GLU TRP THR GLY ASN VAL
SEQRES 25 B 422 LYS THR MET ALA ASP ARG ILE LEU THR MET ARG SER GLU
SEQRES 26 B 422 LEU ARG ALA ARG LEU GLU ALA LEU LYS THR PRO GLY THR
SEQRES 27 B 422 TRP ASN HIS ILE THR ASP GLN ILE GLY MET PHE SER PHE
SEQRES 28 B 422 THR GLY LEU ASN PRO LYS GLN VAL GLU TYR LEU VAL ASN
SEQRES 29 B 422 GLU LYS HIS ILE TYR LEU LEU PRO SER GLY ARG ILE ASN
SEQRES 30 B 422 VAL SER GLY LEU THR THR LYS ASN LEU ASP TYR VAL ALA
SEQRES 31 B 422 THR SER ILE HIS GLU ALA VAL THR LYS ILE ALA GLU ASN
SEQRES 32 B 422 LEU TYR PHE GLN SER HIS HIS HIS HIS HIS HIS ASP TYR
SEQRES 33 B 422 LYS ASP ASP ASP ASP LYS
SEQRES 1 C 422 MET GLN PRO VAL LEU VAL PHE LYS LEU THR ALA ASP PHE
SEQRES 2 C 422 ARG GLU ASP PRO ASP PRO ARG LYS VAL ASN LEU GLY VAL
SEQRES 3 C 422 GLY ALA TYR ARG THR ASP ASP CYS HIS PRO TRP VAL LEU
SEQRES 4 C 422 PRO VAL VAL LYS LYS VAL GLU GLN LYS ILE ALA ASN ASP
SEQRES 5 C 422 ASN SER LEU ASN HIS GLU TYR LEU PRO ILE LEU GLY LEU
SEQRES 6 C 422 ALA GLU PHE ARG SER CYS ALA SER ARG LEU ALA LEU GLY
SEQRES 7 C 422 ASP ASP SER PRO ALA LEU LYS GLU LYS ARG VAL GLY GLY
SEQRES 8 C 422 VAL GLN SER LEU GLY GLY THR GLY ALA LEU ARG ILE GLY
SEQRES 9 C 422 ALA ASP PHE LEU ALA ARG TRP TYR ASN GLY THR ASN ASN
SEQRES 10 C 422 LYS ASN THR PRO VAL TYR VAL SER SER PRO THR TRP GLU
SEQRES 11 C 422 ASN HIS ASN ALA VAL PHE SER ALA ALA GLY PHE LYS ASP
SEQRES 12 C 422 ILE ARG SER TYR ARG TYR TRP ASP ALA GLU LYS ARG GLY
SEQRES 13 C 422 LEU ASP LEU GLN GLY PHE LEU ASN ASP LEU GLU ASN ALA
SEQRES 14 C 422 PRO GLU PHE SER ILE VAL VAL LEU HIS ALA CYS ALA HIS
SEQRES 15 C 422 ASN PRO THR GLY ILE ASP PRO THR PRO GLU GLN TRP LYS
SEQRES 16 C 422 GLN ILE ALA SER VAL MET LYS HIS ARG PHE LEU PHE PRO
SEQRES 17 C 422 PHE PHE ASP SER ALA TYR GLN GLY PHE ALA SER GLY ASN
SEQRES 18 C 422 LEU GLU ARG ASP ALA TRP ALA ILE ARG TYR PHE VAL SER
SEQRES 19 C 422 GLU GLY PHE GLU PHE PHE CYS ALA GLN SER PHE SER LYS
SEQRES 20 C 422 ASN PHE GLY LEU TYR ASN GLU ARG VAL GLY ASN LEU THR
SEQRES 21 C 422 VAL VAL GLY LYS GLU PRO GLU SER ILE LEU GLN VAL LEU
SEQRES 22 C 422 SER GLN MET GLU LYS ILE VAL ARG ILE THR TRP SER ASN
SEQRES 23 C 422 PRO PRO ALA GLN GLY ALA ARG ILE VAL ALA SER THR LEU
SEQRES 24 C 422 SER ASN PRO GLU LEU PHE GLU GLU TRP THR GLY ASN VAL
SEQRES 25 C 422 LYS THR MET ALA ASP ARG ILE LEU THR MET ARG SER GLU
SEQRES 26 C 422 LEU ARG ALA ARG LEU GLU ALA LEU LYS THR PRO GLY THR
SEQRES 27 C 422 TRP ASN HIS ILE THR ASP GLN ILE GLY MET PHE SER PHE
SEQRES 28 C 422 THR GLY LEU ASN PRO LYS GLN VAL GLU TYR LEU VAL ASN
SEQRES 29 C 422 GLU LYS HIS ILE TYR LEU LEU PRO SER GLY ARG ILE ASN
SEQRES 30 C 422 VAL SER GLY LEU THR THR LYS ASN LEU ASP TYR VAL ALA
SEQRES 31 C 422 THR SER ILE HIS GLU ALA VAL THR LYS ILE ALA GLU ASN
SEQRES 32 C 422 LEU TYR PHE GLN SER HIS HIS HIS HIS HIS HIS ASP TYR
SEQRES 33 C 422 LYS ASP ASP ASP ASP LYS
SEQRES 1 D 422 MET GLN PRO VAL LEU VAL PHE LYS LEU THR ALA ASP PHE
SEQRES 2 D 422 ARG GLU ASP PRO ASP PRO ARG LYS VAL ASN LEU GLY VAL
SEQRES 3 D 422 GLY ALA TYR ARG THR ASP ASP CYS HIS PRO TRP VAL LEU
SEQRES 4 D 422 PRO VAL VAL LYS LYS VAL GLU GLN LYS ILE ALA ASN ASP
SEQRES 5 D 422 ASN SER LEU ASN HIS GLU TYR LEU PRO ILE LEU GLY LEU
SEQRES 6 D 422 ALA GLU PHE ARG SER CYS ALA SER ARG LEU ALA LEU GLY
SEQRES 7 D 422 ASP ASP SER PRO ALA LEU LYS GLU LYS ARG VAL GLY GLY
SEQRES 8 D 422 VAL GLN SER LEU GLY GLY THR GLY ALA LEU ARG ILE GLY
SEQRES 9 D 422 ALA ASP PHE LEU ALA ARG TRP TYR ASN GLY THR ASN ASN
SEQRES 10 D 422 LYS ASN THR PRO VAL TYR VAL SER SER PRO THR TRP GLU
SEQRES 11 D 422 ASN HIS ASN ALA VAL PHE SER ALA ALA GLY PHE LYS ASP
SEQRES 12 D 422 ILE ARG SER TYR ARG TYR TRP ASP ALA GLU LYS ARG GLY
SEQRES 13 D 422 LEU ASP LEU GLN GLY PHE LEU ASN ASP LEU GLU ASN ALA
SEQRES 14 D 422 PRO GLU PHE SER ILE VAL VAL LEU HIS ALA CYS ALA HIS
SEQRES 15 D 422 ASN PRO THR GLY ILE ASP PRO THR PRO GLU GLN TRP LYS
SEQRES 16 D 422 GLN ILE ALA SER VAL MET LYS HIS ARG PHE LEU PHE PRO
SEQRES 17 D 422 PHE PHE ASP SER ALA TYR GLN GLY PHE ALA SER GLY ASN
SEQRES 18 D 422 LEU GLU ARG ASP ALA TRP ALA ILE ARG TYR PHE VAL SER
SEQRES 19 D 422 GLU GLY PHE GLU PHE PHE CYS ALA GLN SER PHE SER LYS
SEQRES 20 D 422 ASN PHE GLY LEU TYR ASN GLU ARG VAL GLY ASN LEU THR
SEQRES 21 D 422 VAL VAL GLY LYS GLU PRO GLU SER ILE LEU GLN VAL LEU
SEQRES 22 D 422 SER GLN MET GLU LYS ILE VAL ARG ILE THR TRP SER ASN
SEQRES 23 D 422 PRO PRO ALA GLN GLY ALA ARG ILE VAL ALA SER THR LEU
SEQRES 24 D 422 SER ASN PRO GLU LEU PHE GLU GLU TRP THR GLY ASN VAL
SEQRES 25 D 422 LYS THR MET ALA ASP ARG ILE LEU THR MET ARG SER GLU
SEQRES 26 D 422 LEU ARG ALA ARG LEU GLU ALA LEU LYS THR PRO GLY THR
SEQRES 27 D 422 TRP ASN HIS ILE THR ASP GLN ILE GLY MET PHE SER PHE
SEQRES 28 D 422 THR GLY LEU ASN PRO LYS GLN VAL GLU TYR LEU VAL ASN
SEQRES 29 D 422 GLU LYS HIS ILE TYR LEU LEU PRO SER GLY ARG ILE ASN
SEQRES 30 D 422 VAL SER GLY LEU THR THR LYS ASN LEU ASP TYR VAL ALA
SEQRES 31 D 422 THR SER ILE HIS GLU ALA VAL THR LYS ILE ALA GLU ASN
SEQRES 32 D 422 LEU TYR PHE GLN SER HIS HIS HIS HIS HIS HIS ASP TYR
SEQRES 33 D 422 LYS ASP ASP ASP ASP LYS
HET PLP A 1 16
HET TAR A 435 10
HET EDO A 3 4
HET EDO A 11 4
HET EDO A 436 4
HET PLP B 2 16
HET TAR B 435 10
HET EDO B 1 4
HET EDO B 10 4
HET EDO B 436 4
HET PLP C 3 16
HET TAR C 435 10
HET EDO C 5 4
HET EDO C 7 4
HET EDO C 12 4
HET EDO C 436 4
HET PLP D 4 16
HET TAR D 435 10
HET EDO D 6 4
HET EDO D 8 4
HET EDO D 9 4
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM TAR D(-)-TARTARIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETSYN PLP VITAMIN B6 PHOSPHATE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 PLP 4(C8 H10 N O6 P)
FORMUL 6 TAR 4(C4 H6 O6)
FORMUL 7 EDO 13(C2 H6 O2)
FORMUL 26 HOH *733(H2 O)
HELIX 1 1 VAL A 16 ASP A 28 1 13
HELIX 2 2 LEU A 51 ASN A 63 1 13
HELIX 3 3 LEU A 77 GLY A 90 1 14
HELIX 4 4 SER A 93 GLU A 98 1 6
HELIX 5 5 GLY A 108 TYR A 124 1 17
HELIX 6 6 GLU A 142 ALA A 151 1 10
HELIX 7 7 ASP A 170 ASN A 180 1 11
HELIX 8 8 THR A 202 PHE A 217 1 16
HELIX 9 9 ASN A 233 ALA A 238 1 6
HELIX 10 10 ALA A 238 GLU A 247 1 10
HELIX 11 11 LEU A 263 GLU A 266 5 4
HELIX 12 12 GLU A 277 ILE A 294 1 18
HELIX 13 13 ALA A 301 SER A 312 1 12
HELIX 14 14 ASN A 313 LEU A 345 1 33
HELIX 15 15 TRP A 351 GLN A 357 1 7
HELIX 16 16 ASN A 367 HIS A 379 1 13
HELIX 17 17 SER A 391 LEU A 393 5 3
HELIX 18 18 ASN A 397 ILE A 412 1 16
HELIX 19 19 VAL B 16 ASP B 28 1 13
HELIX 20 20 LEU B 51 ASP B 64 1 14
HELIX 21 21 LEU B 77 GLY B 90 1 14
HELIX 22 22 SER B 93 GLU B 98 1 6
HELIX 23 23 GLY B 108 TYR B 124 1 17
HELIX 24 24 GLU B 142 ALA B 151 1 10
HELIX 25 25 ASP B 170 ASN B 180 1 11
HELIX 26 26 THR B 202 PHE B 217 1 16
HELIX 27 27 ASN B 233 ALA B 238 1 6
HELIX 28 28 ALA B 238 GLU B 247 1 10
HELIX 29 29 LEU B 263 GLU B 266 5 4
HELIX 30 30 GLU B 277 ILE B 294 1 18
HELIX 31 31 ALA B 301 SER B 312 1 12
HELIX 32 32 ASN B 313 LEU B 345 1 33
HELIX 33 33 TRP B 351 GLN B 357 1 7
HELIX 34 34 ASN B 367 HIS B 379 1 13
HELIX 35 35 SER B 391 LEU B 393 5 3
HELIX 36 36 ASN B 397 ILE B 412 1 16
HELIX 37 37 VAL C 16 ASP C 28 1 13
HELIX 38 38 LEU C 51 ASN C 63 1 13
HELIX 39 39 LEU C 77 GLY C 90 1 14
HELIX 40 40 SER C 93 GLU C 98 1 6
HELIX 41 41 GLY C 108 TYR C 124 1 17
HELIX 42 42 GLU C 142 GLY C 152 1 11
HELIX 43 43 ASP C 170 ASN C 180 1 11
HELIX 44 44 THR C 202 PHE C 217 1 16
HELIX 45 45 ASN C 233 ALA C 238 1 6
HELIX 46 46 ALA C 238 GLU C 247 1 10
HELIX 47 47 LEU C 263 GLU C 266 5 4
HELIX 48 48 GLU C 277 ILE C 294 1 18
HELIX 49 49 ALA C 301 SER C 312 1 12
HELIX 50 50 ASN C 313 LEU C 345 1 33
HELIX 51 51 TRP C 351 GLN C 357 1 7
HELIX 52 52 ASN C 367 HIS C 379 1 13
HELIX 53 53 SER C 391 LEU C 393 5 3
HELIX 54 54 ASN C 397 ILE C 412 1 16
HELIX 55 55 VAL D 16 ASP D 28 1 13
HELIX 56 56 LEU D 51 ASP D 64 1 14
HELIX 57 57 LEU D 77 GLY D 90 1 14
HELIX 58 58 SER D 93 GLU D 98 1 6
HELIX 59 59 GLY D 108 TYR D 124 1 17
HELIX 60 60 GLU D 142 GLY D 152 1 11
HELIX 61 61 ASP D 170 ASN D 180 1 11
HELIX 62 62 THR D 202 ARG D 216 1 15
HELIX 63 63 ASN D 233 ALA D 238 1 6
HELIX 64 64 ALA D 238 GLU D 247 1 10
HELIX 65 65 LEU D 263 GLU D 266 5 4
HELIX 66 66 GLU D 277 ILE D 294 1 18
HELIX 67 67 ALA D 301 ASN D 313 1 13
HELIX 68 68 ASN D 313 LEU D 345 1 33
HELIX 69 69 TRP D 351 GLN D 357 1 7
HELIX 70 70 ASN D 367 GLU D 377 1 11
HELIX 71 71 SER D 391 LEU D 393 5 3
HELIX 72 72 ASN D 397 ILE D 412 1 16
SHEET 1 A 2 VAL A 34 ASN A 35 0
SHEET 2 A 2 ILE A 380 TYR A 381 1 O TYR A 381 N VAL A 34
SHEET 1 B 7 VAL A 101 LEU A 107 0
SHEET 2 B 7 VAL A 268 VAL A 274 -1 O LEU A 271 N VAL A 104
SHEET 3 B 7 PHE A 251 SER A 256 -1 N GLN A 255 O ASN A 270
SHEET 4 B 7 PHE A 219 SER A 224 1 N SER A 224 O ALA A 254
SHEET 5 B 7 ILE A 186 HIS A 190 1 N VAL A 187 O PHE A 219
SHEET 6 B 7 VAL A 134 SER A 138 1 N TYR A 135 O ILE A 186
SHEET 7 B 7 ILE A 156 ARG A 160 1 O ARG A 157 N VAL A 134
SHEET 1 C 2 TRP A 162 ASP A 163 0
SHEET 2 C 2 GLY A 168 LEU A 169 -1 O GLY A 168 N ASP A 163
SHEET 1 D 2 PHE A 361 PHE A 363 0
SHEET 2 D 2 ARG A 387 ASN A 389 -1 O ILE A 388 N SER A 362
SHEET 1 E 2 VAL B 34 ASN B 35 0
SHEET 2 E 2 ILE B 380 TYR B 381 1 O TYR B 381 N VAL B 34
SHEET 1 F 7 VAL B 101 LEU B 107 0
SHEET 2 F 7 VAL B 268 VAL B 274 -1 O LEU B 271 N VAL B 104
SHEET 3 F 7 PHE B 251 SER B 256 -1 N GLN B 255 O ASN B 270
SHEET 4 F 7 PHE B 219 SER B 224 1 N SER B 224 O ALA B 254
SHEET 5 F 7 ILE B 186 HIS B 190 1 N VAL B 187 O PHE B 219
SHEET 6 F 7 VAL B 134 SER B 138 1 N TYR B 135 O ILE B 186
SHEET 7 F 7 ILE B 156 ARG B 160 1 O ARG B 157 N VAL B 134
SHEET 1 G 2 TRP B 162 ASP B 163 0
SHEET 2 G 2 GLY B 168 LEU B 169 -1 O GLY B 168 N ASP B 163
SHEET 1 H 2 PHE B 361 PHE B 363 0
SHEET 2 H 2 ARG B 387 ASN B 389 -1 O ILE B 388 N SER B 362
SHEET 1 I 2 VAL C 34 ASN C 35 0
SHEET 2 I 2 ILE C 380 TYR C 381 1 O TYR C 381 N VAL C 34
SHEET 1 J 7 VAL C 101 LEU C 107 0
SHEET 2 J 7 VAL C 268 VAL C 274 -1 O VAL C 273 N GLY C 102
SHEET 3 J 7 PHE C 251 SER C 256 -1 N GLN C 255 O ASN C 270
SHEET 4 J 7 PHE C 219 SER C 224 1 N SER C 224 O ALA C 254
SHEET 5 J 7 ILE C 186 HIS C 190 1 N VAL C 187 O PHE C 219
SHEET 6 J 7 VAL C 134 SER C 138 1 N TYR C 135 O VAL C 188
SHEET 7 J 7 ILE C 156 ARG C 160 1 O ARG C 157 N VAL C 134
SHEET 1 K 2 TRP C 162 ASP C 163 0
SHEET 2 K 2 GLY C 168 LEU C 169 -1 O GLY C 168 N ASP C 163
SHEET 1 L 2 PHE C 361 PHE C 363 0
SHEET 2 L 2 ARG C 387 ASN C 389 -1 O ILE C 388 N SER C 362
SHEET 1 M 2 VAL D 34 ASN D 35 0
SHEET 2 M 2 ILE D 380 TYR D 381 1 O TYR D 381 N VAL D 34
SHEET 1 N 7 VAL D 101 LEU D 107 0
SHEET 2 N 7 VAL D 268 VAL D 274 -1 O VAL D 273 N GLY D 102
SHEET 3 N 7 PHE D 251 SER D 256 -1 N GLN D 255 O ASN D 270
SHEET 4 N 7 PHE D 219 SER D 224 1 N PHE D 222 O ALA D 254
SHEET 5 N 7 ILE D 186 HIS D 190 1 N VAL D 187 O PHE D 219
SHEET 6 N 7 VAL D 134 SER D 138 1 N TYR D 135 O VAL D 188
SHEET 7 N 7 ILE D 156 ARG D 160 1 O ARG D 157 N VAL D 134
SHEET 1 O 2 TRP D 162 ASP D 163 0
SHEET 2 O 2 GLY D 168 LEU D 169 -1 O GLY D 168 N ASP D 163
SHEET 1 P 2 PHE D 361 PHE D 363 0
SHEET 2 P 2 ARG D 387 ASN D 389 -1 O ILE D 388 N SER D 362
CISPEP 1 SER A 138 PRO A 139 0 -6.80
CISPEP 2 ASN A 195 PRO A 196 0 14.51
CISPEP 3 SER B 138 PRO B 139 0 -2.70
CISPEP 4 ASN B 195 PRO B 196 0 15.36
CISPEP 5 GLN C 14 PRO C 15 0 6.67
CISPEP 6 SER C 138 PRO C 139 0 -5.18
CISPEP 7 ASN C 195 PRO C 196 0 14.75
CISPEP 8 GLN D 14 PRO D 15 0 8.16
CISPEP 9 SER D 138 PRO D 139 0 -4.30
CISPEP 10 ASN D 195 PRO D 196 0 16.94
SITE 1 AC1 15 GLY A 108 GLY A 109 THR A 110 TRP A 141
SITE 2 AC1 15 ASN A 195 ASP A 223 ALA A 225 TYR A 226
SITE 3 AC1 15 SER A 256 SER A 258 LYS A 259 ARG A 267
SITE 4 AC1 15 TAR A 435 HOH A 445 TYR D 71
SITE 1 AC2 15 PLP A 1 VAL A 18 PHE A 19 VAL A 38
SITE 2 AC2 15 GLY A 39 TRP A 141 ASN A 195 TYR A 226
SITE 3 AC2 15 LYS A 259 PHE A 361 ARG A 387 HOH A 445
SITE 4 AC2 15 HOH A 548 TYR D 71 ARG D 293
SITE 1 AC3 4 ASN A 128 LYS A 130 HOH A 438 EDO C 7
SITE 1 AC4 5 TYR A 41 THR A 43 TRP A 49 HOH A 455
SITE 2 AC4 5 HOH A 500
SITE 1 AC5 7 ALA A 78 ARG A 81 SER A 82 SER A 85
SITE 2 AC5 7 GLY A 102 GLY A 103 HOH A 475
SITE 1 AC6 15 GLY B 108 GLY B 109 THR B 110 TRP B 141
SITE 2 AC6 15 ASN B 195 ASP B 223 ALA B 225 TYR B 226
SITE 3 AC6 15 SER B 256 SER B 258 LYS B 259 ARG B 267
SITE 4 AC6 15 TAR B 435 HOH B 483 TYR C 71
SITE 1 AC7 14 PLP B 2 VAL B 18 PHE B 19 VAL B 38
SITE 2 AC7 14 GLY B 39 TRP B 141 ASN B 195 TYR B 226
SITE 3 AC7 14 LYS B 259 ARG B 387 HOH B 483 HOH B 576
SITE 4 AC7 14 TYR C 71 ARG C 293
SITE 1 AC8 4 TYR B 41 THR B 43 TRP B 49 HOH B 551
SITE 1 AC9 4 ASN B 128 LYS B 130 HOH B 470 EDO D 6
SITE 1 BC1 6 ALA B 78 ARG B 81 SER B 82 GLY B 103
SITE 2 BC1 6 HOH B 510 HOH B 696
SITE 1 BC2 14 TYR B 71 HOH B 462 GLY C 108 GLY C 109
SITE 2 BC2 14 THR C 110 TRP C 141 ASN C 195 ASP C 223
SITE 3 BC2 14 TYR C 226 SER C 256 SER C 258 LYS C 259
SITE 4 BC2 14 ARG C 267 TAR C 435
SITE 1 BC3 15 TYR B 71 ARG B 293 HOH B 462 PLP C 3
SITE 2 BC3 15 VAL C 18 PHE C 19 VAL C 38 GLY C 39
SITE 3 BC3 15 TRP C 141 ASN C 195 TYR C 226 LYS C 259
SITE 4 BC3 15 PHE C 361 ARG C 387 HOH C 527
SITE 1 BC4 3 LEU A 416 TYR C 124 ASN C 125
SITE 1 BC5 3 EDO A 3 ARG C 157 SER C 158
SITE 1 BC6 3 TYR C 41 THR C 326 HOH C 704
SITE 1 BC7 4 ARG C 81 GLY C 103 HOH C 467 HOH C 468
SITE 1 BC8 14 TYR A 71 HOH A 458 GLY D 108 GLY D 109
SITE 2 BC8 14 THR D 110 TRP D 141 ASN D 195 ASP D 223
SITE 3 BC8 14 TYR D 226 SER D 256 SER D 258 LYS D 259
SITE 4 BC8 14 ARG D 267 TAR D 435
SITE 1 BC9 14 TYR A 71 ARG A 293 HOH A 458 PLP D 4
SITE 2 BC9 14 VAL D 18 PHE D 19 GLY D 39 TRP D 141
SITE 3 BC9 14 ASN D 195 TYR D 226 LYS D 259 PHE D 361
SITE 4 BC9 14 ARG D 387 HOH D 521
SITE 1 CC1 3 EDO B 10 ARG D 157 SER D 158
SITE 1 CC2 4 TYR D 41 THR D 43 TRP D 49 HOH D 497
SITE 1 CC3 5 ARG D 81 SER D 85 VAL D 101 HOH D 535
SITE 2 CC3 5 HOH D 551
CRYST1 78.531 107.347 239.997 90.00 90.00 90.00 P 21 21 21 16
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 0.012734 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009316 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004167 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
