HEADER TRANSFERASE/CELL CYCLE 24-MAY-19 6K4L
TITLE CRYSTAL STRUCTURE OF SE-LABELLED SIDJ COMPLEX WITH CAM AT 2.95 A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIDJ;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: CALMODULIN-1;
COMPND 7 CHAIN: C, D;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEGIONELLA PNEUMOPHILA SUBSP. PNEUMOPHILA STR.
SOURCE 3 PHILADELPHIA 1;
SOURCE 4 ORGANISM_TAXID: 272624;
SOURCE 5 GENE: LPG2155;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: CALM1, CALM, CAM, CAM1;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS EFFECT FACTOR, TOXIN, TRANSFERASE-CELL CYCLE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.Y.OUYANG
REVDAT 3 28-AUG-19 6K4L 1 JRNL
REVDAT 2 31-JUL-19 6K4L 1 JRNL
REVDAT 1 24-JUL-19 6K4L 0
JRNL AUTH N.GAN,X.ZHEN,Y.LIU,X.XU,C.HE,J.QIU,Y.LIU,G.M.FUJIMOTO,
JRNL AUTH 2 E.S.NAKAYASU,B.ZHOU,L.ZHAO,K.PUVAR,C.DAS,S.OUYANG,Z.Q.LUO
JRNL TITL REGULATION OF PHOSPHORIBOSYL UBIQUITINATION BY A
JRNL TITL 2 CALMODULIN-DEPENDENT GLUTAMYLASE.
JRNL REF NATURE V. 572 387 2019
JRNL REFN ESSN 1476-4687
JRNL PMID 31330531
JRNL DOI 10.1038/S41586-019-1439-1
REMARK 2
REMARK 2 RESOLUTION. 2.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 68.32
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 53446
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.244
REMARK 3 R VALUE (WORKING SET) : 0.243
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.820
REMARK 3 FREE R VALUE TEST SET COUNT : 2575
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 68.3343 - 7.7258 0.99 2867 131 0.2211 0.2163
REMARK 3 2 7.7258 - 6.1335 1.00 2860 132 0.2472 0.2521
REMARK 3 3 6.1335 - 5.3585 1.00 2887 126 0.2376 0.2419
REMARK 3 4 5.3585 - 4.8687 1.00 2825 132 0.2144 0.2168
REMARK 3 5 4.8687 - 4.5198 1.00 2836 159 0.1996 0.2248
REMARK 3 6 4.5198 - 4.2534 1.00 2791 158 0.2003 0.2705
REMARK 3 7 4.2534 - 4.0404 1.00 2806 145 0.2169 0.2592
REMARK 3 8 4.0404 - 3.8646 1.00 2811 169 0.2215 0.2820
REMARK 3 9 3.8646 - 3.7158 1.00 2788 172 0.2384 0.2559
REMARK 3 10 3.7158 - 3.5876 1.00 2808 155 0.2454 0.2722
REMARK 3 11 3.5876 - 3.4754 1.00 2835 135 0.2742 0.3113
REMARK 3 12 3.4754 - 3.3761 1.00 2788 153 0.2822 0.3388
REMARK 3 13 3.3761 - 3.2872 1.00 2849 136 0.2894 0.3092
REMARK 3 14 3.2872 - 3.2070 1.00 2818 122 0.2966 0.3284
REMARK 3 15 3.2070 - 3.1341 1.00 2867 118 0.3102 0.3529
REMARK 3 16 3.1341 - 3.0674 1.00 2804 149 0.3156 0.3453
REMARK 3 17 3.0674 - 3.0060 1.00 2823 138 0.3261 0.3552
REMARK 3 18 3.0060 - 2.9493 1.00 2808 145 0.3583 0.3942
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.450
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.740
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 12866
REMARK 3 ANGLE : 0.872 17496
REMARK 3 CHIRALITY : 0.049 2021
REMARK 3 PLANARITY : 0.005 2250
REMARK 3 DIHEDRAL : 5.430 7695
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 34.0432 50.9321 20.8439
REMARK 3 T TENSOR
REMARK 3 T11: 0.0751 T22: 0.1083
REMARK 3 T33: 0.1315 T12: 0.0019
REMARK 3 T13: -0.0191 T23: 0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 0.1137 L22: 0.2047
REMARK 3 L33: 0.5843 L12: -0.0039
REMARK 3 L13: -0.1390 L23: -0.1455
REMARK 3 S TENSOR
REMARK 3 S11: 0.0102 S12: -0.0455 S13: -0.0385
REMARK 3 S21: -0.0223 S22: -0.0466 S23: -0.0405
REMARK 3 S31: -0.0720 S32: 0.0561 S33: -0.0047
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6K4L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1300012267.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAY-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0-8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97981
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53504
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.949
REMARK 200 RESOLUTION RANGE LOW (A) : 133.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 2.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.2M NAI, PH 7.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 299K
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 79.62300
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 MSE A 1
REMARK 465 PHE A 2
REMARK 465 GLY A 3
REMARK 465 PHE A 4
REMARK 465 ILE A 5
REMARK 465 LYS A 6
REMARK 465 LYS A 7
REMARK 465 VAL A 8
REMARK 465 LEU A 9
REMARK 465 ASP A 10
REMARK 465 PHE A 11
REMARK 465 PHE A 12
REMARK 465 GLY A 13
REMARK 465 VAL A 14
REMARK 465 ASP A 15
REMARK 465 GLN A 16
REMARK 465 SER A 17
REMARK 465 GLU A 18
REMARK 465 ASP A 19
REMARK 465 ASN A 20
REMARK 465 PRO A 21
REMARK 465 SER A 22
REMARK 465 GLU A 23
REMARK 465 THR A 24
REMARK 465 ALA A 25
REMARK 465 VAL A 26
REMARK 465 GLU A 27
REMARK 465 THR A 28
REMARK 465 THR A 29
REMARK 465 ASP A 30
REMARK 465 VAL A 31
REMARK 465 SER A 32
REMARK 465 THR A 33
REMARK 465 LYS A 34
REMARK 465 ILE A 35
REMARK 465 LYS A 36
REMARK 465 THR A 37
REMARK 465 THR A 38
REMARK 465 ASP A 39
REMARK 465 THR A 40
REMARK 465 THR A 41
REMARK 465 GLN A 42
REMARK 465 GLU A 43
REMARK 465 GLU A 44
REMARK 465 SER A 45
REMARK 465 SER A 46
REMARK 465 VAL A 47
REMARK 465 LYS A 48
REMARK 465 THR A 49
REMARK 465 LYS A 50
REMARK 465 THR A 51
REMARK 465 VAL A 52
REMARK 465 VAL A 53
REMARK 465 PRO A 54
REMARK 465 THR A 55
REMARK 465 GLN A 56
REMARK 465 PRO A 57
REMARK 465 GLY A 58
REMARK 465 GLY A 59
REMARK 465 SER A 60
REMARK 465 VAL A 61
REMARK 465 LYS A 62
REMARK 465 PRO A 63
REMARK 465 GLU A 64
REMARK 465 THR A 65
REMARK 465 ILE A 66
REMARK 465 ALA A 67
REMARK 465 PRO A 68
REMARK 465 ASP A 69
REMARK 465 GLN A 70
REMARK 465 GLN A 71
REMARK 465 LYS A 72
REMARK 465 LYS A 73
REMARK 465 HIS A 74
REMARK 465 GLN A 75
REMARK 465 ILE A 76
REMARK 465 LYS A 77
REMARK 465 THR A 78
REMARK 465 GLU A 79
REMARK 465 THR A 80
REMARK 465 THR A 81
REMARK 465 THR A 82
REMARK 465 SER A 83
REMARK 465 THR A 84
REMARK 465 THR A 85
REMARK 465 LYS A 86
REMARK 465 GLN A 87
REMARK 465 LYS A 88
REMARK 465 GLY A 89
REMARK 465 PRO A 90
REMARK 465 LYS A 91
REMARK 465 VAL A 92
REMARK 465 THR A 93
REMARK 465 LEU A 94
REMARK 465 MSE A 95
REMARK 465 ASP A 96
REMARK 465 GLY A 97
REMARK 465 HIS A 98
REMARK 465 ASP A 424
REMARK 465 PHE A 425
REMARK 465 GLU A 426
REMARK 465 ARG A 427
REMARK 465 PHE A 428
REMARK 465 LYS A 429
REMARK 465 THR A 430
REMARK 465 LEU A 431
REMARK 465 HIS A 492
REMARK 465 THR A 493
REMARK 465 HIS A 494
REMARK 465 PHE A 495
REMARK 465 GLY A 496
REMARK 465 GLU A 497
REMARK 465 ASP A 498
REMARK 465 GLU A 499
REMARK 465 ARG A 500
REMARK 465 GLU A 501
REMARK 465 ASP A 502
REMARK 465 MSE A 626
REMARK 465 GLU A 847
REMARK 465 ALA A 848
REMARK 465 ARG A 849
REMARK 465 LYS A 850
REMARK 465 ASN A 851
REMARK 465 LEU A 852
REMARK 465 SER A 853
REMARK 465 GLU A 854
REMARK 465 LYS A 855
REMARK 465 SER A 856
REMARK 465 ASP A 857
REMARK 465 ILE A 858
REMARK 465 ASP A 859
REMARK 465 SER A 860
REMARK 465 GLU A 861
REMARK 465 LYS A 862
REMARK 465 PRO A 863
REMARK 465 GLU A 864
REMARK 465 SER A 865
REMARK 465 GLU A 866
REMARK 465 ARG A 867
REMARK 465 THR A 868
REMARK 465 THR A 869
REMARK 465 ASP A 870
REMARK 465 LYS A 871
REMARK 465 ARG A 872
REMARK 465 LEU A 873
REMARK 465 MSE B 1
REMARK 465 PHE B 2
REMARK 465 GLY B 3
REMARK 465 PHE B 4
REMARK 465 ILE B 5
REMARK 465 LYS B 6
REMARK 465 LYS B 7
REMARK 465 VAL B 8
REMARK 465 LEU B 9
REMARK 465 ASP B 10
REMARK 465 PHE B 11
REMARK 465 PHE B 12
REMARK 465 GLY B 13
REMARK 465 VAL B 14
REMARK 465 ASP B 15
REMARK 465 GLN B 16
REMARK 465 SER B 17
REMARK 465 GLU B 18
REMARK 465 ASP B 19
REMARK 465 ASN B 20
REMARK 465 PRO B 21
REMARK 465 SER B 22
REMARK 465 GLU B 23
REMARK 465 THR B 24
REMARK 465 ALA B 25
REMARK 465 VAL B 26
REMARK 465 GLU B 27
REMARK 465 THR B 28
REMARK 465 THR B 29
REMARK 465 ASP B 30
REMARK 465 VAL B 31
REMARK 465 SER B 32
REMARK 465 THR B 33
REMARK 465 LYS B 34
REMARK 465 ILE B 35
REMARK 465 LYS B 36
REMARK 465 THR B 37
REMARK 465 THR B 38
REMARK 465 ASP B 39
REMARK 465 THR B 40
REMARK 465 THR B 41
REMARK 465 GLN B 42
REMARK 465 GLU B 43
REMARK 465 GLU B 44
REMARK 465 SER B 45
REMARK 465 SER B 46
REMARK 465 VAL B 47
REMARK 465 LYS B 48
REMARK 465 THR B 49
REMARK 465 LYS B 50
REMARK 465 THR B 51
REMARK 465 VAL B 52
REMARK 465 VAL B 53
REMARK 465 PRO B 54
REMARK 465 THR B 55
REMARK 465 GLN B 56
REMARK 465 PRO B 57
REMARK 465 GLY B 58
REMARK 465 GLY B 59
REMARK 465 SER B 60
REMARK 465 VAL B 61
REMARK 465 LYS B 62
REMARK 465 PRO B 63
REMARK 465 GLU B 64
REMARK 465 THR B 65
REMARK 465 ILE B 66
REMARK 465 ALA B 67
REMARK 465 PRO B 68
REMARK 465 ASP B 69
REMARK 465 GLN B 70
REMARK 465 GLN B 71
REMARK 465 LYS B 72
REMARK 465 LYS B 73
REMARK 465 HIS B 74
REMARK 465 GLN B 75
REMARK 465 ILE B 76
REMARK 465 LYS B 77
REMARK 465 THR B 78
REMARK 465 GLU B 79
REMARK 465 THR B 80
REMARK 465 THR B 81
REMARK 465 THR B 82
REMARK 465 SER B 83
REMARK 465 THR B 84
REMARK 465 THR B 85
REMARK 465 LYS B 86
REMARK 465 GLN B 87
REMARK 465 LYS B 88
REMARK 465 GLY B 89
REMARK 465 PRO B 90
REMARK 465 LYS B 91
REMARK 465 VAL B 92
REMARK 465 THR B 93
REMARK 465 LEU B 94
REMARK 465 MSE B 95
REMARK 465 ASP B 96
REMARK 465 GLY B 97
REMARK 465 HIS B 98
REMARK 465 VAL B 99
REMARK 465 HIS B 492
REMARK 465 THR B 493
REMARK 465 HIS B 494
REMARK 465 PHE B 495
REMARK 465 GLY B 496
REMARK 465 GLU B 497
REMARK 465 ASP B 498
REMARK 465 GLU B 499
REMARK 465 ARG B 500
REMARK 465 GLU B 501
REMARK 465 ASP B 502
REMARK 465 GLU B 847
REMARK 465 ALA B 848
REMARK 465 ARG B 849
REMARK 465 LYS B 850
REMARK 465 ASN B 851
REMARK 465 LEU B 852
REMARK 465 SER B 853
REMARK 465 GLU B 854
REMARK 465 LYS B 855
REMARK 465 SER B 856
REMARK 465 ASP B 857
REMARK 465 ILE B 858
REMARK 465 ASP B 859
REMARK 465 SER B 860
REMARK 465 GLU B 861
REMARK 465 LYS B 862
REMARK 465 PRO B 863
REMARK 465 GLU B 864
REMARK 465 SER B 865
REMARK 465 GLU B 866
REMARK 465 ARG B 867
REMARK 465 THR B 868
REMARK 465 THR B 869
REMARK 465 ASP B 870
REMARK 465 LYS B 871
REMARK 465 ARG B 872
REMARK 465 LEU B 873
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 ASP C 3
REMARK 465 GLU C 115
REMARK 465 LYS C 116
REMARK 465 LEU C 117
REMARK 465 THR C 118
REMARK 465 ASP C 119
REMARK 465 GLU C 120
REMARK 465 GLU C 121
REMARK 465 VAL C 122
REMARK 465 ASP C 123
REMARK 465 GLU C 124
REMARK 465 MET C 125
REMARK 465 ILE C 126
REMARK 465 ARG C 127
REMARK 465 GLU C 128
REMARK 465 ALA C 129
REMARK 465 ASP C 130
REMARK 465 ILE C 131
REMARK 465 ASP C 132
REMARK 465 GLY C 133
REMARK 465 ASP C 134
REMARK 465 GLY C 135
REMARK 465 GLN C 136
REMARK 465 VAL C 137
REMARK 465 ASN C 138
REMARK 465 TYR C 139
REMARK 465 GLU C 140
REMARK 465 GLU C 141
REMARK 465 PHE C 142
REMARK 465 VAL C 143
REMARK 465 GLN C 144
REMARK 465 MET C 145
REMARK 465 MET C 146
REMARK 465 THR C 147
REMARK 465 ALA C 148
REMARK 465 LYS C 149
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 ASP D 3
REMARK 465 ILE D 53
REMARK 465 ASN D 54
REMARK 465 ARG D 87
REMARK 465 GLU D 88
REMARK 465 ALA D 89
REMARK 465 PHE D 90
REMARK 465 ARG D 91
REMARK 465 VAL D 92
REMARK 465 PHE D 93
REMARK 465 ASP D 94
REMARK 465 LYS D 95
REMARK 465 ASP D 96
REMARK 465 GLY D 97
REMARK 465 ASN D 98
REMARK 465 GLY D 99
REMARK 465 TYR D 100
REMARK 465 ILE D 101
REMARK 465 SER D 102
REMARK 465 ALA D 103
REMARK 465 ALA D 104
REMARK 465 GLU D 105
REMARK 465 LEU D 106
REMARK 465 ARG D 107
REMARK 465 HIS D 108
REMARK 465 VAL D 109
REMARK 465 MET D 110
REMARK 465 THR D 111
REMARK 465 ASN D 112
REMARK 465 LEU D 113
REMARK 465 GLY D 114
REMARK 465 GLU D 115
REMARK 465 LYS D 116
REMARK 465 LEU D 117
REMARK 465 THR D 118
REMARK 465 ASP D 119
REMARK 465 GLU D 120
REMARK 465 GLU D 121
REMARK 465 VAL D 122
REMARK 465 ASP D 123
REMARK 465 GLU D 124
REMARK 465 MET D 125
REMARK 465 ILE D 126
REMARK 465 ARG D 127
REMARK 465 GLU D 128
REMARK 465 ALA D 129
REMARK 465 ASP D 130
REMARK 465 ILE D 131
REMARK 465 ASP D 132
REMARK 465 GLY D 133
REMARK 465 ASP D 134
REMARK 465 GLY D 135
REMARK 465 GLN D 136
REMARK 465 VAL D 137
REMARK 465 ASN D 138
REMARK 465 TYR D 139
REMARK 465 GLU D 140
REMARK 465 GLU D 141
REMARK 465 PHE D 142
REMARK 465 VAL D 143
REMARK 465 GLN D 144
REMARK 465 MET D 145
REMARK 465 MET D 146
REMARK 465 THR D 147
REMARK 465 ALA D 148
REMARK 465 LYS D 149
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 100 CG CD CE NZ
REMARK 470 ARG A 106 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 127 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 159 CG CD CE NZ
REMARK 470 LYS A 211 CG CD CE NZ
REMARK 470 GLU A 215 CG CD OE1 OE2
REMARK 470 GLN A 259 CG CD OE1 NE2
REMARK 470 GLU A 294 CG CD OE1 OE2
REMARK 470 ARG A 295 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 323 CG CD OE1 OE2
REMARK 470 LYS A 328 CG CD CE NZ
REMARK 470 GLU A 329 CG CD OE1 OE2
REMARK 470 LYS A 330 CG CD CE NZ
REMARK 470 ASP A 334 CG OD1 OD2
REMARK 470 ASN A 361 CG OD1 ND2
REMARK 470 LYS A 370 CG CD CE NZ
REMARK 470 LYS A 371 CG CD CE NZ
REMARK 470 GLU A 373 CG CD OE1 OE2
REMARK 470 LYS A 375 CG CD CE NZ
REMARK 470 GLU A 380 CG CD OE1 OE2
REMARK 470 ARG A 393 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 403 CG CD OE1 NE2
REMARK 470 LYS A 411 CG CD CE NZ
REMARK 470 LYS A 412 CG CD CE NZ
REMARK 470 GLU A 414 CG CD OE1 OE2
REMARK 470 LEU A 416 CG CD1 CD2
REMARK 470 GLU A 417 CG CD OE1 OE2
REMARK 470 ILE A 418 CG1 CG2 CD1
REMARK 470 ARG A 420 CG CD NE CZ NH1 NH2
REMARK 470 SER A 422 OG
REMARK 470 LEU A 423 CG CD1 CD2
REMARK 470 ILE A 432 CG1 CG2 CD1
REMARK 470 ASP A 433 CG OD1 OD2
REMARK 470 SER A 435 OG
REMARK 470 LYS A 436 CG CD CE NZ
REMARK 470 LYS A 456 CG CD CE NZ
REMARK 470 ASP A 489 CG OD1 OD2
REMARK 470 PHE A 491 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 503 CG CD CE NZ
REMARK 470 LEU A 516 CG CD1 CD2
REMARK 470 GLN A 517 CG CD OE1 NE2
REMARK 470 PHE A 518 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 519 CG CD OE1 NE2
REMARK 470 LYS A 528 CG CD CE NZ
REMARK 470 LEU A 543 CG CD1 CD2
REMARK 470 ASP A 545 CG OD1 OD2
REMARK 470 ASP A 557 CG OD1 OD2
REMARK 470 HIS A 561 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 578 CG CD CE NZ
REMARK 470 ARG A 623 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 624 CG OD1 OD2
REMARK 470 ASP A 627 CG OD1 OD2
REMARK 470 LYS A 628 CG CD CE NZ
REMARK 470 LYS A 630 CG CD CE NZ
REMARK 470 LYS A 631 CG CD CE NZ
REMARK 470 GLU A 632 CG CD OE1 OE2
REMARK 470 LYS A 688 CG CD CE NZ
REMARK 470 GLU A 691 CG CD OE1 OE2
REMARK 470 GLN A 695 CG CD OE1 NE2
REMARK 470 SER A 703 OG
REMARK 470 GLU A 707 CG CD OE1 OE2
REMARK 470 GLU A 709 CG CD OE1 OE2
REMARK 470 LYS A 713 CG CD CE NZ
REMARK 470 LYS A 760 CG CD CE NZ
REMARK 470 LYS A 778 CG CD CE NZ
REMARK 470 ASN A 782 CG OD1 ND2
REMARK 470 ASP A 826 CG OD1 OD2
REMARK 470 ARG A 843 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 844 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP A 845 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 845 CZ3 CH2
REMARK 470 ARG A 846 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 100 CG CD CE NZ
REMARK 470 ARG B 106 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 107 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 127 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 159 CG CD CE NZ
REMARK 470 LYS B 205 CG CD CE NZ
REMARK 470 LYS B 211 CG CD CE NZ
REMARK 470 GLU B 215 CG CD OE1 OE2
REMARK 470 GLN B 259 CG CD OE1 NE2
REMARK 470 PHE B 292 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 294 CG CD OE1 OE2
REMARK 470 LYS B 328 CG CD CE NZ
REMARK 470 GLU B 329 CG CD OE1 OE2
REMARK 470 LYS B 330 CG CD CE NZ
REMARK 470 ASP B 344 CG OD1 OD2
REMARK 470 ARG B 345 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 360 CG CD OE1 NE2
REMARK 470 ASN B 361 CG OD1 ND2
REMARK 470 LYS B 370 CG CD CE NZ
REMARK 470 LYS B 371 CG CD CE NZ
REMARK 470 LYS B 375 CG CD CE NZ
REMARK 470 ARG B 393 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 403 CG CD OE1 NE2
REMARK 470 LYS B 411 CG CD CE NZ
REMARK 470 LYS B 412 CG CD CE NZ
REMARK 470 GLU B 414 CG CD OE1 OE2
REMARK 470 GLU B 417 CG CD OE1 OE2
REMARK 470 ARG B 420 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 423 CG CD1 CD2
REMARK 470 ASP B 424 CG OD1 OD2
REMARK 470 PHE B 425 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 426 CG CD OE1 OE2
REMARK 470 PHE B 428 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 429 CG CD CE NZ
REMARK 470 LEU B 431 CG CD1 CD2
REMARK 470 SER B 435 OG
REMARK 470 LYS B 436 CG CD CE NZ
REMARK 470 ASP B 437 CG OD1 OD2
REMARK 470 LEU B 438 CG CD1 CD2
REMARK 470 GLN B 447 CG CD OE1 NE2
REMARK 470 PHE B 491 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 503 CG CD CE NZ
REMARK 470 LEU B 516 CG CD1 CD2
REMARK 470 GLN B 517 CG CD OE1 NE2
REMARK 470 PHE B 518 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN B 519 CG CD OE1 NE2
REMARK 470 LEU B 520 CG CD1 CD2
REMARK 470 ASP B 545 CG OD1 OD2
REMARK 470 ASP B 557 CG OD1 OD2
REMARK 470 ASP B 624 CG OD1 OD2
REMARK 470 MSE B 625 CG SE CE
REMARK 470 ASP B 627 CG OD1 OD2
REMARK 470 LYS B 628 CG CD CE NZ
REMARK 470 LYS B 630 CG CD CE NZ
REMARK 470 GLU B 632 CG CD OE1 OE2
REMARK 470 GLU B 691 CG CD OE1 OE2
REMARK 470 GLN B 695 CG CD OE1 NE2
REMARK 470 GLU B 707 CG CD OE1 OE2
REMARK 470 GLU B 709 CG CD OE1 OE2
REMARK 470 LYS B 713 CG CD CE NZ
REMARK 470 LYS B 778 CG CD CE NZ
REMARK 470 ASN B 782 CG OD1 ND2
REMARK 470 GLN B 842 CG CD OE1 NE2
REMARK 470 ARG B 843 CG CD NE CZ NH1 NH2
REMARK 470 PHE B 844 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP B 845 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 845 CZ3 CH2
REMARK 470 ARG B 846 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 4 CG CD OE1 NE2
REMARK 470 GLU C 7 CG CD OE1 OE2
REMARK 470 GLU C 8 CG CD OE1 OE2
REMARK 470 ASP C 25 CG OD1 OD2
REMARK 470 LYS C 31 CG CD CE NZ
REMARK 470 THR C 45 OG1 CG2
REMARK 470 GLU C 46 CG CD OE1 OE2
REMARK 470 GLU C 48 CG CD OE1 OE2
REMARK 470 LEU C 49 CG CD1 CD2
REMARK 470 GLN C 50 CG CD OE1 NE2
REMARK 470 ASP C 51 CG OD1 OD2
REMARK 470 MET C 52 CG SD CE
REMARK 470 ILE C 53 CG1 CG2 CD1
REMARK 470 ASN C 54 CG OD1 ND2
REMARK 470 GLU C 55 CG CD OE1 OE2
REMARK 470 GLU C 68 CG CD OE1 OE2
REMARK 470 PHE C 69 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR C 71 OG1 CG2
REMARK 470 MET C 72 CG SD CE
REMARK 470 MET C 73 CG SD CE
REMARK 470 ARG C 75 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 76 CG CD CE NZ
REMARK 470 LYS C 78 CG CD CE NZ
REMARK 470 ASP C 79 CG OD1 OD2
REMARK 470 THR C 80 OG1 CG2
REMARK 470 ASP C 81 CG OD1 OD2
REMARK 470 SER C 82 OG
REMARK 470 GLU C 83 CG CD OE1 OE2
REMARK 470 GLU C 84 CG CD OE1 OE2
REMARK 470 ARG C 87 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 88 CG CD OE1 OE2
REMARK 470 PHE C 90 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG C 91 CG CD NE CZ NH1 NH2
REMARK 470 VAL C 92 CG1 CG2
REMARK 470 PHE C 93 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP C 94 CG OD1 OD2
REMARK 470 LYS C 95 CG CD CE NZ
REMARK 470 ASP C 96 CG OD1 OD2
REMARK 470 ASN C 98 CG OD1 ND2
REMARK 470 ILE C 101 CG1 CG2 CD1
REMARK 470 GLU C 105 CG CD OE1 OE2
REMARK 470 ARG C 107 CG CD NE CZ NH1 NH2
REMARK 470 HIS C 108 CG ND1 CD2 CE1 NE2
REMARK 470 VAL C 109 CG1 CG2
REMARK 470 MET C 110 CG SD CE
REMARK 470 THR C 111 OG1 CG2
REMARK 470 ASN C 112 CG OD1 ND2
REMARK 470 LEU C 113 CG CD1 CD2
REMARK 470 GLN D 4 CG CD OE1 NE2
REMARK 470 GLU D 7 CG CD OE1 OE2
REMARK 470 GLU D 8 CG CD OE1 OE2
REMARK 470 GLN D 9 CG CD OE1 NE2
REMARK 470 ILE D 28 CG1 CG2 CD1
REMARK 470 LYS D 31 CG CD CE NZ
REMARK 470 LEU D 33 CG CD1 CD2
REMARK 470 GLU D 46 CG CD OE1 OE2
REMARK 470 GLU D 48 CG CD OE1 OE2
REMARK 470 LEU D 49 CG CD1 CD2
REMARK 470 GLN D 50 CG CD OE1 NE2
REMARK 470 ASP D 51 CG OD1 OD2
REMARK 470 MET D 52 CG SD CE
REMARK 470 GLU D 55 CG CD OE1 OE2
REMARK 470 ASP D 57 CG OD1 OD2
REMARK 470 ASN D 61 CG OD1 ND2
REMARK 470 GLU D 68 CG CD OE1 OE2
REMARK 470 PHE D 69 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR D 71 OG1 CG2
REMARK 470 MET D 72 CG SD CE
REMARK 470 MET D 73 CG SD CE
REMARK 470 ARG D 75 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 76 CG CD CE NZ
REMARK 470 MET D 77 CG SD CE
REMARK 470 LYS D 78 CG CD CE NZ
REMARK 470 ASP D 79 CG OD1 OD2
REMARK 470 ASP D 81 CG OD1 OD2
REMARK 470 GLU D 83 CG CD OE1 OE2
REMARK 470 ILE D 86 CG1 CG2 CD1
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 THR C 80 N SER C 82 1.88
REMARK 500 NH1 ARG B 676 O SER B 700 1.98
REMARK 500 NZ LYS A 367 OE1 GLU A 381 1.98
REMARK 500 OE2 GLU A 137 NH1 ARG A 140 2.13
REMARK 500 O VAL D 36 OG SER D 39 2.15
REMARK 500 O GLN A 458 OH TYR A 617 2.15
REMARK 500 OG SER A 399 OD2 ASP A 473 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 CB SER A 435 CE MET C 77 2656 1.88
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 ASP A 542 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ASP A 692 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ASP A 692 CB - CG - OD2 ANGL. DEV. = -8.6 DEGREES
REMARK 500 GLU A 767 CA - CB - CG ANGL. DEV. = 15.4 DEGREES
REMARK 500 LEU B 346 CA - CB - CG ANGL. DEV. = 21.6 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 LYS A 229 48.65 -86.66
REMARK 500 ASN A 230 -175.39 -173.88
REMARK 500 ARG A 295 81.31 -67.05
REMARK 500 LEU A 296 -0.10 69.84
REMARK 500 GLN A 350 50.48 -93.79
REMARK 500 ARG A 352 16.46 46.92
REMARK 500 LEU A 509 69.86 -100.87
REMARK 500 TYR A 532 41.15 -104.90
REMARK 500 LEU A 543 30.87 -86.31
REMARK 500 THR A 568 -60.30 -95.78
REMARK 500 GLN A 695 45.38 -81.28
REMARK 500 VAL A 718 -60.71 -122.83
REMARK 500 ARG B 107 67.83 61.13
REMARK 500 PRO B 120 76.87 -69.64
REMARK 500 ASN B 230 -177.27 -171.54
REMARK 500 LEU B 296 -4.73 79.32
REMARK 500 ARG B 345 63.78 -102.27
REMARK 500 LEU B 423 1.50 -68.97
REMARK 500 ASP B 424 43.48 -141.28
REMARK 500 THR B 430 38.96 -97.22
REMARK 500 LEU B 431 67.50 63.12
REMARK 500 LEU B 438 48.49 34.04
REMARK 500 LEU B 509 71.00 -100.21
REMARK 500 GLN B 519 -22.35 84.02
REMARK 500 TYR B 532 40.12 -108.48
REMARK 500 MSE B 626 -2.88 77.49
REMARK 500 VAL B 718 -60.72 -122.65
REMARK 500 ASN C 43 74.75 -154.07
REMARK 500 GLN C 50 -15.32 82.93
REMARK 500 ASP C 51 -50.01 -148.33
REMARK 500 MET C 52 -28.39 65.74
REMARK 500 ILE C 53 -30.36 46.59
REMARK 500 ASN C 54 -62.95 -139.02
REMARK 500 ARG C 75 3.33 -67.05
REMARK 500 THR C 80 -88.97 -77.70
REMARK 500 ASP C 81 -42.15 -17.92
REMARK 500 ALA C 89 -80.11 -67.03
REMARK 500 PHE C 90 131.60 179.74
REMARK 500 ARG C 91 -9.39 61.91
REMARK 500 PHE C 93 -177.30 -68.88
REMARK 500 LYS C 95 -155.57 -148.34
REMARK 500 ALA C 104 82.55 -152.64
REMARK 500 GLU C 105 -61.36 -132.82
REMARK 500 LEU C 106 -0.03 -143.68
REMARK 500 HIS C 108 -154.72 -161.41
REMARK 500 VAL C 109 71.68 70.00
REMARK 500 MET C 110 63.04 66.40
REMARK 500 ASP D 25 40.88 -149.97
REMARK 500 THR D 29 73.01 59.06
REMARK 500 LYS D 31 10.28 -145.44
REMARK 500
REMARK 500 THIS ENTRY HAS 60 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 MSE B 625 MSE B 626 149.90
REMARK 500 GLN C 50 ASP C 51 147.29
REMARK 500 ILE C 53 ASN C 54 141.36
REMARK 500 PHE D 66 PRO D 67 135.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1004 DISTANCE = 8.11 ANGSTROMS
REMARK 525 HOH C 304 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH C 305 DISTANCE = 7.00 ANGSTROMS
REMARK 525 HOH C 306 DISTANCE = 7.76 ANGSTROMS
REMARK 525 HOH D 301 DISTANCE = 6.90 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 21 OD1
REMARK 620 2 ASP C 23 OD1 80.2
REMARK 620 3 THR C 27 O 153.3 126.2
REMARK 620 4 THR C 27 OG1 109.0 62.0 84.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 21 OD1
REMARK 620 2 ASP D 21 OD2 47.5
REMARK 620 3 ASP D 23 OD1 78.0 118.7
REMARK 620 4 THR D 27 OG1 75.9 118.8 54.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 201
DBREF 6K4L A 1 873 UNP Q5ZTK6 Q5ZTK6_LEGPH 1 873
DBREF 6K4L B 1 873 UNP Q5ZTK6 Q5ZTK6_LEGPH 1 873
DBREF 6K4L C 1 149 UNP P0DP23 CALM1_HUMAN 1 149
DBREF 6K4L D 1 149 UNP P0DP23 CALM1_HUMAN 1 149
SEQRES 1 A 873 MSE PHE GLY PHE ILE LYS LYS VAL LEU ASP PHE PHE GLY
SEQRES 2 A 873 VAL ASP GLN SER GLU ASP ASN PRO SER GLU THR ALA VAL
SEQRES 3 A 873 GLU THR THR ASP VAL SER THR LYS ILE LYS THR THR ASP
SEQRES 4 A 873 THR THR GLN GLU GLU SER SER VAL LYS THR LYS THR VAL
SEQRES 5 A 873 VAL PRO THR GLN PRO GLY GLY SER VAL LYS PRO GLU THR
SEQRES 6 A 873 ILE ALA PRO ASP GLN GLN LYS LYS HIS GLN ILE LYS THR
SEQRES 7 A 873 GLU THR THR THR SER THR THR LYS GLN LYS GLY PRO LYS
SEQRES 8 A 873 VAL THR LEU MSE ASP GLY HIS VAL LYS GLN TYR TYR PHE
SEQRES 9 A 873 ALA ARG ARG GLY GLU THR SER THR HIS ASP THR SER LEU
SEQRES 10 A 873 PRO PRO PRO VAL LYS VAL LEU SER GLY ARG SER ILE PRO
SEQRES 11 A 873 LEU LYS GLU ILE PRO PHE GLU ALA THR ARG ASN GLU LEU
SEQRES 12 A 873 VAL GLN ILE TYR LEU THR SER ILE ASP LYS LEU ILE LYS
SEQRES 13 A 873 SER ASN LYS LEU ASN SER ILE PRO SER GLN GLN ILE ALA
SEQRES 14 A 873 SER HIS TYR LEU PHE LEU ARG SER LEU ALA ASN SER GLU
SEQRES 15 A 873 THR ASP GLY ILE LYS LYS ASN GLN ILE LEU SER LEU ALA
SEQRES 16 A 873 LYS PRO LEU GLY THR TYR LEU ALA SER LYS GLU PRO HIS
SEQRES 17 A 873 VAL TRP LYS MSE ILE ASN GLU LEU ILE GLU LYS SER GLU
SEQRES 18 A 873 TYR PRO ILE ILE HIS TYR LEU LYS ASN ASN ARG ALA HIS
SEQRES 19 A 873 SER ASN PHE MSE LEU ALA LEU ILE HIS GLU TYR HIS LYS
SEQRES 20 A 873 GLU PRO LEU THR LYS ASN GLN SER ALA PHE VAL GLN LYS
SEQRES 21 A 873 PHE ARG ASP SER SER VAL PHE LEU PHE PRO ASN PRO ILE
SEQRES 22 A 873 TYR THR ALA TRP LEU ALA HIS SER TYR ASP GLU ASP SER
SEQRES 23 A 873 SER PHE ASN PRO MSE PHE ARG GLU ARG LEU SER THR ASN
SEQRES 24 A 873 PHE TYR HIS SER THR LEU THR ASP ASN LEU LEU LEU ARG
SEQRES 25 A 873 THR GLU PRO LYS GLU VAL THR LEU SER SER GLU HIS HIS
SEQRES 26 A 873 TYR LYS LYS GLU LYS GLY PRO ILE ASP SER SER PHE ARG
SEQRES 27 A 873 TYR GLN MSE SER SER ASP ARG LEU LEU ARG ILE GLN GLY
SEQRES 28 A 873 ARG THR LEU LEU PHE SER THR PRO GLN ASN ASP VAL VAL
SEQRES 29 A 873 ALA VAL LYS VAL GLN LYS LYS GLY GLU PRO LYS SER THR
SEQRES 30 A 873 LEU GLU GLU GLU PHE GLU MSE ALA ASP TYR LEU LEU LYS
SEQRES 31 A 873 HIS GLN ARG ARG LEU ASP VAL HIS SER LYS LEU PRO GLN
SEQRES 32 A 873 PRO LEU GLY GLN TYR SER VAL LYS LYS SER GLU ILE LEU
SEQRES 33 A 873 GLU ILE SER ARG GLY SER LEU ASP PHE GLU ARG PHE LYS
SEQRES 34 A 873 THR LEU ILE ASP ASP SER LYS ASP LEU GLU VAL TYR VAL
SEQRES 35 A 873 TYR LYS ALA PRO GLN SER TYR PHE THR TYR LEU HIS ASP
SEQRES 36 A 873 LYS ASN GLN ASP LEU GLU ASP LEU THR ALA SER VAL LYS
SEQRES 37 A 873 THR ASN VAL HIS ASP LEU PHE VAL LEU LEU ARG GLU GLY
SEQRES 38 A 873 ILE VAL PHE PRO GLN LEU ALA ASP ILE PHE HIS THR HIS
SEQRES 39 A 873 PHE GLY GLU ASP GLU ARG GLU ASP LYS GLY ARG TYR GLN
SEQRES 40 A 873 ALA LEU VAL GLN LEU LEU ASN VAL LEU GLN PHE GLN LEU
SEQRES 41 A 873 GLY ARG ILE ASP LYS TRP GLN LYS ALA VAL GLU TYR VAL
SEQRES 42 A 873 ASN LEU ARG SER SER GLY LEU ALA ASP LEU GLY ASP SER
SEQRES 43 A 873 LEU PRO ILE THR SER LEU PHE THR SER SER ASP PHE THR
SEQRES 44 A 873 LYS HIS TYR PHE SER GLU LEU LEU THR GLY GLY TYR HIS
SEQRES 45 A 873 PRO THR PHE PHE ASP LYS SER SER GLY THR ALA ASN SER
SEQRES 46 A 873 LEU PHE THR GLY LYS ARG ARG LEU PHE GLY ASN TYR LEU
SEQRES 47 A 873 TYR LEU ASN THR ILE ALA GLU TYR LEU LEU VAL ILE GLN
SEQRES 48 A 873 LEU THR LEU GLY SER TYR GLY ASP LYS VAL THR ARG ASP
SEQRES 49 A 873 MSE MSE ASP LYS PRO LYS LYS GLU ALA VAL TRP ARG GLU
SEQRES 50 A 873 LEU ALA ASN VAL MSE PHE THR SER CYS ALA GLU ALA ILE
SEQRES 51 A 873 HIS ILE MSE THR GLY ILE PRO GLN SER ARG ALA LEU THR
SEQRES 52 A 873 LEU LEU LYS GLN ARG ALA ASN ILE GLU LYS HIS PHE ARG
SEQRES 53 A 873 GLN THR GLN PHE TRP MSE THR PRO ASP TYR SER LYS LEU
SEQRES 54 A 873 ASP GLU ASP THR LEU GLN MSE GLU GLN TYR SER ILE TYR
SEQRES 55 A 873 SER GLY GLU PRO GLU TYR GLU PHE THR ASP LYS LEU VAL
SEQRES 56 A 873 SER GLY VAL GLY LEU SER VAL ASP GLY VAL HIS GLN ASP
SEQRES 57 A 873 LEU GLY GLY TYR ASN ARG GLU SER PRO LEU ARG GLU LEU
SEQRES 58 A 873 GLU LYS LEU LEU TYR ALA THR VAL THR LEU ILE GLU GLY
SEQRES 59 A 873 THR MSE GLN LEU ASP LYS GLU PHE PHE LYS GLN LEU GLU
SEQRES 60 A 873 GLN VAL GLU LYS ILE LEU SER GLY GLU ILE LYS THR ASP
SEQRES 61 A 873 ALA ASN SER CYS PHE GLU ALA VAL ALA GLN LEU LEU ASP
SEQRES 62 A 873 LEU ALA ARG PRO GLY CYS HIS PHE GLN LYS ARG LEU VAL
SEQRES 63 A 873 LEU SER TYR TYR GLU GLU ALA LYS LEU LYS TYR PRO SER
SEQRES 64 A 873 ALA PRO THR ASP ALA TYR ASP SER ARG PHE GLN VAL VAL
SEQRES 65 A 873 ALA ARG THR ASN ALA ALA ILE THR ILE GLN ARG PHE TRP
SEQRES 66 A 873 ARG GLU ALA ARG LYS ASN LEU SER GLU LYS SER ASP ILE
SEQRES 67 A 873 ASP SER GLU LYS PRO GLU SER GLU ARG THR THR ASP LYS
SEQRES 68 A 873 ARG LEU
SEQRES 1 B 873 MSE PHE GLY PHE ILE LYS LYS VAL LEU ASP PHE PHE GLY
SEQRES 2 B 873 VAL ASP GLN SER GLU ASP ASN PRO SER GLU THR ALA VAL
SEQRES 3 B 873 GLU THR THR ASP VAL SER THR LYS ILE LYS THR THR ASP
SEQRES 4 B 873 THR THR GLN GLU GLU SER SER VAL LYS THR LYS THR VAL
SEQRES 5 B 873 VAL PRO THR GLN PRO GLY GLY SER VAL LYS PRO GLU THR
SEQRES 6 B 873 ILE ALA PRO ASP GLN GLN LYS LYS HIS GLN ILE LYS THR
SEQRES 7 B 873 GLU THR THR THR SER THR THR LYS GLN LYS GLY PRO LYS
SEQRES 8 B 873 VAL THR LEU MSE ASP GLY HIS VAL LYS GLN TYR TYR PHE
SEQRES 9 B 873 ALA ARG ARG GLY GLU THR SER THR HIS ASP THR SER LEU
SEQRES 10 B 873 PRO PRO PRO VAL LYS VAL LEU SER GLY ARG SER ILE PRO
SEQRES 11 B 873 LEU LYS GLU ILE PRO PHE GLU ALA THR ARG ASN GLU LEU
SEQRES 12 B 873 VAL GLN ILE TYR LEU THR SER ILE ASP LYS LEU ILE LYS
SEQRES 13 B 873 SER ASN LYS LEU ASN SER ILE PRO SER GLN GLN ILE ALA
SEQRES 14 B 873 SER HIS TYR LEU PHE LEU ARG SER LEU ALA ASN SER GLU
SEQRES 15 B 873 THR ASP GLY ILE LYS LYS ASN GLN ILE LEU SER LEU ALA
SEQRES 16 B 873 LYS PRO LEU GLY THR TYR LEU ALA SER LYS GLU PRO HIS
SEQRES 17 B 873 VAL TRP LYS MSE ILE ASN GLU LEU ILE GLU LYS SER GLU
SEQRES 18 B 873 TYR PRO ILE ILE HIS TYR LEU LYS ASN ASN ARG ALA HIS
SEQRES 19 B 873 SER ASN PHE MSE LEU ALA LEU ILE HIS GLU TYR HIS LYS
SEQRES 20 B 873 GLU PRO LEU THR LYS ASN GLN SER ALA PHE VAL GLN LYS
SEQRES 21 B 873 PHE ARG ASP SER SER VAL PHE LEU PHE PRO ASN PRO ILE
SEQRES 22 B 873 TYR THR ALA TRP LEU ALA HIS SER TYR ASP GLU ASP SER
SEQRES 23 B 873 SER PHE ASN PRO MSE PHE ARG GLU ARG LEU SER THR ASN
SEQRES 24 B 873 PHE TYR HIS SER THR LEU THR ASP ASN LEU LEU LEU ARG
SEQRES 25 B 873 THR GLU PRO LYS GLU VAL THR LEU SER SER GLU HIS HIS
SEQRES 26 B 873 TYR LYS LYS GLU LYS GLY PRO ILE ASP SER SER PHE ARG
SEQRES 27 B 873 TYR GLN MSE SER SER ASP ARG LEU LEU ARG ILE GLN GLY
SEQRES 28 B 873 ARG THR LEU LEU PHE SER THR PRO GLN ASN ASP VAL VAL
SEQRES 29 B 873 ALA VAL LYS VAL GLN LYS LYS GLY GLU PRO LYS SER THR
SEQRES 30 B 873 LEU GLU GLU GLU PHE GLU MSE ALA ASP TYR LEU LEU LYS
SEQRES 31 B 873 HIS GLN ARG ARG LEU ASP VAL HIS SER LYS LEU PRO GLN
SEQRES 32 B 873 PRO LEU GLY GLN TYR SER VAL LYS LYS SER GLU ILE LEU
SEQRES 33 B 873 GLU ILE SER ARG GLY SER LEU ASP PHE GLU ARG PHE LYS
SEQRES 34 B 873 THR LEU ILE ASP ASP SER LYS ASP LEU GLU VAL TYR VAL
SEQRES 35 B 873 TYR LYS ALA PRO GLN SER TYR PHE THR TYR LEU HIS ASP
SEQRES 36 B 873 LYS ASN GLN ASP LEU GLU ASP LEU THR ALA SER VAL LYS
SEQRES 37 B 873 THR ASN VAL HIS ASP LEU PHE VAL LEU LEU ARG GLU GLY
SEQRES 38 B 873 ILE VAL PHE PRO GLN LEU ALA ASP ILE PHE HIS THR HIS
SEQRES 39 B 873 PHE GLY GLU ASP GLU ARG GLU ASP LYS GLY ARG TYR GLN
SEQRES 40 B 873 ALA LEU VAL GLN LEU LEU ASN VAL LEU GLN PHE GLN LEU
SEQRES 41 B 873 GLY ARG ILE ASP LYS TRP GLN LYS ALA VAL GLU TYR VAL
SEQRES 42 B 873 ASN LEU ARG SER SER GLY LEU ALA ASP LEU GLY ASP SER
SEQRES 43 B 873 LEU PRO ILE THR SER LEU PHE THR SER SER ASP PHE THR
SEQRES 44 B 873 LYS HIS TYR PHE SER GLU LEU LEU THR GLY GLY TYR HIS
SEQRES 45 B 873 PRO THR PHE PHE ASP LYS SER SER GLY THR ALA ASN SER
SEQRES 46 B 873 LEU PHE THR GLY LYS ARG ARG LEU PHE GLY ASN TYR LEU
SEQRES 47 B 873 TYR LEU ASN THR ILE ALA GLU TYR LEU LEU VAL ILE GLN
SEQRES 48 B 873 LEU THR LEU GLY SER TYR GLY ASP LYS VAL THR ARG ASP
SEQRES 49 B 873 MSE MSE ASP LYS PRO LYS LYS GLU ALA VAL TRP ARG GLU
SEQRES 50 B 873 LEU ALA ASN VAL MSE PHE THR SER CYS ALA GLU ALA ILE
SEQRES 51 B 873 HIS ILE MSE THR GLY ILE PRO GLN SER ARG ALA LEU THR
SEQRES 52 B 873 LEU LEU LYS GLN ARG ALA ASN ILE GLU LYS HIS PHE ARG
SEQRES 53 B 873 GLN THR GLN PHE TRP MSE THR PRO ASP TYR SER LYS LEU
SEQRES 54 B 873 ASP GLU ASP THR LEU GLN MSE GLU GLN TYR SER ILE TYR
SEQRES 55 B 873 SER GLY GLU PRO GLU TYR GLU PHE THR ASP LYS LEU VAL
SEQRES 56 B 873 SER GLY VAL GLY LEU SER VAL ASP GLY VAL HIS GLN ASP
SEQRES 57 B 873 LEU GLY GLY TYR ASN ARG GLU SER PRO LEU ARG GLU LEU
SEQRES 58 B 873 GLU LYS LEU LEU TYR ALA THR VAL THR LEU ILE GLU GLY
SEQRES 59 B 873 THR MSE GLN LEU ASP LYS GLU PHE PHE LYS GLN LEU GLU
SEQRES 60 B 873 GLN VAL GLU LYS ILE LEU SER GLY GLU ILE LYS THR ASP
SEQRES 61 B 873 ALA ASN SER CYS PHE GLU ALA VAL ALA GLN LEU LEU ASP
SEQRES 62 B 873 LEU ALA ARG PRO GLY CYS HIS PHE GLN LYS ARG LEU VAL
SEQRES 63 B 873 LEU SER TYR TYR GLU GLU ALA LYS LEU LYS TYR PRO SER
SEQRES 64 B 873 ALA PRO THR ASP ALA TYR ASP SER ARG PHE GLN VAL VAL
SEQRES 65 B 873 ALA ARG THR ASN ALA ALA ILE THR ILE GLN ARG PHE TRP
SEQRES 66 B 873 ARG GLU ALA ARG LYS ASN LEU SER GLU LYS SER ASP ILE
SEQRES 67 B 873 ASP SER GLU LYS PRO GLU SER GLU ARG THR THR ASP LYS
SEQRES 68 B 873 ARG LEU
SEQRES 1 C 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 C 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 C 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 C 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 C 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 C 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 C 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 C 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 C 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 C 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 C 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 C 149 GLN MET MET THR ALA LYS
SEQRES 1 D 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 D 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 D 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 D 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 D 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 D 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 D 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 D 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 D 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 D 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 D 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 D 149 GLN MET MET THR ALA LYS
MODRES 6K4L MSE A 212 MET MODIFIED RESIDUE
MODRES 6K4L MSE A 238 MET MODIFIED RESIDUE
MODRES 6K4L MSE A 291 MET MODIFIED RESIDUE
MODRES 6K4L MSE A 341 MET MODIFIED RESIDUE
MODRES 6K4L MSE A 384 MET MODIFIED RESIDUE
MODRES 6K4L MSE A 625 MET MODIFIED RESIDUE
MODRES 6K4L MSE A 642 MET MODIFIED RESIDUE
MODRES 6K4L MSE A 653 MET MODIFIED RESIDUE
MODRES 6K4L MSE A 682 MET MODIFIED RESIDUE
MODRES 6K4L MSE A 696 MET MODIFIED RESIDUE
MODRES 6K4L MSE A 756 MET MODIFIED RESIDUE
MODRES 6K4L MSE B 212 MET MODIFIED RESIDUE
MODRES 6K4L MSE B 238 MET MODIFIED RESIDUE
MODRES 6K4L MSE B 291 MET MODIFIED RESIDUE
MODRES 6K4L MSE B 341 MET MODIFIED RESIDUE
MODRES 6K4L MSE B 384 MET MODIFIED RESIDUE
MODRES 6K4L MSE B 626 MET MODIFIED RESIDUE
MODRES 6K4L MSE B 642 MET MODIFIED RESIDUE
MODRES 6K4L MSE B 653 MET MODIFIED RESIDUE
MODRES 6K4L MSE B 682 MET MODIFIED RESIDUE
MODRES 6K4L MSE B 696 MET MODIFIED RESIDUE
MODRES 6K4L MSE B 756 MET MODIFIED RESIDUE
HET MSE A 212 8
HET MSE A 238 8
HET MSE A 291 8
HET MSE A 341 8
HET MSE A 384 8
HET MSE A 625 8
HET MSE A 642 8
HET MSE A 653 8
HET MSE A 682 8
HET MSE A 696 8
HET MSE A 756 8
HET MSE B 212 8
HET MSE B 238 8
HET MSE B 291 8
HET MSE B 341 8
HET MSE B 384 8
HET MSE B 625 5
HET MSE B 626 8
HET MSE B 642 8
HET MSE B 653 8
HET MSE B 682 8
HET MSE B 696 8
HET MSE B 756 8
HET CL A 901 1
HET CL A 902 1
HET CL B 901 1
HET CL B 902 1
HET CA C 201 1
HET CA D 201 1
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM CA CALCIUM ION
FORMUL 1 MSE 23(C5 H11 N O2 SE)
FORMUL 5 CL 4(CL 1-)
FORMUL 9 CA 2(CA 2+)
FORMUL 11 HOH *16(H2 O)
HELIX 1 AA1 PRO A 135 SER A 157 1 23
HELIX 2 AA2 PRO A 164 GLU A 182 1 19
HELIX 3 AA3 ASP A 184 GLU A 206 1 23
HELIX 4 AA4 GLU A 206 GLU A 218 1 13
HELIX 5 AA5 TYR A 222 LEU A 228 1 7
HELIX 6 AA6 ASN A 230 SER A 235 5 6
HELIX 7 AA7 ASN A 236 HIS A 246 1 11
HELIX 8 AA8 THR A 251 PHE A 261 1 11
HELIX 9 AA9 SER A 264 PHE A 269 5 6
HELIX 10 AB1 PRO A 270 SER A 281 1 12
HELIX 11 AB2 TYR A 301 LEU A 311 1 11
HELIX 12 AB3 PRO A 374 HIS A 391 1 18
HELIX 13 AB4 HIS A 391 ASP A 396 1 6
HELIX 14 AB5 LYS A 412 ILE A 418 1 7
HELIX 15 AB6 PRO A 446 THR A 451 5 6
HELIX 16 AB7 ASP A 459 GLU A 480 1 22
HELIX 17 AB8 LEU A 509 LEU A 513 5 5
HELIX 18 AB9 LYS A 525 VAL A 530 1 6
HELIX 19 AC1 THR A 550 THR A 554 5 5
HELIX 20 AC2 SER A 556 PHE A 563 1 8
HELIX 21 AC3 PHE A 563 GLY A 569 1 7
HELIX 22 AC4 HIS A 572 THR A 574 5 3
HELIX 23 AC5 LEU A 586 ARG A 592 5 7
HELIX 24 AC6 LEU A 593 ARG A 623 1 31
HELIX 25 AC7 LYS A 628 GLY A 655 1 28
HELIX 26 AC8 PRO A 657 ALA A 669 1 13
HELIX 27 AC9 ASN A 670 MSE A 682 1 13
HELIX 28 AD1 THR A 683 LEU A 689 5 7
HELIX 29 AD2 ASP A 690 TYR A 702 1 13
HELIX 30 AD3 LEU A 738 SER A 774 1 37
HELIX 31 AD4 ASP A 780 LEU A 794 1 15
HELIX 32 AD5 CYS A 799 TYR A 817 1 19
HELIX 33 AD6 THR A 822 PHE A 844 1 23
HELIX 34 AD7 PRO B 135 SER B 157 1 23
HELIX 35 AD8 LYS B 159 ILE B 163 5 5
HELIX 36 AD9 PRO B 164 GLU B 182 1 19
HELIX 37 AE1 ASP B 184 GLU B 206 1 23
HELIX 38 AE2 GLU B 206 GLU B 218 1 13
HELIX 39 AE3 TYR B 222 LEU B 228 1 7
HELIX 40 AE4 ASN B 230 SER B 235 5 6
HELIX 41 AE5 ASN B 236 HIS B 246 1 11
HELIX 42 AE6 THR B 251 PHE B 261 1 11
HELIX 43 AE7 SER B 264 PHE B 269 5 6
HELIX 44 AE8 PRO B 270 SER B 281 1 12
HELIX 45 AE9 TYR B 301 LEU B 311 1 11
HELIX 46 AF1 PRO B 374 HIS B 391 1 18
HELIX 47 AF2 HIS B 391 ASP B 396 1 6
HELIX 48 AF3 LYS B 411 ARG B 420 1 10
HELIX 49 AF4 PRO B 446 THR B 451 5 6
HELIX 50 AF5 GLU B 461 GLU B 480 1 20
HELIX 51 AF6 LYS B 525 VAL B 530 1 6
HELIX 52 AF7 THR B 550 THR B 554 5 5
HELIX 53 AF8 SER B 556 PHE B 563 1 8
HELIX 54 AF9 PHE B 563 GLY B 569 1 7
HELIX 55 AG1 HIS B 572 THR B 574 5 3
HELIX 56 AG2 LEU B 586 ARG B 592 5 7
HELIX 57 AG3 LEU B 593 ARG B 623 1 31
HELIX 58 AG4 ASP B 627 GLY B 655 1 29
HELIX 59 AG5 PRO B 657 ALA B 669 1 13
HELIX 60 AG6 ASN B 670 MSE B 682 1 13
HELIX 61 AG7 PRO B 684 LEU B 689 5 6
HELIX 62 AG8 THR B 693 TYR B 702 1 10
HELIX 63 AG9 LEU B 738 GLY B 775 1 38
HELIX 64 AH1 ASP B 780 LEU B 794 1 15
HELIX 65 AH2 CYS B 799 TYR B 817 1 19
HELIX 66 AH3 THR B 822 GLN B 842 1 21
HELIX 67 AH4 THR C 6 ASP C 21 1 16
HELIX 68 AH5 THR C 29 SER C 39 1 11
HELIX 69 AH6 ALA C 58 THR C 71 1 14
HELIX 70 AH7 ARG C 75 ARG C 87 1 13
HELIX 71 AH8 ASP C 96 ILE C 101 1 6
HELIX 72 AH9 SER C 102 ALA C 104 5 3
HELIX 73 AI1 THR D 6 PHE D 20 1 15
HELIX 74 AI2 GLU D 32 SER D 39 1 8
HELIX 75 AI3 ALA D 58 PHE D 66 1 9
HELIX 76 AI4 LYS D 76 GLU D 83 1 8
HELIX 77 AI5 GLU D 84 ILE D 86 5 3
SHEET 1 AA1 2 ALA A 105 GLU A 109 0
SHEET 2 AA1 2 LYS A 316 LEU A 320 -1 O GLU A 317 N GLY A 108
SHEET 1 AA2 4 VAL A 121 LEU A 124 0
SHEET 2 AA2 4 ARG A 127 GLU A 133 -1 O ILE A 129 N LYS A 122
SHEET 3 AA2 4 THR A 582 SER A 585 1 O ALA A 583 N PRO A 130
SHEET 4 AA2 4 PHE A 576 ASP A 577 -1 N ASP A 577 O THR A 582
SHEET 1 AA3 2 MSE A 291 ARG A 293 0
SHEET 2 AA3 2 THR A 298 PHE A 300 -1 O ASN A 299 N PHE A 292
SHEET 1 AA4 5 LEU A 346 ILE A 349 0
SHEET 2 AA4 5 THR A 353 PHE A 356 -1 O LEU A 355 N ARG A 348
SHEET 3 AA4 5 VAL A 363 VAL A 368 -1 O VAL A 366 N LEU A 354
SHEET 4 AA4 5 ASP A 437 ALA A 445 -1 O TYR A 443 N ALA A 365
SHEET 5 AA4 5 GLN A 403 LYS A 411 -1 N TYR A 408 O VAL A 440
SHEET 1 AA5 2 ILE A 482 VAL A 483 0
SHEET 2 AA5 2 LEU A 547 PRO A 548 -1 O LEU A 547 N VAL A 483
SHEET 1 AA6 2 LEU A 535 ARG A 536 0
SHEET 2 AA6 2 GLY A 539 LEU A 540 -1 O GLY A 539 N ARG A 536
SHEET 1 AA7 2 GLY B 108 GLU B 109 0
SHEET 2 AA7 2 LYS B 316 GLU B 317 -1 O GLU B 317 N GLY B 108
SHEET 1 AA8 4 VAL B 121 LEU B 124 0
SHEET 2 AA8 4 ARG B 127 GLU B 133 -1 O ILE B 129 N LYS B 122
SHEET 3 AA8 4 THR B 582 SER B 585 1 O ALA B 583 N PRO B 130
SHEET 4 AA8 4 PHE B 576 ASP B 577 -1 N ASP B 577 O THR B 582
SHEET 1 AA9 2 MSE B 291 GLU B 294 0
SHEET 2 AA9 2 SER B 297 PHE B 300 -1 O SER B 297 N GLU B 294
SHEET 1 AB1 5 LEU B 346 ILE B 349 0
SHEET 2 AB1 5 THR B 353 PHE B 356 -1 O LEU B 355 N ARG B 348
SHEET 3 AB1 5 VAL B 363 VAL B 368 -1 O VAL B 366 N LEU B 354
SHEET 4 AB1 5 VAL B 440 ALA B 445 -1 O TYR B 441 N LYS B 367
SHEET 5 AB1 5 GLN B 403 TYR B 408 -1 N GLY B 406 O VAL B 442
SHEET 1 AB2 2 ILE B 482 VAL B 483 0
SHEET 2 AB2 2 LEU B 547 PRO B 548 -1 O LEU B 547 N VAL B 483
LINK C LYS A 211 N MSE A 212 1555 1555 1.33
LINK C MSE A 212 N ILE A 213 1555 1555 1.33
LINK C PHE A 237 N MSE A 238 1555 1555 1.33
LINK C MSE A 238 N LEU A 239 1555 1555 1.33
LINK C PRO A 290 N MSE A 291 1555 1555 1.33
LINK C MSE A 291 N PHE A 292 1555 1555 1.33
LINK C GLN A 340 N MSE A 341 1555 1555 1.33
LINK C MSE A 341 N SER A 342 1555 1555 1.33
LINK C GLU A 383 N MSE A 384 1555 1555 1.33
LINK C MSE A 384 N ALA A 385 1555 1555 1.34
LINK C ASP A 624 N MSE A 625 1555 1555 1.33
LINK C VAL A 641 N MSE A 642 1555 1555 1.33
LINK C MSE A 642 N PHE A 643 1555 1555 1.34
LINK C ILE A 652 N MSE A 653 1555 1555 1.33
LINK C MSE A 653 N THR A 654 1555 1555 1.34
LINK C TRP A 681 N MSE A 682 1555 1555 1.33
LINK C MSE A 682 N THR A 683 1555 1555 1.34
LINK C GLN A 695 N MSE A 696 1555 1555 1.33
LINK C MSE A 696 N GLU A 697 1555 1555 1.33
LINK C THR A 755 N MSE A 756 1555 1555 1.33
LINK C MSE A 756 N GLN A 757 1555 1555 1.34
LINK C LYS B 211 N MSE B 212 1555 1555 1.33
LINK C MSE B 212 N ILE B 213 1555 1555 1.33
LINK C PHE B 237 N MSE B 238 1555 1555 1.33
LINK C MSE B 238 N LEU B 239 1555 1555 1.34
LINK C PRO B 290 N MSE B 291 1555 1555 1.33
LINK C MSE B 291 N PHE B 292 1555 1555 1.33
LINK C GLN B 340 N MSE B 341 1555 1555 1.32
LINK C MSE B 341 N SER B 342 1555 1555 1.33
LINK C GLU B 383 N MSE B 384 1555 1555 1.33
LINK C MSE B 384 N ALA B 385 1555 1555 1.34
LINK C ASP B 624 N MSE B 625 1555 1555 1.34
LINK C MSE B 625 N MSE B 626 1555 1555 1.33
LINK C MSE B 626 N ASP B 627 1555 1555 1.33
LINK C VAL B 641 N MSE B 642 1555 1555 1.33
LINK C MSE B 642 N PHE B 643 1555 1555 1.34
LINK C ILE B 652 N MSE B 653 1555 1555 1.33
LINK C MSE B 653 N THR B 654 1555 1555 1.34
LINK C TRP B 681 N MSE B 682 1555 1555 1.33
LINK C MSE B 682 N THR B 683 1555 1555 1.33
LINK C GLN B 695 N MSE B 696 1555 1555 1.33
LINK C MSE B 696 N GLU B 697 1555 1555 1.34
LINK C THR B 755 N MSE B 756 1555 1555 1.33
LINK C MSE B 756 N GLN B 757 1555 1555 1.33
LINK OD1 ASP C 21 CA CA C 201 1555 1555 2.73
LINK OD1 ASP C 23 CA CA C 201 1555 1555 2.34
LINK O THR C 27 CA CA C 201 1555 1555 2.40
LINK OG1 THR C 27 CA CA C 201 1555 1555 2.03
LINK OD1 ASP D 21 CA CA D 201 1555 1555 2.27
LINK OD2 ASP D 21 CA CA D 201 1555 1555 2.94
LINK OD1 ASP D 23 CA CA D 201 1555 1555 2.42
LINK OG1 THR D 27 CA CA D 201 1555 1555 2.45
SITE 1 AC1 2 LYS A 260 PHE A 587
SITE 1 AC2 3 ILE A 163 GLN A 167 LEU A 241
SITE 1 AC3 2 LYS B 260 PHE B 587
SITE 1 AC4 3 ARG B 505 THR B 602 GLU B 605
SITE 1 AC5 4 ASP C 21 ASP C 23 THR C 27 ILE C 28
SITE 1 AC6 6 ASP D 21 ASP D 23 ASP D 25 GLY D 26
SITE 2 AC6 6 THR D 27 ILE D 28
CRYST1 61.060 159.246 135.809 90.00 101.68 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.016377 0.000000 0.003385 0.00000
SCALE2 0.000000 0.006280 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007519 0.00000
(ATOM LINES ARE NOT SHOWN.)
END