HEADER HYDROLASE 30-NOV-15 5F14
TITLE STRUCTURE OF NATIVE HEN EGG-WHITE LYSOZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME C;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 1,4-BETA-N-ACETYLMURAMIDASE C,ALLERGEN GAL D IV;
COMPND 5 EC: 3.2.1.17
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 TISSUE: EGG-WHITE
KEYWDS LYSOZYME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.MCGLONE,J.C.NIX,R.C.PAGE
REVDAT 3 27-SEP-23 5F14 1 REMARK
REVDAT 2 30-MAR-16 5F14 1 JRNL
REVDAT 1 24-FEB-16 5F14 0
JRNL AUTH M.LUCIUS,R.FALATACH,C.MCGLONE,K.MAKAROFF,A.DANIELSON,
JRNL AUTH 2 C.WILLIAMS,J.C.NIX,D.KONKOLEWICZ,R.C.PAGE,J.A.BERBERICH
JRNL TITL INVESTIGATING THE IMPACT OF POLYMER FUNCTIONAL GROUPS ON THE
JRNL TITL 2 STABILITY AND ACTIVITY OF LYSOZYME-POLYMER CONJUGATES.
JRNL REF BIOMACROMOLECULES V. 17 1123 2016
JRNL REFN ESSN 1526-4602
JRNL PMID 26866284
JRNL DOI 10.1021/ACS.BIOMAC.5B01743
REMARK 2
REMARK 2 RESOLUTION. 1.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.73
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 3 NUMBER OF REFLECTIONS : 40309
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 1998
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 55.7300 - 2.7666 0.97 3027 159 0.1497 0.1527
REMARK 3 2 2.7666 - 2.1959 1.00 2938 153 0.1527 0.1766
REMARK 3 3 2.1959 - 1.9183 1.00 2933 153 0.1492 0.1479
REMARK 3 4 1.9183 - 1.7429 1.00 2881 150 0.1629 0.2089
REMARK 3 5 1.7429 - 1.6180 1.00 2878 151 0.1600 0.1983
REMARK 3 6 1.6180 - 1.5226 1.00 2878 150 0.1605 0.1843
REMARK 3 7 1.5226 - 1.4463 1.00 2855 149 0.1687 0.1774
REMARK 3 8 1.4463 - 1.3833 1.00 2837 147 0.1706 0.2228
REMARK 3 9 1.3833 - 1.3301 1.00 2873 150 0.1940 0.2300
REMARK 3 10 1.3301 - 1.2842 1.00 2841 149 0.1956 0.2209
REMARK 3 11 1.2842 - 1.2440 0.98 2777 144 0.2301 0.2318
REMARK 3 12 1.2440 - 1.2085 0.93 2630 135 0.2366 0.2427
REMARK 3 13 1.2085 - 1.1766 0.79 2226 117 0.2403 0.2543
REMARK 3 14 1.1766 - 1.1480 0.61 1737 91 0.3013 0.2753
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) : 0.100
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.950
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 : 0.010 1043
REMARK 3 ANGLE : 1.350 1407
REMARK 3 CHIRALITY : 0.064 147
REMARK 3 PLANARITY : 0.006 184
REMARK 3 DIHEDRAL : 11.677 379
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 14 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.5112 16.4015 65.3667
REMARK 3 T TENSOR
REMARK 3 T11: 0.0903 T22: 0.1030
REMARK 3 T33: 0.1412 T12: -0.0227
REMARK 3 T13: -0.0290 T23: -0.0351
REMARK 3 L TENSOR
REMARK 3 L11: 4.2826 L22: 3.0393
REMARK 3 L33: 5.3233 L12: -3.0138
REMARK 3 L13: -0.1167 L23: 1.3578
REMARK 3 S TENSOR
REMARK 3 S11: -0.0061 S12: 0.2431 S13: -0.2094
REMARK 3 S21: 0.0714 S22: -0.0466 S23: 0.1214
REMARK 3 S31: 0.1998 S32: -0.1671 S33: 0.0704
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 15 THROUGH 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.5173 23.4587 76.5789
REMARK 3 T TENSOR
REMARK 3 T11: 0.0493 T22: 0.1237
REMARK 3 T33: 0.0896 T12: 0.0116
REMARK 3 T13: 0.0188 T23: -0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 5.2091 L22: 7.5280
REMARK 3 L33: 1.7236 L12: 2.5869
REMARK 3 L13: 1.4382 L23: -1.7604
REMARK 3 S TENSOR
REMARK 3 S11: -0.1494 S12: 0.1626 S13: -0.0059
REMARK 3 S21: -0.0909 S22: 0.2195 S23: 0.2336
REMARK 3 S31: -0.0565 S32: -0.1551 S33: 0.0251
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 25 THROUGH 58 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.9590 20.4356 73.1500
REMARK 3 T TENSOR
REMARK 3 T11: 0.0791 T22: 0.0640
REMARK 3 T33: 0.0666 T12: -0.0083
REMARK 3 T13: -0.0066 T23: -0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 2.1670 L22: 1.9150
REMARK 3 L33: 1.0247 L12: -1.6786
REMARK 3 L13: 0.7195 L23: -0.7127
REMARK 3 S TENSOR
REMARK 3 S11: -0.0672 S12: 0.0339 S13: 0.0005
REMARK 3 S21: 0.1162 S22: 0.0100 S23: -0.0143
REMARK 3 S31: -0.0605 S32: 0.0489 S33: 0.0491
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 59 THROUGH 68 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.3726 15.9712 85.3962
REMARK 3 T TENSOR
REMARK 3 T11: 0.1376 T22: 0.1264
REMARK 3 T33: 0.1039 T12: 0.0314
REMARK 3 T13: -0.0080 T23: -0.0123
REMARK 3 L TENSOR
REMARK 3 L11: 3.8325 L22: 5.3726
REMARK 3 L33: 2.9432 L12: -4.2734
REMARK 3 L13: -1.3763 L23: 0.7925
REMARK 3 S TENSOR
REMARK 3 S11: -0.3540 S12: -0.5141 S13: 0.1584
REMARK 3 S21: 0.3393 S22: 0.3340 S23: -0.1482
REMARK 3 S31: -0.1675 S32: 0.0258 S33: -0.0114
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 69 THROUGH 78 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2234 14.1465 88.9135
REMARK 3 T TENSOR
REMARK 3 T11: 0.1780 T22: 0.2544
REMARK 3 T33: 0.0969 T12: 0.0544
REMARK 3 T13: 0.0233 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 5.5473 L22: 0.7494
REMARK 3 L33: 0.3565 L12: -1.9382
REMARK 3 L13: -0.9907 L23: 0.2338
REMARK 3 S TENSOR
REMARK 3 S11: -0.3504 S12: -0.8519 S13: 0.0734
REMARK 3 S21: 0.2395 S22: 0.2522 S23: 0.1318
REMARK 3 S31: -0.1601 S32: 0.0348 S33: 0.0511
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 79 THROUGH 88 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4407 9.6753 75.2307
REMARK 3 T TENSOR
REMARK 3 T11: 0.1215 T22: 0.0623
REMARK 3 T33: 0.1579 T12: -0.0148
REMARK 3 T13: 0.0242 T23: -0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 7.7094 L22: 1.5093
REMARK 3 L33: 4.0469 L12: -3.0644
REMARK 3 L13: 4.1409 L23: -1.3081
REMARK 3 S TENSOR
REMARK 3 S11: 0.0852 S12: 0.0868 S13: -0.3341
REMARK 3 S21: -0.0876 S22: -0.1130 S23: 0.2640
REMARK 3 S31: 0.2567 S32: -0.0596 S33: -0.0029
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 89 THROUGH 100 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.9907 17.6120 81.2758
REMARK 3 T TENSOR
REMARK 3 T11: 0.0842 T22: 0.0809
REMARK 3 T33: 0.1043 T12: -0.0056
REMARK 3 T13: 0.0140 T23: 0.0233
REMARK 3 L TENSOR
REMARK 3 L11: 3.8890 L22: 5.4409
REMARK 3 L33: 7.6228 L12: -1.7234
REMARK 3 L13: -1.2383 L23: 5.9849
REMARK 3 S TENSOR
REMARK 3 S11: -0.0852 S12: -0.1126 S13: -0.1985
REMARK 3 S21: 0.1956 S22: -0.0162 S23: 0.1580
REMARK 3 S31: 0.2124 S32: -0.2457 S33: 0.0932
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 101 THROUGH 108 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.6138 27.9716 82.0033
REMARK 3 T TENSOR
REMARK 3 T11: 0.1110 T22: 0.0779
REMARK 3 T33: 0.0768 T12: 0.0328
REMARK 3 T13: -0.0118 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 7.0233 L22: 4.0416
REMARK 3 L33: 5.4826 L12: 0.4711
REMARK 3 L13: -1.3948 L23: -0.1212
REMARK 3 S TENSOR
REMARK 3 S11: -0.1342 S12: -0.2943 S13: 0.0802
REMARK 3 S21: 0.3833 S22: 0.1014 S23: -0.1179
REMARK 3 S31: 0.0846 S32: 0.2592 S33: 0.0658
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 109 THROUGH 114 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.8912 31.9582 74.1345
REMARK 3 T TENSOR
REMARK 3 T11: 0.0772 T22: 0.1358
REMARK 3 T33: 0.0829 T12: -0.0278
REMARK 3 T13: -0.0091 T23: 0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 5.4927 L22: 3.6484
REMARK 3 L33: 0.7086 L12: -0.6387
REMARK 3 L13: -1.2870 L23: -0.8931
REMARK 3 S TENSOR
REMARK 3 S11: 0.0384 S12: -0.5401 S13: -0.1813
REMARK 3 S21: 0.1253 S22: -0.0624 S23: -0.1812
REMARK 3 S31: -0.2538 S32: 0.3030 S33: 0.0301
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 115 THROUGH 129 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3282 28.4742 64.2420
REMARK 3 T TENSOR
REMARK 3 T11: 0.1038 T22: 0.1595
REMARK 3 T33: 0.1095 T12: -0.0150
REMARK 3 T13: -0.0353 T23: 0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 4.9942 L22: 7.1998
REMARK 3 L33: 5.3191 L12: 4.8847
REMARK 3 L13: 4.6437 L23: 5.8853
REMARK 3 S TENSOR
REMARK 3 S11: -0.0124 S12: -0.0166 S13: -0.0699
REMARK 3 S21: -0.2620 S22: -0.0126 S23: 0.3068
REMARK 3 S31: -0.0915 S32: -0.4094 S33: 0.0742
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 5F14 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215823.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUL-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.4-4.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 4.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CMOS
REMARK 200 DETECTOR MANUFACTURER : RDI CMOS_8M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40396
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.148
REMARK 200 RESOLUTION RANGE LOW (A) : 55.730
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 200 DATA REDUNDANCY : 10.40
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.56100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
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: 1IEE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% (W/V) SODIUM CHLORIDE, 0.1M SODIUM
REMARK 280 ACETATE, PH 4.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 18.64600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.40700
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.40700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.96900
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.40700
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.40700
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 9.32300
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.40700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.40700
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 27.96900
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.40700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.40700
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 9.32300
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 18.64600
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 357 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 361 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 545 LIES ON A SPECIAL POSITION.
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 407 O HOH A 507 1.71
REMARK 500 O HOH A 304 O HOH A 396 1.82
REMARK 500 O HOH A 307 O HOH A 388 1.84
REMARK 500 O HOH A 312 O HOH A 342 1.87
REMARK 500 O HOH A 331 O HOH A 520 1.91
REMARK 500 O HOH A 388 O HOH A 516 1.95
REMARK 500 O LEU A 129 O HOH A 301 2.00
REMARK 500 O HOH A 433 O HOH A 438 2.06
REMARK 500 O HOH A 301 O HOH A 305 2.11
REMARK 500 O HOH A 437 O HOH A 461 2.11
REMARK 500 N ASN A 74 O HOH A 302 2.16
REMARK 500 O HOH A 379 O HOH A 382 2.16
REMARK 500 O HOH A 308 O HOH A 429 2.16
REMARK 500 O HOH A 463 O HOH A 473 2.18
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 O HOH A 552 O HOH A 552 8559 1.43
REMARK 500 O HOH A 448 O HOH A 534 8558 1.95
REMARK 500 O HOH A 308 O HOH A 491 7559 2.06
REMARK 500 O HOH A 301 O HOH A 411 4454 2.17
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 A 553 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A 554 DISTANCE = 6.16 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 NA A 201 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 60 O
REMARK 620 2 CYS A 64 O 88.4
REMARK 620 3 SER A 72 OG 93.5 167.7
REMARK 620 4 ARG A 73 O 95.5 87.3 104.7
REMARK 620 5 HOH A 410 O 99.3 82.0 85.6 161.4
REMARK 620 6 HOH A 433 O 174.3 96.7 81.0 87.1 79.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IEE RELATED DB: PDB
REMARK 900 1IEE CONTAINS THE SAME PROTEIN
REMARK 900 RELATED ID: 5F16 RELATED DB: PDB
DBREF 5F14 A 1 129 UNP P00698 LYSC_CHICK 19 147
SEQRES 1 A 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS
SEQRES 2 A 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY
SEQRES 3 A 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN
SEQRES 4 A 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP
SEQRES 5 A 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN
SEQRES 6 A 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE
SEQRES 7 A 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER
SEQRES 8 A 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY
SEQRES 9 A 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY
SEQRES 10 A 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU
HET NA A 201 1
HET CL A 202 1
HET CL A 203 1
HET CL A 204 1
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
FORMUL 2 NA NA 1+
FORMUL 3 CL 3(CL 1-)
FORMUL 6 HOH *254(H2 O)
HELIX 1 AA1 GLY A 4 HIS A 15 1 12
HELIX 2 AA2 ASN A 19 TYR A 23 5 5
HELIX 3 AA3 SER A 24 ASN A 37 1 14
HELIX 4 AA4 PRO A 79 SER A 85 5 7
HELIX 5 AA5 ILE A 88 SER A 100 1 13
HELIX 6 AA6 ASN A 103 ALA A 107 5 5
HELIX 7 AA7 TRP A 108 CYS A 115 1 8
HELIX 8 AA8 ASP A 119 ARG A 125 5 7
SHEET 1 AA1 3 THR A 43 ARG A 45 0
SHEET 2 AA1 3 THR A 51 TYR A 53 -1 O ASP A 52 N ASN A 44
SHEET 3 AA1 3 ILE A 58 ASN A 59 -1 O ILE A 58 N TYR A 53
SSBOND 1 CYS A 6 CYS A 127 1555 1555 2.03
SSBOND 2 CYS A 30 CYS A 115 1555 1555 2.06
SSBOND 3 CYS A 64 CYS A 80 1555 1555 2.05
SSBOND 4 CYS A 76 CYS A 94 1555 1555 2.03
LINK O SER A 60 NA NA A 201 1555 1555 2.23
LINK O CYS A 64 NA NA A 201 1555 1555 2.63
LINK OG SER A 72 NA NA A 201 1555 1555 2.38
LINK O ARG A 73 NA NA A 201 1555 1555 2.47
LINK NA NA A 201 O HOH A 410 1555 1555 2.33
LINK NA NA A 201 O HOH A 433 1555 1555 2.25
SITE 1 AC1 6 SER A 60 CYS A 64 SER A 72 ARG A 73
SITE 2 AC1 6 HOH A 410 HOH A 433
SITE 1 AC2 3 TYR A 23 ASN A 113 HOH A 543
SITE 1 AC3 3 GLY A 67 ARG A 68 THR A 69
SITE 1 AC4 2 ILE A 88 HOH A 490
CRYST1 78.814 78.814 37.292 90.00 90.00 90.00 P 43 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012688 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012688 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026815 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
