HEADER IMMUNE SYSTEM 22-OCT-14 4RMW
TITLE CRYSTAL STRUCTURE OF THE D76A BETA-2 MICROGLOBULIN MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 21-119;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: B2M, CDABP0092, HDCMA22P, NM_004048;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS IMMUNOGLOBIN, BETA-SANDWITCH, AMYLOIDOSIS, PATHOLOGIC MUTATION,
KEYWDS 2 GENETIC DISEASE, MHC CLASS I, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR M.DE ROSA,M.BOLOGNESI,S.RICAGNO
REVDAT 3 20-SEP-23 4RMW 1 REMARK SEQADV
REVDAT 2 27-JUN-18 4RMW 1 JRNL
REVDAT 1 18-NOV-15 4RMW 0
JRNL AUTH T.LE MARCHAND,M.DE ROSA,N.SALVI,B.M.SALA,L.B.ANDREAS,
JRNL AUTH 2 E.BARBET-MASSIN,P.SORMANNI,A.BARBIROLI,R.PORCARI,
JRNL AUTH 3 C.SOUSA MOTA,D.DE SANCTIS,M.BOLOGNESI,L.EMSLEY,V.BELLOTTI,
JRNL AUTH 4 M.BLACKLEDGE,C.CAMILLONI,G.PINTACUDA,S.RICAGNO
JRNL TITL CONFORMATIONAL DYNAMICS IN CRYSTALS REVEAL THE MOLECULAR
JRNL TITL 2 BASES FOR D76N BETA-2 MICROGLOBULIN AGGREGATION PROPENSITY.
JRNL REF NAT COMMUN V. 9 1658 2018
JRNL REFN ESSN 2041-1723
JRNL PMID 29695721
JRNL DOI 10.1038/S41467-018-04078-Y
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.59
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 19920
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1992
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 38.6079 - 3.3737 0.99 1344 149 0.1615 0.1954
REMARK 3 2 3.3737 - 2.6780 0.99 1294 145 0.1745 0.2092
REMARK 3 3 2.6780 - 2.3395 1.00 1288 142 0.1783 0.1956
REMARK 3 4 2.3395 - 2.1257 1.00 1290 144 0.1667 0.1974
REMARK 3 5 2.1257 - 1.9733 1.00 1250 138 0.1685 0.2223
REMARK 3 6 1.9733 - 1.8570 1.00 1306 146 0.1705 0.1863
REMARK 3 7 1.8570 - 1.7640 1.00 1266 141 0.1783 0.2070
REMARK 3 8 1.7640 - 1.6872 1.00 1268 140 0.1817 0.2250
REMARK 3 9 1.6872 - 1.6222 1.00 1265 141 0.2019 0.2478
REMARK 3 10 1.6222 - 1.5663 1.00 1286 143 0.1990 0.2458
REMARK 3 11 1.5663 - 1.5173 1.00 1258 140 0.2100 0.2329
REMARK 3 12 1.5173 - 1.4739 1.00 1265 140 0.2194 0.2441
REMARK 3 13 1.4739 - 1.4351 1.00 1266 141 0.2488 0.2869
REMARK 3 14 1.4351 - 1.4000 1.00 1282 142 0.2622 0.3138
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.680
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 : 0.020 1003
REMARK 3 ANGLE : 1.948 1374
REMARK 3 CHIRALITY : 0.112 142
REMARK 3 PLANARITY : 0.011 182
REMARK 3 DIHEDRAL : 15.028 390
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 12 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.6379 -20.5590 -19.5847
REMARK 3 T TENSOR
REMARK 3 T11: 0.0772 T22: 0.0571
REMARK 3 T33: 0.0992 T12: -0.0041
REMARK 3 T13: 0.0175 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 7.6752 L22: 1.6527
REMARK 3 L33: 5.2840 L12: 3.2842
REMARK 3 L13: 6.2642 L23: 2.8680
REMARK 3 S TENSOR
REMARK 3 S11: 0.0352 S12: 0.1139 S13: -0.0929
REMARK 3 S21: -0.0357 S22: 0.0599 S23: -0.0325
REMARK 3 S31: 0.0227 S32: 0.0787 S33: -0.1823
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 13 THROUGH 20 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.9963 -4.9824 -12.7827
REMARK 3 T TENSOR
REMARK 3 T11: 0.3458 T22: 0.2561
REMARK 3 T33: 0.3118 T12: -0.1092
REMARK 3 T13: 0.1178 T23: -0.1244
REMARK 3 L TENSOR
REMARK 3 L11: 5.8509 L22: 7.4525
REMARK 3 L33: 0.1235 L12: -2.1503
REMARK 3 L13: 0.5932 L23: 0.4282
REMARK 3 S TENSOR
REMARK 3 S11: 0.3631 S12: -0.8879 S13: 1.1574
REMARK 3 S21: 0.4540 S22: -0.0145 S23: -0.3998
REMARK 3 S31: -1.2318 S32: 0.5807 S33: -0.1880
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 21 THROUGH 41 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0275 -13.6877 -15.2306
REMARK 3 T TENSOR
REMARK 3 T11: 0.0786 T22: 0.0392
REMARK 3 T33: 0.0805 T12: -0.0157
REMARK 3 T13: 0.0277 T23: 0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 3.7910 L22: 1.7276
REMARK 3 L33: 3.8479 L12: 1.1594
REMARK 3 L13: 2.8039 L23: 1.5033
REMARK 3 S TENSOR
REMARK 3 S11: 0.0113 S12: -0.0576 S13: 0.0943
REMARK 3 S21: 0.0496 S22: 0.0139 S23: -0.0135
REMARK 3 S31: -0.1080 S32: 0.0872 S33: -0.0148
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 42 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5150 -7.2915 -11.8626
REMARK 3 T TENSOR
REMARK 3 T11: 0.3496 T22: 0.2154
REMARK 3 T33: 0.2719 T12: 0.0250
REMARK 3 T13: 0.0011 T23: -0.0635
REMARK 3 L TENSOR
REMARK 3 L11: 1.5298 L22: 0.7407
REMARK 3 L33: 4.9266 L12: -0.0073
REMARK 3 L13: 1.1030 L23: -1.8550
REMARK 3 S TENSOR
REMARK 3 S11: -0.2158 S12: -0.3777 S13: 0.4779
REMARK 3 S21: 0.3746 S22: -0.2220 S23: -0.0630
REMARK 3 S31: -1.2924 S32: -0.4784 S33: 0.2794
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 57 THROUGH 61 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.7261 -17.2336 -32.7321
REMARK 3 T TENSOR
REMARK 3 T11: 0.2431 T22: 0.2893
REMARK 3 T33: 0.0859 T12: 0.0211
REMARK 3 T13: 0.0048 T23: -0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 5.5047 L22: 5.2726
REMARK 3 L33: 7.3503 L12: 4.0948
REMARK 3 L13: 6.3476 L23: 4.9922
REMARK 3 S TENSOR
REMARK 3 S11: 0.3342 S12: 0.5780 S13: -0.2313
REMARK 3 S21: -0.4166 S22: -0.1845 S23: -0.0160
REMARK 3 S31: 0.8349 S32: -0.5387 S33: -0.1107
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 62 THROUGH 70 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9361 -9.8370 -16.0189
REMARK 3 T TENSOR
REMARK 3 T11: 0.1595 T22: 0.1079
REMARK 3 T33: 0.1587 T12: -0.0298
REMARK 3 T13: 0.0196 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 4.4001 L22: 5.9938
REMARK 3 L33: 7.5518 L12: 2.1189
REMARK 3 L13: 3.8663 L23: 4.4198
REMARK 3 S TENSOR
REMARK 3 S11: 0.0862 S12: -0.0508 S13: 0.0991
REMARK 3 S21: 0.4730 S22: 0.0838 S23: -0.3051
REMARK 3 S31: -0.1265 S32: 0.3524 S33: -0.1935
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 71 THROUGH 77 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2690 -13.9968 1.7336
REMARK 3 T TENSOR
REMARK 3 T11: 0.5860 T22: 0.5292
REMARK 3 T33: 0.3621 T12: -0.1433
REMARK 3 T13: -0.2103 T23: -0.0251
REMARK 3 L TENSOR
REMARK 3 L11: 2.0730 L22: 0.5577
REMARK 3 L33: 2.6282 L12: -1.0659
REMARK 3 L13: -2.3288 L23: 1.1985
REMARK 3 S TENSOR
REMARK 3 S11: 0.1446 S12: -0.5371 S13: -0.0414
REMARK 3 S21: 0.7929 S22: 0.2748 S23: -0.9101
REMARK 3 S31: 0.2377 S32: 1.3868 S33: -0.3414
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 78 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.3307 -18.6441 -11.6458
REMARK 3 T TENSOR
REMARK 3 T11: 0.1003 T22: 0.1267
REMARK 3 T33: 0.0802 T12: -0.0531
REMARK 3 T13: 0.0151 T23: 0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 6.3071 L22: 0.7314
REMARK 3 L33: 1.1159 L12: 1.7211
REMARK 3 L13: 1.8936 L23: 0.1049
REMARK 3 S TENSOR
REMARK 3 S11: 0.3309 S12: -0.7683 S13: -0.0505
REMARK 3 S21: 0.2771 S22: -0.3483 S23: 0.0157
REMARK 3 S31: 0.3347 S32: -0.3737 S33: 0.0482
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 91 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.2370 -20.0694 -6.2060
REMARK 3 T TENSOR
REMARK 3 T11: 0.1344 T22: 0.1149
REMARK 3 T33: 0.1742 T12: -0.0041
REMARK 3 T13: -0.0253 T23: 0.0508
REMARK 3 L TENSOR
REMARK 3 L11: 7.6141 L22: 3.3306
REMARK 3 L33: 3.7925 L12: 1.0782
REMARK 3 L13: 0.0685 L23: -1.5306
REMARK 3 S TENSOR
REMARK 3 S11: 0.2723 S12: -0.5299 S13: -0.9053
REMARK 3 S21: -0.0302 S22: -0.2018 S23: -0.2940
REMARK 3 S31: 0.2250 S32: 0.2736 S33: -0.0561
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 4RMW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1000087543.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-APR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19921
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 44.840
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.48200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
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 2YXF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 21% PEG4000, 15% GLYCEROL, 0.2 M
REMARK 280 AMMONIUM ACETATE, 0.1 M SODIUM ACETATE, PH 5.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 38.81200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 14.49600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 38.81200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 14.49600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 58 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 270 O HOH A 314 2.05
REMARK 500 ND2 ASN A 83 O HOH A 257 2.06
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 SER A 11 OG SER A 57 2554 2.05
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 CYS A 25 CB CYS A 25 SG -0.131
REMARK 500 CYS A 80 CB CYS A 80 SG 0.171
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 CYS A 80 CA - CB - SG ANGL. DEV. = 7.9 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 SER A 57 -79.07 -121.69
REMARK 500 SER A 61 116.68 -165.27
REMARK 500 THR A 73 155.86 67.11
REMARK 500 LYS A 75 -71.17 -81.27
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 PGE A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 102
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2YXF RELATED DB: PDB
REMARK 900 RELATED ID: 4FXL RELATED DB: PDB
REMARK 900 RELATED ID: 4RMQ RELATED DB: PDB
REMARK 900 RELATED ID: 4RMR RELATED DB: PDB
REMARK 900 RELATED ID: 4RMS RELATED DB: PDB
REMARK 900 RELATED ID: 4RMT RELATED DB: PDB
REMARK 900 RELATED ID: 4RMU RELATED DB: PDB
REMARK 900 RELATED ID: 4RMV RELATED DB: PDB
DBREF 4RMW A 1 99 UNP P61769 B2MG_HUMAN 21 119
SEQADV 4RMW MET A 0 UNP P61769 INITIATING METHIONINE
SEQADV 4RMW ALA A 76 UNP P61769 ASP 96 ENGINEERED MUTATION
SEQRES 1 A 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 A 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 A 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 A 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 A 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 A 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ALA GLU
SEQRES 7 A 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 A 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
HET PGE A 101 10
HET ACT A 102 4
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM ACT ACETATE ION
FORMUL 2 PGE C6 H14 O4
FORMUL 3 ACT C2 H3 O2 1-
FORMUL 4 HOH *115(H2 O)
HELIX 1 1 PRO A 14 GLY A 18 5 5
SHEET 1 A 4 LYS A 6 ARG A 12 0
SHEET 2 A 4 ASN A 21 PHE A 30 -1 O ASN A 24 N TYR A 10
SHEET 3 A 4 PHE A 62 PHE A 70 -1 O LEU A 64 N VAL A 27
SHEET 4 A 4 HIS A 51 PHE A 56 -1 N ASP A 53 O LEU A 65
SHEET 1 B 4 GLU A 44 ARG A 45 0
SHEET 2 B 4 GLU A 36 LYS A 41 -1 N LYS A 41 O GLU A 44
SHEET 3 B 4 TYR A 78 ASN A 83 -1 O ARG A 81 N ASP A 38
SHEET 4 B 4 LYS A 91 LYS A 94 -1 O VAL A 93 N CYS A 80
SSBOND 1 CYS A 25 CYS A 80 1555 1555 2.03
CISPEP 1 HIS A 31 PRO A 32 0 -6.86
SITE 1 AC1 3 TYR A 10 TYR A 26 SER A 28
SITE 1 AC2 9 LYS A 41 THR A 71 PRO A 72 THR A 73
SITE 2 AC2 9 TYR A 78 ASP A 96 ARG A 97 ASP A 98
SITE 3 AC2 9 HOH A 252
CRYST1 77.624 28.992 56.293 90.00 127.20 90.00 C 1 2 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 0.012883 0.000000 0.009777 0.00000
SCALE2 0.000000 0.034492 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022301 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
