HEADER MEMBRANE PROTEIN 02-MAY-15 4ZM1
TITLE SHIGELLA FLEXNERI LIPOPOLYSACCHARIDE O-ANTIGEN CHAIN-LENGTH REGULATOR
TITLE 2 WZZBSF - WILD TYPE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHAIN LENGTH DETERMINANT PROTEIN;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: UNP RESIDUES 54-291;
COMPND 5 SYNONYM: POLYSACCHARIDE ANTIGEN CHAIN REGULATOR;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SHIGELLA FLEXNERI;
SOURCE 3 ORGANISM_TAXID: 623;
SOURCE 4 VARIANT: SEROTYPE Y WZZ::KANR;
SOURCE 5 GENE: WZZB, CLD, ROL, SF2089, S2210;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS LIPOPOLYSACCHARIDE, CHAIN-LENGTH, VIRULENCE, SEROSPECIFICITY,
KEYWDS 2 MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.ERICSSON,C.-W.CHANG,T.LONHIENNE,L.CASEY,F.BENNING,B.KOBE,
AUTHOR 2 E.N.H.TRAN,R.MORONA
REVDAT 4 27-SEP-23 4ZM1 1 REMARK
REVDAT 3 08-JAN-20 4ZM1 1 REMARK
REVDAT 2 27-SEP-17 4ZM1 1 REMARK
REVDAT 1 23-MAR-16 4ZM1 0
JRNL AUTH C.W.CHANG,E.N.TRAN,D.J.ERICSSON,L.W.CASEY,T.LONHIENNE,
JRNL AUTH 2 F.BENNING,R.MORONA,B.KOBE
JRNL TITL STRUCTURAL AND BIOCHEMICAL ANALYSIS OF A SINGLE AMINO-ACID
JRNL TITL 2 MUTANT OF WZZBSF THAT ALTERS LIPOPOLYSACCHARIDE O-ANTIGEN
JRNL TITL 3 CHAIN LENGTH IN SHIGELLA FLEXNERI.
JRNL REF PLOS ONE V. 10 38266 2015
JRNL REFN ESSN 1932-6203
JRNL PMID 26378781
JRNL DOI 10.1371/JOURNAL.PONE.0138266
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.PAPADOPOULOS,R.MORONA
REMARK 1 TITL MUTAGENESIS AND CHEMICAL CROSS-LINKING SUGGEST THAT WZZ
REMARK 1 TITL 2 DIMER STABILITY AND OLIGOMERIZATION AFFECT
REMARK 1 TITL 3 LIPOPOLYSACCHARIDE O-ANTIGEN MODAL CHAIN LENGTH CONTROL.
REMARK 1 REF J. BACTERIOL. V. 192 3385 2010
REMARK 1 REFN ESSN 1098-5530
REMARK 1 PMID 20453100
REMARK 1 DOI 10.1128/JB.01134-09
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.N.TRAN,M.PAPADOPOULOS,R.MORONA
REMARK 1 TITL RELATIONSHIP BETWEEN O-ANTIGEN CHAIN LENGTH AND RESISTANCE
REMARK 1 TITL 2 TO COLICIN E2 IN SHIGELLA FLEXNERI.
REMARK 1 REF MICROBIOLOGY (READING, V. 160 589 2014
REMARK 1 REF 2 ENGL.)
REMARK 1 REFN ESSN 1465-2080
REMARK 1 PMID 24425769
REMARK 1 DOI 10.1099/MIC.0.074955-0
REMARK 1 REFERENCE 3
REMARK 1 AUTH P.NATH,E.N.TRAN,R.MORONA
REMARK 1 TITL MUTATIONAL ANALYSIS OF THE SHIGELLA FLEXNERI O-ANTIGEN
REMARK 1 TITL 2 POLYMERASE WZY: IDENTIFICATION OF WZZ-DEPENDENT WZY MUTANTS.
REMARK 1 REF J. BACTERIOL. V. 197 108 2015
REMARK 1 REFN ESSN 1098-5530
REMARK 1 PMID 25313393
REMARK 1 DOI 10.1128/JB.01885-14
REMARK 1 REFERENCE 4
REMARK 1 AUTH P.NATH,R.MORONA
REMARK 1 TITL MUTATIONAL ANALYSIS OF THE MAJOR PERIPLASMIC LOOPS OF
REMARK 1 TITL 2 SHIGELLA FLEXNERI WZY: IDENTIFICATION OF THE RESIDUES
REMARK 1 TITL 3 AFFECTING O ANTIGEN MODAL CHAIN LENGTH CONTROL, AND
REMARK 1 TITL 4 WZZ-DEPENDENT POLYMERIZATION ACTIVITY.
REMARK 1 REF MICROBIOLOGY (READING, V. 161 774 2015
REMARK 1 REF 2 ENGL.)
REMARK 1 REFN ESSN 1465-2080
REMARK 1 PMID 25627441
REMARK 1 DOI 10.1099/MIC.0.000042
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 28725
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 1430
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 14
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.65
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.26
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2913
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2353
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2767
REMARK 3 BIN R VALUE (WORKING SET) : 0.2344
REMARK 3 BIN FREE R VALUE : 0.2514
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.01
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 146
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5633
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 58
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.88
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.63960
REMARK 3 B22 (A**2) : 2.14400
REMARK 3 B33 (A**2) : 5.49570
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.56480
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.404
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.447
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.248
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.487
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.256
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5724 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 7756 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2774 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 213 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 785 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5724 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 771 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 6635 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.09
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.64
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.40
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|5 - 102 }
REMARK 3 ORIGIN FOR THE GROUP (A): -15.4681 -17.2581 -37.4940
REMARK 3 T TENSOR
REMARK 3 T11: 0.0101 T22: -0.2901
REMARK 3 T33: -0.3442 T12: 0.0241
REMARK 3 T13: -0.0537 T23: -0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 2.2907 L22: 2.0828
REMARK 3 L33: 6.3737 L12: 0.1411
REMARK 3 L13: -1.8907 L23: 1.1990
REMARK 3 S TENSOR
REMARK 3 S11: -0.1009 S12: -0.2179 S13: 0.1417
REMARK 3 S21: 0.2581 S22: 0.2201 S23: 0.0216
REMARK 3 S31: 0.0160 S32: -0.0888 S33: -0.1191
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|103 - 152 }
REMARK 3 ORIGIN FOR THE GROUP (A): -20.9026 1.7641 -8.8689
REMARK 3 T TENSOR
REMARK 3 T11: 0.5042 T22: -0.1781
REMARK 3 T33: -0.1991 T12: -0.1146
REMARK 3 T13: 0.0090 T23: -0.0741
REMARK 3 L TENSOR
REMARK 3 L11: -0.1366 L22: 0.0000
REMARK 3 L33: 9.4642 L12: -0.5285
REMARK 3 L13: 1.0320 L23: 3.2275
REMARK 3 S TENSOR
REMARK 3 S11: 0.0372 S12: 0.0134 S13: 0.0231
REMARK 3 S21: -0.0447 S22: -0.0666 S23: -0.1755
REMARK 3 S31: -0.4434 S32: -0.5737 S33: 0.0294
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { A|153 - 191 }
REMARK 3 ORIGIN FOR THE GROUP (A): -16.4419 16.3080 27.8726
REMARK 3 T TENSOR
REMARK 3 T11: 0.5131 T22: -0.2568
REMARK 3 T33: -0.2597 T12: 0.0670
REMARK 3 T13: -0.2000 T23: -0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 0.3928 L22: 15.2483
REMARK 3 L33: 8.8973 L12: -1.8998
REMARK 3 L13: 4.1374 L23: 0.0228
REMARK 3 S TENSOR
REMARK 3 S11: -0.1792 S12: 0.0131 S13: 0.4820
REMARK 3 S21: 0.4145 S22: -0.1579 S23: -0.1868
REMARK 3 S31: -1.1646 S32: 0.4722 S33: 0.3371
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { A|192 - 232 }
REMARK 3 ORIGIN FOR THE GROUP (A): -12.1978 3.1825 -13.7414
REMARK 3 T TENSOR
REMARK 3 T11: 0.5049 T22: -0.0479
REMARK 3 T33: -0.1133 T12: -0.2276
REMARK 3 T13: 0.0316 T23: -0.2398
REMARK 3 L TENSOR
REMARK 3 L11: 0.5093 L22: 4.8403
REMARK 3 L33: 8.8608 L12: -3.2626
REMARK 3 L13: -3.7857 L23: 6.5773
REMARK 3 S TENSOR
REMARK 3 S11: 0.0800 S12: -0.1502 S13: 0.1645
REMARK 3 S21: -0.0057 S22: 0.3200 S23: -0.4194
REMARK 3 S31: -0.7466 S32: 0.8488 S33: -0.3999
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { A|233 - 239 }
REMARK 3 ORIGIN FOR THE GROUP (A): -10.6907 -24.8866 -54.8640
REMARK 3 T TENSOR
REMARK 3 T11: 0.3625 T22: -0.1386
REMARK 3 T33: -0.2062 T12: -0.0750
REMARK 3 T13: -0.0025 T23: -0.0742
REMARK 3 L TENSOR
REMARK 3 L11: -0.9984 L22: 0.1794
REMARK 3 L33: 5.2584 L12: -0.7402
REMARK 3 L13: 8.6427 L23: -1.4114
REMARK 3 S TENSOR
REMARK 3 S11: -0.0660 S12: 0.2396 S13: -0.7298
REMARK 3 S21: -0.3340 S22: -0.0110 S23: 0.1088
REMARK 3 S31: 0.4146 S32: -0.1140 S33: 0.0769
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: { B|3 - 70 }
REMARK 3 ORIGIN FOR THE GROUP (A): -32.6133 -21.5667 -22.4085
REMARK 3 T TENSOR
REMARK 3 T11: 0.0184 T22: -0.0532
REMARK 3 T33: -0.3432 T12: -0.1126
REMARK 3 T13: -0.0362 T23: -0.0650
REMARK 3 L TENSOR
REMARK 3 L11: 1.6994 L22: 2.3613
REMARK 3 L33: 4.6070 L12: -0.3171
REMARK 3 L13: -1.3039 L23: 0.1244
REMARK 3 S TENSOR
REMARK 3 S11: -0.1698 S12: 0.4170 S13: -0.1723
REMARK 3 S21: -0.1588 S22: 0.2629 S23: -0.1275
REMARK 3 S31: -0.0677 S32: -0.4272 S33: -0.0931
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: { B|71 - 107 }
REMARK 3 ORIGIN FOR THE GROUP (A): -35.7221 -24.0579 -32.3201
REMARK 3 T TENSOR
REMARK 3 T11: 0.0697 T22: 0.2286
REMARK 3 T33: -0.1810 T12: -0.1643
REMARK 3 T13: -0.0670 T23: -0.1498
REMARK 3 L TENSOR
REMARK 3 L11: 2.4508 L22: 1.0316
REMARK 3 L33: 7.2479 L12: 0.2551
REMARK 3 L13: -0.2408 L23: -1.9753
REMARK 3 S TENSOR
REMARK 3 S11: -0.2153 S12: 0.4790 S13: -0.0212
REMARK 3 S21: -0.2135 S22: 0.0072 S23: 0.2898
REMARK 3 S31: 0.3093 S32: -1.4429 S33: 0.2082
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: { B|108 - 151 }
REMARK 3 ORIGIN FOR THE GROUP (A): -28.7348 -11.0176 10.0829
REMARK 3 T TENSOR
REMARK 3 T11: 0.1404 T22: -0.0956
REMARK 3 T33: -0.2512 T12: -0.0468
REMARK 3 T13: -0.0485 T23: -0.0390
REMARK 3 L TENSOR
REMARK 3 L11: 1.5531 L22: 1.9408
REMARK 3 L33: 10.8469 L12: 1.6252
REMARK 3 L13: 3.1752 L23: 5.1946
REMARK 3 S TENSOR
REMARK 3 S11: 0.0448 S12: 0.0108 S13: 0.0542
REMARK 3 S21: -0.0245 S22: -0.1415 S23: -0.0505
REMARK 3 S31: 0.6278 S32: -0.5805 S33: 0.0967
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: { B|152 - 220 }
REMARK 3 ORIGIN FOR THE GROUP (A): -19.9665 2.9294 25.6919
REMARK 3 T TENSOR
REMARK 3 T11: -0.0073 T22: -0.3253
REMARK 3 T33: -0.3042 T12: 0.0451
REMARK 3 T13: -0.0294 T23: -0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 1.8767 L22: 1.5461
REMARK 3 L33: 7.5944 L12: -0.2971
REMARK 3 L13: 1.9624 L23: -0.0196
REMARK 3 S TENSOR
REMARK 3 S11: -0.2773 S12: -0.0528 S13: 0.3290
REMARK 3 S21: -0.0231 S22: -0.0912 S23: 0.0946
REMARK 3 S31: -0.3986 S32: -0.1201 S33: 0.3685
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: { B|221 - 240 }
REMARK 3 ORIGIN FOR THE GROUP (A): -35.4043 -16.9132 -33.2067
REMARK 3 T TENSOR
REMARK 3 T11: 0.1371 T22: 0.2464
REMARK 3 T33: -0.1533 T12: 0.0661
REMARK 3 T13: -0.0317 T23: -0.1023
REMARK 3 L TENSOR
REMARK 3 L11: 2.4411 L22: 0.0000
REMARK 3 L33: 4.4362 L12: 1.4675
REMARK 3 L13: 4.0718 L23: -4.9970
REMARK 3 S TENSOR
REMARK 3 S11: 0.1180 S12: 0.2305 S13: 0.1040
REMARK 3 S21: 0.3672 S22: -0.1315 S23: 0.1650
REMARK 3 S31: -0.4637 S32: -0.6880 S33: 0.0134
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: { C|5 - 99 }
REMARK 3 ORIGIN FOR THE GROUP (A): -28.9310 -36.2385 -10.4870
REMARK 3 T TENSOR
REMARK 3 T11: 0.1953 T22: -0.2471
REMARK 3 T33: -0.3145 T12: -0.2351
REMARK 3 T13: 0.0302 T23: -0.0666
REMARK 3 L TENSOR
REMARK 3 L11: 1.2543 L22: 0.0000
REMARK 3 L33: 10.7323 L12: -0.6083
REMARK 3 L13: 0.6900 L23: 0.4737
REMARK 3 S TENSOR
REMARK 3 S11: -0.3141 S12: 0.0970 S13: -0.2112
REMARK 3 S21: -0.0553 S22: 0.0177 S23: 0.1479
REMARK 3 S31: 0.9095 S32: -0.3560 S33: 0.2965
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: { C|100 - 152 }
REMARK 3 ORIGIN FOR THE GROUP (A): -16.5476 -26.5116 18.3725
REMARK 3 T TENSOR
REMARK 3 T11: 0.2158 T22: -0.2501
REMARK 3 T33: -0.2390 T12: 0.0270
REMARK 3 T13: -0.0150 T23: -0.0419
REMARK 3 L TENSOR
REMARK 3 L11: 2.2654 L22: 3.7140
REMARK 3 L33: 8.5082 L12: 2.7325
REMARK 3 L13: 3.9045 L23: 4.9139
REMARK 3 S TENSOR
REMARK 3 S11: 0.0549 S12: 0.3458 S13: -0.3278
REMARK 3 S21: 0.1076 S22: 0.3001 S23: -0.3170
REMARK 3 S31: 0.8840 S32: 0.4278 S33: -0.3550
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: { C|153 - 201 }
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0726 0.1063 42.8669
REMARK 3 T TENSOR
REMARK 3 T11: 0.1464 T22: -0.1757
REMARK 3 T33: -0.2243 T12: 0.0162
REMARK 3 T13: -0.0612 T23: -0.0326
REMARK 3 L TENSOR
REMARK 3 L11: 5.2659 L22: 5.1436
REMARK 3 L33: 2.0114 L12: 3.0644
REMARK 3 L13: 1.9760 L23: 0.0897
REMARK 3 S TENSOR
REMARK 3 S11: -0.1723 S12: -0.1269 S13: 0.1599
REMARK 3 S21: 0.1306 S22: -0.0042 S23: -0.0888
REMARK 3 S31: -0.4293 S32: 0.0609 S33: 0.1765
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: { C|202 - 222 }
REMARK 3 ORIGIN FOR THE GROUP (A): -23.3939 -20.4815 17.9701
REMARK 3 T TENSOR
REMARK 3 T11: 0.1837 T22: -0.1580
REMARK 3 T33: -0.2843 T12: 0.0583
REMARK 3 T13: -0.0495 T23: -0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 3.9163 L22: 8.3542
REMARK 3 L33: 9.9219 L12: -3.8516
REMARK 3 L13: 1.8277 L23: -0.3200
REMARK 3 S TENSOR
REMARK 3 S11: -0.0906 S12: 0.2524 S13: -0.1674
REMARK 3 S21: -0.3715 S22: -0.0547 S23: 0.6137
REMARK 3 S31: 0.2803 S32: -0.4555 S33: 0.1453
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: { C|223 - 240 }
REMARK 3 ORIGIN FOR THE GROUP (A): -38.8300 -37.8635 -15.0040
REMARK 3 T TENSOR
REMARK 3 T11: 0.0714 T22: 0.1070
REMARK 3 T33: -0.3515 T12: -0.4561
REMARK 3 T13: 0.0833 T23: -0.1215
REMARK 3 L TENSOR
REMARK 3 L11: 6.1758 L22: 2.6851
REMARK 3 L33: 0.4741 L12: 0.1438
REMARK 3 L13: 3.4477 L23: -1.8822
REMARK 3 S TENSOR
REMARK 3 S11: -0.2389 S12: 0.3338 S13: -0.4791
REMARK 3 S21: 0.2260 S22: 0.3575 S23: 0.2572
REMARK 3 S31: 0.5496 S32: -1.2083 S33: -0.1186
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4ZM1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000209409.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS JULY 4, 2012
REMARK 200 DATA SCALING SOFTWARE : XSCALE JULY 4, 2012
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28733
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.420
REMARK 200 RESOLUTION RANGE LOW (A) : 90.630
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.42
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 61.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 1.28200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 2.4.0
REMARK 200 STARTING MODEL: 3B8P
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12.5MG/ML PROTEIN, 15% PEG400, 15% PEG
REMARK 280 8000, 0.1M MGCL, PH 7.7 (0.1M NEWMAN BUFFER CITRIC ACID:HEPES:
REMARK 280 CHES), VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
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 30.65500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 1
REMARK 465 ASN A 2
REMARK 465 ALA A 3
REMARK 465 GLU A 4
REMARK 465 ASP A 240
REMARK 465 SER A 241
REMARK 465 PRO A 242
REMARK 465 LYS A 243
REMARK 465 SER B 1
REMARK 465 ASN B 2
REMARK 465 SER B 241
REMARK 465 PRO B 242
REMARK 465 LYS B 243
REMARK 465 SER C 1
REMARK 465 ASN C 2
REMARK 465 ALA C 3
REMARK 465 GLU C 4
REMARK 465 GLU C 64
REMARK 465 GLU C 65
REMARK 465 PRO C 66
REMARK 465 GLU C 67
REMARK 465 SER C 241
REMARK 465 PRO C 242
REMARK 465 LYS C 243
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 76 -73.73 -43.41
REMARK 500 ASN A 77 36.84 -95.20
REMARK 500 GLN A 168 38.41 -78.13
REMARK 500 GLN A 169 95.54 57.86
REMARK 500 ASP A 172 68.52 -107.22
REMARK 500 GLN B 169 101.34 -165.28
REMARK 500 GLU B 171 -82.47 -93.90
REMARK 500 ASN C 77 1.42 81.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO C 197 O
REMARK 620 2 HOH C 415 O 88.0
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CIT A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ZM5 RELATED DB: PDB
DBREF 4ZM1 A 4 241 UNP P37792 WZZB_SHIFL 54 291
DBREF 4ZM1 B 4 241 UNP P37792 WZZB_SHIFL 54 291
DBREF 4ZM1 C 4 241 UNP P37792 WZZB_SHIFL 54 291
SEQADV 4ZM1 SER A 1 UNP P37792 EXPRESSION TAG
SEQADV 4ZM1 ASN A 2 UNP P37792 EXPRESSION TAG
SEQADV 4ZM1 ALA A 3 UNP P37792 EXPRESSION TAG
SEQADV 4ZM1 PRO A 242 UNP P37792 EXPRESSION TAG
SEQADV 4ZM1 LYS A 243 UNP P37792 EXPRESSION TAG
SEQADV 4ZM1 SER B 1 UNP P37792 EXPRESSION TAG
SEQADV 4ZM1 ASN B 2 UNP P37792 EXPRESSION TAG
SEQADV 4ZM1 ALA B 3 UNP P37792 EXPRESSION TAG
SEQADV 4ZM1 PRO B 242 UNP P37792 EXPRESSION TAG
SEQADV 4ZM1 LYS B 243 UNP P37792 EXPRESSION TAG
SEQADV 4ZM1 SER C 1 UNP P37792 EXPRESSION TAG
SEQADV 4ZM1 ASN C 2 UNP P37792 EXPRESSION TAG
SEQADV 4ZM1 ALA C 3 UNP P37792 EXPRESSION TAG
SEQADV 4ZM1 PRO C 242 UNP P37792 EXPRESSION TAG
SEQADV 4ZM1 LYS C 243 UNP P37792 EXPRESSION TAG
SEQRES 1 A 243 SER ASN ALA GLU LYS TRP THR SER THR ALA ILE ILE THR
SEQRES 2 A 243 GLN PRO ASP VAL GLY GLN ILE ALA GLY TYR ASN ASN ALA
SEQRES 3 A 243 MET ASN VAL ILE TYR GLY GLN ALA ALA PRO LYS VAL SER
SEQRES 4 A 243 ASP LEU GLN GLU THR LEU ILE GLY ARG PHE SER SER ALA
SEQRES 5 A 243 PHE SER ALA LEU ALA GLU THR LEU ASP ASN GLN GLU GLU
SEQRES 6 A 243 PRO GLU LYS LEU THR ILE GLU PRO SER VAL LYS ASN GLN
SEQRES 7 A 243 GLN LEU PRO LEU THR VAL SER TYR VAL GLY GLN THR ALA
SEQRES 8 A 243 GLU GLY ALA GLN MET LYS LEU ALA GLN TYR ILE GLN GLN
SEQRES 9 A 243 VAL ASP ASP LYS VAL ASN GLN GLU LEU GLU LYS ASP LEU
SEQRES 10 A 243 LYS ASP ASN ILE ALA LEU GLY ARG LYS ASN LEU GLN ASP
SEQRES 11 A 243 SER LEU ARG THR GLN GLU VAL VAL ALA GLN GLU GLN LYS
SEQRES 12 A 243 ASP LEU ARG ILE ARG GLN ILE GLN GLU ALA LEU GLN TYR
SEQRES 13 A 243 ALA ASN GLN ALA GLN VAL THR LYS PRO GLN VAL GLN GLN
SEQRES 14 A 243 THR GLU ASP VAL THR GLN ASP THR LEU PHE LEU LEU GLY
SEQRES 15 A 243 SER GLU ALA LEU GLU SER MET ILE LYS HIS GLU ALA THR
SEQRES 16 A 243 ARG PRO LEU VAL PHE SER PRO ASN TYR TYR GLN THR ARG
SEQRES 17 A 243 GLN ASN LEU LEU ASP ILE GLU LYS LEU LYS PHE ASP ASP
SEQRES 18 A 243 LEU ASP ILE HIS ALA TYR ARG TYR VAL MET LYS PRO THR
SEQRES 19 A 243 LEU PRO ILE ARG ARG ASP SER PRO LYS
SEQRES 1 B 243 SER ASN ALA GLU LYS TRP THR SER THR ALA ILE ILE THR
SEQRES 2 B 243 GLN PRO ASP VAL GLY GLN ILE ALA GLY TYR ASN ASN ALA
SEQRES 3 B 243 MET ASN VAL ILE TYR GLY GLN ALA ALA PRO LYS VAL SER
SEQRES 4 B 243 ASP LEU GLN GLU THR LEU ILE GLY ARG PHE SER SER ALA
SEQRES 5 B 243 PHE SER ALA LEU ALA GLU THR LEU ASP ASN GLN GLU GLU
SEQRES 6 B 243 PRO GLU LYS LEU THR ILE GLU PRO SER VAL LYS ASN GLN
SEQRES 7 B 243 GLN LEU PRO LEU THR VAL SER TYR VAL GLY GLN THR ALA
SEQRES 8 B 243 GLU GLY ALA GLN MET LYS LEU ALA GLN TYR ILE GLN GLN
SEQRES 9 B 243 VAL ASP ASP LYS VAL ASN GLN GLU LEU GLU LYS ASP LEU
SEQRES 10 B 243 LYS ASP ASN ILE ALA LEU GLY ARG LYS ASN LEU GLN ASP
SEQRES 11 B 243 SER LEU ARG THR GLN GLU VAL VAL ALA GLN GLU GLN LYS
SEQRES 12 B 243 ASP LEU ARG ILE ARG GLN ILE GLN GLU ALA LEU GLN TYR
SEQRES 13 B 243 ALA ASN GLN ALA GLN VAL THR LYS PRO GLN VAL GLN GLN
SEQRES 14 B 243 THR GLU ASP VAL THR GLN ASP THR LEU PHE LEU LEU GLY
SEQRES 15 B 243 SER GLU ALA LEU GLU SER MET ILE LYS HIS GLU ALA THR
SEQRES 16 B 243 ARG PRO LEU VAL PHE SER PRO ASN TYR TYR GLN THR ARG
SEQRES 17 B 243 GLN ASN LEU LEU ASP ILE GLU LYS LEU LYS PHE ASP ASP
SEQRES 18 B 243 LEU ASP ILE HIS ALA TYR ARG TYR VAL MET LYS PRO THR
SEQRES 19 B 243 LEU PRO ILE ARG ARG ASP SER PRO LYS
SEQRES 1 C 243 SER ASN ALA GLU LYS TRP THR SER THR ALA ILE ILE THR
SEQRES 2 C 243 GLN PRO ASP VAL GLY GLN ILE ALA GLY TYR ASN ASN ALA
SEQRES 3 C 243 MET ASN VAL ILE TYR GLY GLN ALA ALA PRO LYS VAL SER
SEQRES 4 C 243 ASP LEU GLN GLU THR LEU ILE GLY ARG PHE SER SER ALA
SEQRES 5 C 243 PHE SER ALA LEU ALA GLU THR LEU ASP ASN GLN GLU GLU
SEQRES 6 C 243 PRO GLU LYS LEU THR ILE GLU PRO SER VAL LYS ASN GLN
SEQRES 7 C 243 GLN LEU PRO LEU THR VAL SER TYR VAL GLY GLN THR ALA
SEQRES 8 C 243 GLU GLY ALA GLN MET LYS LEU ALA GLN TYR ILE GLN GLN
SEQRES 9 C 243 VAL ASP ASP LYS VAL ASN GLN GLU LEU GLU LYS ASP LEU
SEQRES 10 C 243 LYS ASP ASN ILE ALA LEU GLY ARG LYS ASN LEU GLN ASP
SEQRES 11 C 243 SER LEU ARG THR GLN GLU VAL VAL ALA GLN GLU GLN LYS
SEQRES 12 C 243 ASP LEU ARG ILE ARG GLN ILE GLN GLU ALA LEU GLN TYR
SEQRES 13 C 243 ALA ASN GLN ALA GLN VAL THR LYS PRO GLN VAL GLN GLN
SEQRES 14 C 243 THR GLU ASP VAL THR GLN ASP THR LEU PHE LEU LEU GLY
SEQRES 15 C 243 SER GLU ALA LEU GLU SER MET ILE LYS HIS GLU ALA THR
SEQRES 16 C 243 ARG PRO LEU VAL PHE SER PRO ASN TYR TYR GLN THR ARG
SEQRES 17 C 243 GLN ASN LEU LEU ASP ILE GLU LYS LEU LYS PHE ASP ASP
SEQRES 18 C 243 LEU ASP ILE HIS ALA TYR ARG TYR VAL MET LYS PRO THR
SEQRES 19 C 243 LEU PRO ILE ARG ARG ASP SER PRO LYS
HET CIT A 301 13
HET MG C 301 1
HET MG C 302 1
HETNAM CIT CITRIC ACID
HETNAM MG MAGNESIUM ION
FORMUL 4 CIT C6 H8 O7
FORMUL 5 MG 2(MG 2+)
FORMUL 7 HOH *58(H2 O)
HELIX 1 AA1 ILE A 20 GLY A 32 1 13
HELIX 2 AA2 GLN A 33 ALA A 35 5 3
HELIX 3 AA3 LYS A 37 ASN A 62 1 26
HELIX 4 AA4 THR A 90 ALA A 160 1 71
HELIX 5 AA5 THR A 177 LEU A 180 5 4
HELIX 6 AA6 LEU A 181 ARG A 196 1 16
HELIX 7 AA7 SER A 201 LYS A 216 1 16
HELIX 8 AA8 VAL B 17 GLN B 19 5 3
HELIX 9 AA9 ILE B 20 GLY B 32 1 13
HELIX 10 AB1 GLN B 33 ALA B 35 5 3
HELIX 11 AB2 LYS B 37 ASN B 62 1 26
HELIX 12 AB3 THR B 90 GLN B 161 1 72
HELIX 13 AB4 THR B 177 LEU B 180 5 4
HELIX 14 AB5 LEU B 181 HIS B 192 1 12
HELIX 15 AB6 GLU B 193 ARG B 196 5 4
HELIX 16 AB7 SER B 201 GLU B 215 1 15
HELIX 17 AB8 VAL C 17 GLN C 19 5 3
HELIX 18 AB9 ILE C 20 GLY C 32 1 13
HELIX 19 AC1 GLN C 33 ALA C 35 5 3
HELIX 20 AC2 LYS C 37 ASN C 62 1 26
HELIX 21 AC3 THR C 90 ALA C 160 1 71
HELIX 22 AC4 GLN C 169 VAL C 173 5 5
HELIX 23 AC5 THR C 177 LEU C 181 5 5
HELIX 24 AC6 GLY C 182 HIS C 192 1 11
HELIX 25 AC7 GLU C 193 ARG C 196 5 4
HELIX 26 AC8 SER C 201 LYS C 216 1 16
SHEET 1 AA1 4 LEU A 69 PRO A 73 0
SHEET 2 AA1 4 LEU A 82 GLY A 88 -1 O THR A 83 N GLU A 72
SHEET 3 AA1 4 TRP A 6 THR A 13 -1 N ILE A 12 O LEU A 82
SHEET 4 AA1 4 ARG A 228 MET A 231 -1 O VAL A 230 N ILE A 11
SHEET 1 AA2 4 LEU A 69 PRO A 73 0
SHEET 2 AA2 4 LEU A 82 GLY A 88 -1 O THR A 83 N GLU A 72
SHEET 3 AA2 4 TRP A 6 THR A 13 -1 N ILE A 12 O LEU A 82
SHEET 4 AA2 4 ILE A 237 ARG A 238 -1 O ILE A 237 N THR A 7
SHEET 1 AA3 4 LEU B 69 PRO B 73 0
SHEET 2 AA3 4 LEU B 82 GLY B 88 -1 O THR B 83 N GLU B 72
SHEET 3 AA3 4 TRP B 6 THR B 13 -1 N ILE B 12 O LEU B 82
SHEET 4 AA3 4 ARG B 228 MET B 231 -1 O VAL B 230 N ILE B 11
SHEET 1 AA4 4 LEU C 69 PRO C 73 0
SHEET 2 AA4 4 LEU C 82 GLY C 88 -1 O THR C 83 N GLU C 72
SHEET 3 AA4 4 TRP C 6 THR C 13 -1 N ILE C 12 O LEU C 82
SHEET 4 AA4 4 ARG C 228 MET C 231 -1 O VAL C 230 N ILE C 11
LINK O PRO C 197 MG MG C 302 1555 1555 2.49
LINK MG MG C 302 O HOH C 415 1555 1555 2.58
CISPEP 1 LEU A 80 PRO A 81 0 3.63
CISPEP 2 LEU B 80 PRO B 81 0 1.83
CISPEP 3 LEU C 80 PRO C 81 0 0.50
SITE 1 AC1 4 ASN A 24 ASN A 28 PRO A 36 VAL A 38
SITE 1 AC2 1 THR C 163
SITE 1 AC3 5 LYS C 143 PRO C 197 LEU C 198 HOH C 407
SITE 2 AC3 5 HOH C 415
CRYST1 80.890 61.310 90.860 90.00 94.21 90.00 P 1 21 1 6
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 0.012362 0.000000 0.000910 0.00000
SCALE2 0.000000 0.016311 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011036 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
