HEADER ANTIMICROBIAL PROTEIN 05-JUN-18 6DMM
TITLE CRYSTAL STRUCTURE OF THE G23A MUTANT OF HUMAN ALPHA DEFENSIN HNP4.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUTROPHIL DEFENSIN 4;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 SYNONYM: DEFENSIN,ALPHA 4,HNP-4,HP-4;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606
KEYWDS HUMAN ALPHA-DEFENSIN, ANTIMICROBIAL PEPTIDE, ANTIMICROBIAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR N.GOHAIN,W.D.TOLBERT,M.PAZGIER
REVDAT 3 11-OCT-23 6DMM 1 JRNL
REVDAT 2 20-FEB-19 6DMM 1 JRNL
REVDAT 1 30-JAN-19 6DMM 0
JRNL AUTH H.HU,B.DI,W.D.TOLBERT,N.GOHAIN,W.YUAN,P.GAO,B.MA,Q.HE,
JRNL AUTH 2 M.PAZGIER,L.ZHAO,W.LU
JRNL TITL SYSTEMATIC MUTATIONAL ANALYSIS OF HUMAN NEUTROPHIL
JRNL TITL 2 ALPHA-DEFENSIN HNP4.
JRNL REF BIOCHIM BIOPHYS ACTA V.1861 835 2019
JRNL REF 2 BIOMEMBR
JRNL REFN ESSN 1879-2642
JRNL PMID 30658057
JRNL DOI 10.1016/J.BBAMEM.2019.01.007
REMARK 2
REMARK 2 RESOLUTION. 1.67 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
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) : 1.67
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.57
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.500
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 40053
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 2011
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 34.5741 - 4.0228 0.97 2869 149 0.2150 0.2352
REMARK 3 2 4.0228 - 3.1937 0.99 2761 151 0.1821 0.2173
REMARK 3 3 3.1937 - 2.7902 0.99 2733 163 0.2010 0.2314
REMARK 3 4 2.7902 - 2.5352 0.99 2724 150 0.2218 0.2994
REMARK 3 5 2.5352 - 2.3535 0.99 2713 143 0.2195 0.2801
REMARK 3 6 2.3535 - 2.2148 0.99 2728 133 0.2138 0.2361
REMARK 3 7 2.2148 - 2.1039 0.99 2715 133 0.2069 0.2485
REMARK 3 8 2.1039 - 2.0123 0.99 2692 154 0.2208 0.2327
REMARK 3 9 2.0123 - 1.9349 0.99 2726 118 0.2425 0.2752
REMARK 3 10 1.9349 - 1.8681 0.99 2677 144 0.2407 0.2978
REMARK 3 11 1.8681 - 1.8097 1.00 2671 130 0.2536 0.3136
REMARK 3 12 1.8097 - 1.7580 1.00 2716 162 0.2850 0.3065
REMARK 3 13 1.7580 - 1.7117 1.00 2717 139 0.3175 0.3479
REMARK 3 14 1.7117 - 1.6699 0.97 2600 142 0.3558 0.3759
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.570
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 : 0.011 3148
REMARK 3 ANGLE : 1.320 4271
REMARK 3 CHIRALITY : 0.062 502
REMARK 3 PLANARITY : 0.006 498
REMARK 3 DIHEDRAL : 10.779 1971
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN 'A' AND RESID 1 THROUGH 33)
REMARK 3 ORIGIN FOR THE GROUP (A): -11.2776 6.7076 26.0965
REMARK 3 T TENSOR
REMARK 3 T11: 0.1601 T22: 0.2009
REMARK 3 T33: 0.2137 T12: 0.0016
REMARK 3 T13: -0.0795 T23: 0.0264
REMARK 3 L TENSOR
REMARK 3 L11: 4.3274 L22: 4.8235
REMARK 3 L33: 4.0973 L12: -0.7998
REMARK 3 L13: -2.6250 L23: 0.2213
REMARK 3 S TENSOR
REMARK 3 S11: 0.1207 S12: 0.2790 S13: -0.1557
REMARK 3 S21: -0.3619 S22: -0.0343 S23: 0.4994
REMARK 3 S31: -0.0971 S32: -0.1613 S33: -0.0854
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN 'B' AND RESID 1 THROUGH 31)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.4579 -6.8418 31.6654
REMARK 3 T TENSOR
REMARK 3 T11: 0.1797 T22: 0.2400
REMARK 3 T33: 0.2350 T12: 0.0066
REMARK 3 T13: -0.0674 T23: 0.0317
REMARK 3 L TENSOR
REMARK 3 L11: 1.9610 L22: 7.1155
REMARK 3 L33: 2.1441 L12: 2.0695
REMARK 3 L13: -0.3133 L23: 2.8641
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0056 S13: -0.1090
REMARK 3 S21: 0.0732 S22: -0.0541 S23: -0.1173
REMARK 3 S31: 0.0644 S32: 0.0430 S33: 0.0089
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN 'C' AND RESID 1 THROUGH 33)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.2099 -6.8535 5.6059
REMARK 3 T TENSOR
REMARK 3 T11: 0.1112 T22: 0.1986
REMARK 3 T33: 0.2912 T12: 0.0148
REMARK 3 T13: 0.0307 T23: 0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 2.1355 L22: 6.8637
REMARK 3 L33: 6.0923 L12: -1.5717
REMARK 3 L13: 3.3227 L23: -0.4499
REMARK 3 S TENSOR
REMARK 3 S11: -0.0404 S12: 0.0134 S13: 0.0366
REMARK 3 S21: 0.1213 S22: 0.0768 S23: -0.3240
REMARK 3 S31: 0.0366 S32: 0.1398 S33: 0.0162
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN 'D' AND RESID 1 THROUGH 31)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.9012 6.4235 11.4920
REMARK 3 T TENSOR
REMARK 3 T11: 0.2907 T22: 0.2512
REMARK 3 T33: 0.2700 T12: 0.0987
REMARK 3 T13: 0.0083 T23: 0.0363
REMARK 3 L TENSOR
REMARK 3 L11: 4.5831 L22: 4.2337
REMARK 3 L33: 5.1720 L12: 3.9354
REMARK 3 L13: -1.5537 L23: 0.2407
REMARK 3 S TENSOR
REMARK 3 S11: -0.2584 S12: 0.0441 S13: -0.0676
REMARK 3 S21: -0.3580 S22: 0.1754 S23: 0.1492
REMARK 3 S31: -0.3570 S32: -0.2343 S33: 0.0942
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN 'E' AND RESID 1 THROUGH 33)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.4665 -7.0289 46.2722
REMARK 3 T TENSOR
REMARK 3 T11: 0.1735 T22: 0.1553
REMARK 3 T33: 0.1162 T12: -0.0010
REMARK 3 T13: 0.0105 T23: 0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 7.7224 L22: 4.8752
REMARK 3 L33: 6.1034 L12: 0.0552
REMARK 3 L13: 3.8205 L23: -0.2116
REMARK 3 S TENSOR
REMARK 3 S11: -0.0764 S12: 0.1040 S13: 0.0965
REMARK 3 S21: -0.1983 S22: 0.0729 S23: -0.0961
REMARK 3 S31: 0.0361 S32: 0.0369 S33: 0.0288
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN 'F' AND RESID 1 THROUGH 31)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.8038 6.3204 52.0630
REMARK 3 T TENSOR
REMARK 3 T11: 0.2754 T22: 0.2183
REMARK 3 T33: 0.2341 T12: 0.0276
REMARK 3 T13: -0.0433 T23: -0.0461
REMARK 3 L TENSOR
REMARK 3 L11: 8.1438 L22: 6.6260
REMARK 3 L33: 6.1489 L12: 4.2166
REMARK 3 L13: -2.8166 L23: -2.8621
REMARK 3 S TENSOR
REMARK 3 S11: 0.1045 S12: -0.3519 S13: 0.0706
REMARK 3 S21: 0.0261 S22: -0.0691 S23: 0.0888
REMARK 3 S31: -0.1091 S32: -0.0389 S33: -0.0024
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN 'G' AND RESID 1 THROUGH 31)
REMARK 3 ORIGIN FOR THE GROUP (A): -31.4710 6.6514 55.6365
REMARK 3 T TENSOR
REMARK 3 T11: 0.4124 T22: 0.2259
REMARK 3 T33: 0.1889 T12: -0.0503
REMARK 3 T13: 0.0767 T23: -0.0381
REMARK 3 L TENSOR
REMARK 3 L11: 5.4618 L22: 7.6844
REMARK 3 L33: 5.6621 L12: 1.9397
REMARK 3 L13: -0.1827 L23: 1.5756
REMARK 3 S TENSOR
REMARK 3 S11: -0.1458 S12: 0.3333 S13: -0.0528
REMARK 3 S21: -1.1586 S22: 0.3322 S23: -0.6025
REMARK 3 S31: -1.0500 S32: 0.2200 S33: -0.1866
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN 'H' AND RESID 1 THROUGH 32)
REMARK 3 ORIGIN FOR THE GROUP (A): -27.1765 -6.9636 51.8608
REMARK 3 T TENSOR
REMARK 3 T11: 0.5113 T22: 0.2283
REMARK 3 T33: 0.1727 T12: -0.0006
REMARK 3 T13: 0.0070 T23: 0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 6.0270 L22: 3.1001
REMARK 3 L33: 6.7554 L12: -0.2266
REMARK 3 L13: -0.2531 L23: -1.5614
REMARK 3 S TENSOR
REMARK 3 S11: -0.1368 S12: -0.4518 S13: -0.4383
REMARK 3 S21: 0.7407 S22: 0.1786 S23: 0.1502
REMARK 3 S31: 0.8757 S32: -0.0142 S33: -0.0399
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN 'I' AND RESID 1 THROUGH 32)
REMARK 3 ORIGIN FOR THE GROUP (A): -30.9531 7.0033 14.0784
REMARK 3 T TENSOR
REMARK 3 T11: 0.2662 T22: 0.2368
REMARK 3 T33: 0.1922 T12: -0.0196
REMARK 3 T13: 0.0716 T23: -0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 7.2459 L22: 9.7343
REMARK 3 L33: 6.7387 L12: 2.2853
REMARK 3 L13: 2.1191 L23: 1.8916
REMARK 3 S TENSOR
REMARK 3 S11: -0.1966 S12: 0.5568 S13: -0.2688
REMARK 3 S21: -0.9211 S22: 0.4281 S23: -0.7476
REMARK 3 S31: -0.8540 S32: 0.5197 S33: -0.2201
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN 'J' AND RESID 1 THROUGH 33)
REMARK 3 ORIGIN FOR THE GROUP (A): -26.7854 -7.1270 10.5622
REMARK 3 T TENSOR
REMARK 3 T11: 0.1471 T22: 0.2686
REMARK 3 T33: 0.1526 T12: 0.0298
REMARK 3 T13: 0.0103 T23: 0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 6.7850 L22: 9.4266
REMARK 3 L33: 7.5316 L12: -1.6619
REMARK 3 L13: -0.1399 L23: -0.1898
REMARK 3 S TENSOR
REMARK 3 S11: -0.0934 S12: -0.4278 S13: -0.3818
REMARK 3 S21: 0.4617 S22: 0.2409 S23: -0.0652
REMARK 3 S31: 0.3308 S32: -0.1225 S33: -0.1325
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN 'K' AND RESID 1 THROUGH 32)
REMARK 3 ORIGIN FOR THE GROUP (A): -30.8392 -7.4907 34.6360
REMARK 3 T TENSOR
REMARK 3 T11: 0.1382 T22: 0.1673
REMARK 3 T33: 0.1006 T12: -0.0047
REMARK 3 T13: -0.0037 T23: 0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 8.9732 L22: 9.4749
REMARK 3 L33: 4.4580 L12: 3.2308
REMARK 3 L13: 0.8919 L23: -0.1767
REMARK 3 S TENSOR
REMARK 3 S11: 0.1396 S12: 0.1513 S13: -0.0037
REMARK 3 S21: 0.3349 S22: 0.0740 S23: 0.4388
REMARK 3 S31: 0.2685 S32: -0.1676 S33: -0.1460
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN 'L' AND RESID 1 THROUGH 32)
REMARK 3 ORIGIN FOR THE GROUP (A): -34.7117 6.6011 31.0370
REMARK 3 T TENSOR
REMARK 3 T11: 0.1755 T22: 0.2336
REMARK 3 T33: 0.1965 T12: 0.0578
REMARK 3 T13: -0.0114 T23: 0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 5.8444 L22: 8.1666
REMARK 3 L33: 5.7449 L12: -1.6649
REMARK 3 L13: -0.2345 L23: 1.0640
REMARK 3 S TENSOR
REMARK 3 S11: -0.1688 S12: -0.4169 S13: 0.5516
REMARK 3 S21: 0.6689 S22: 0.3296 S23: -0.1563
REMARK 3 S31: -0.3904 S32: -0.0880 S33: -0.1406
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 6DMM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-18.
REMARK 100 THE DEPOSITION ID IS D_1000234911.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JAN-16
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 : SSRL
REMARK 200 BEAMLINE : BL14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40384
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.670
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.67
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.96600
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1ZMM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% ISOPROPANOL 10% PEG 1500 200 MM
REMARK 280 LITHIUM SULFATE 100 MM SODIUM ACETATE PH 5.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 20.81450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 62.03200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.94700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.03200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.81450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.94700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L
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 ARG B 32
REMARK 465 VAL B 33
REMARK 465 ARG D 32
REMARK 465 VAL D 33
REMARK 465 ARG F 32
REMARK 465 VAL F 33
REMARK 465 ARG G 32
REMARK 465 VAL G 33
REMARK 465 VAL H 33
REMARK 465 VAL I 33
REMARK 465 VAL K 33
REMARK 465 VAL L 33
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 LEU F 6 O HOH F 201 2.03
REMARK 500 OD1 ASN H 18 O HOH H 201 2.07
REMARK 500 OD1 ASN D 18 O HOH D 201 2.08
REMARK 500 O HOH B 228 O HOH F 217 2.08
REMARK 500 O HOH B 212 O HOH B 214 2.08
REMARK 500 O HOH L 216 O HOH L 223 2.11
REMARK 500 O LEU C 6 O HOH C 101 2.18
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 LEU D 14 CB - CG - CD2 ANGL. DEV. = -11.8 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 VAL A 7 -57.98 79.76
REMARK 500 VAL B 7 -62.08 -139.08
REMARK 500 VAL C 7 -49.45 -133.89
REMARK 500 VAL D 7 -56.88 -137.74
REMARK 500 VAL E 7 -63.05 68.47
REMARK 500 VAL G 7 -66.29 -135.54
REMARK 500 VAL H 7 -43.27 73.86
REMARK 500 VAL I 7 -66.09 -136.19
REMARK 500 VAL J 7 -44.82 74.76
REMARK 500 ARG J 32 35.20 142.61
REMARK 500 VAL K 7 -67.23 -134.65
REMARK 500 VAL L 7 -43.77 76.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG L 11 0.13 SIDE CHAIN
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 SO4 A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 I 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 J 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 J 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 J 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD J 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 K 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 L 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 L 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 L 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 L 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 L 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 L 106
DBREF 6DMM A 1 33 UNP P12838 DEF4_HUMAN 64 96
DBREF 6DMM B 1 33 UNP P12838 DEF4_HUMAN 64 96
DBREF 6DMM C 1 33 UNP P12838 DEF4_HUMAN 64 96
DBREF 6DMM D 1 33 UNP P12838 DEF4_HUMAN 64 96
DBREF 6DMM E 1 33 UNP P12838 DEF4_HUMAN 64 96
DBREF 6DMM F 1 33 UNP P12838 DEF4_HUMAN 64 96
DBREF 6DMM G 1 33 UNP P12838 DEF4_HUMAN 64 96
DBREF 6DMM H 1 33 UNP P12838 DEF4_HUMAN 64 96
DBREF 6DMM I 1 33 UNP P12838 DEF4_HUMAN 64 96
DBREF 6DMM J 1 33 UNP P12838 DEF4_HUMAN 64 96
DBREF 6DMM K 1 33 UNP P12838 DEF4_HUMAN 64 96
DBREF 6DMM L 1 33 UNP P12838 DEF4_HUMAN 64 96
SEQADV 6DMM ALA A 23 UNP P12838 GLY 86 ENGINEERED MUTATION
SEQADV 6DMM ALA B 23 UNP P12838 GLY 86 ENGINEERED MUTATION
SEQADV 6DMM ALA C 23 UNP P12838 GLY 86 ENGINEERED MUTATION
SEQADV 6DMM ALA D 23 UNP P12838 GLY 86 ENGINEERED MUTATION
SEQADV 6DMM ALA E 23 UNP P12838 GLY 86 ENGINEERED MUTATION
SEQADV 6DMM ALA F 23 UNP P12838 GLY 86 ENGINEERED MUTATION
SEQADV 6DMM ALA G 23 UNP P12838 GLY 86 ENGINEERED MUTATION
SEQADV 6DMM ALA H 23 UNP P12838 GLY 86 ENGINEERED MUTATION
SEQADV 6DMM ALA I 23 UNP P12838 GLY 86 ENGINEERED MUTATION
SEQADV 6DMM ALA J 23 UNP P12838 GLY 86 ENGINEERED MUTATION
SEQADV 6DMM ALA K 23 UNP P12838 GLY 86 ENGINEERED MUTATION
SEQADV 6DMM ALA L 23 UNP P12838 GLY 86 ENGINEERED MUTATION
SEQRES 1 A 33 VAL CYS SER CYS ARG LEU VAL PHE CYS ARG ARG THR GLU
SEQRES 2 A 33 LEU ARG VAL GLY ASN CYS LEU ILE GLY ALA VAL SER PHE
SEQRES 3 A 33 THR TYR CYS CYS THR ARG VAL
SEQRES 1 B 33 VAL CYS SER CYS ARG LEU VAL PHE CYS ARG ARG THR GLU
SEQRES 2 B 33 LEU ARG VAL GLY ASN CYS LEU ILE GLY ALA VAL SER PHE
SEQRES 3 B 33 THR TYR CYS CYS THR ARG VAL
SEQRES 1 C 33 VAL CYS SER CYS ARG LEU VAL PHE CYS ARG ARG THR GLU
SEQRES 2 C 33 LEU ARG VAL GLY ASN CYS LEU ILE GLY ALA VAL SER PHE
SEQRES 3 C 33 THR TYR CYS CYS THR ARG VAL
SEQRES 1 D 33 VAL CYS SER CYS ARG LEU VAL PHE CYS ARG ARG THR GLU
SEQRES 2 D 33 LEU ARG VAL GLY ASN CYS LEU ILE GLY ALA VAL SER PHE
SEQRES 3 D 33 THR TYR CYS CYS THR ARG VAL
SEQRES 1 E 33 VAL CYS SER CYS ARG LEU VAL PHE CYS ARG ARG THR GLU
SEQRES 2 E 33 LEU ARG VAL GLY ASN CYS LEU ILE GLY ALA VAL SER PHE
SEQRES 3 E 33 THR TYR CYS CYS THR ARG VAL
SEQRES 1 F 33 VAL CYS SER CYS ARG LEU VAL PHE CYS ARG ARG THR GLU
SEQRES 2 F 33 LEU ARG VAL GLY ASN CYS LEU ILE GLY ALA VAL SER PHE
SEQRES 3 F 33 THR TYR CYS CYS THR ARG VAL
SEQRES 1 G 33 VAL CYS SER CYS ARG LEU VAL PHE CYS ARG ARG THR GLU
SEQRES 2 G 33 LEU ARG VAL GLY ASN CYS LEU ILE GLY ALA VAL SER PHE
SEQRES 3 G 33 THR TYR CYS CYS THR ARG VAL
SEQRES 1 H 33 VAL CYS SER CYS ARG LEU VAL PHE CYS ARG ARG THR GLU
SEQRES 2 H 33 LEU ARG VAL GLY ASN CYS LEU ILE GLY ALA VAL SER PHE
SEQRES 3 H 33 THR TYR CYS CYS THR ARG VAL
SEQRES 1 I 33 VAL CYS SER CYS ARG LEU VAL PHE CYS ARG ARG THR GLU
SEQRES 2 I 33 LEU ARG VAL GLY ASN CYS LEU ILE GLY ALA VAL SER PHE
SEQRES 3 I 33 THR TYR CYS CYS THR ARG VAL
SEQRES 1 J 33 VAL CYS SER CYS ARG LEU VAL PHE CYS ARG ARG THR GLU
SEQRES 2 J 33 LEU ARG VAL GLY ASN CYS LEU ILE GLY ALA VAL SER PHE
SEQRES 3 J 33 THR TYR CYS CYS THR ARG VAL
SEQRES 1 K 33 VAL CYS SER CYS ARG LEU VAL PHE CYS ARG ARG THR GLU
SEQRES 2 K 33 LEU ARG VAL GLY ASN CYS LEU ILE GLY ALA VAL SER PHE
SEQRES 3 K 33 THR TYR CYS CYS THR ARG VAL
SEQRES 1 L 33 VAL CYS SER CYS ARG LEU VAL PHE CYS ARG ARG THR GLU
SEQRES 2 L 33 LEU ARG VAL GLY ASN CYS LEU ILE GLY ALA VAL SER PHE
SEQRES 3 L 33 THR TYR CYS CYS THR ARG VAL
HET SO4 A 101 5
HET SO4 B 101 5
HET MPD B 102 8
HET SO4 D 101 5
HET SO4 D 102 5
HET SO4 E 101 5
HET SO4 F 101 5
HET SO4 G 101 5
HET SO4 G 102 5
HET SO4 H 101 5
HET SO4 H 102 5
HET SO4 H 103 5
HET SO4 I 101 5
HET SO4 J 101 5
HET SO4 J 102 5
HET SO4 J 103 5
HET MPD J 104 8
HET SO4 K 101 5
HET SO4 L 101 5
HET SO4 L 102 5
HET SO4 L 103 5
HET SO4 L 104 5
HET SO4 L 105 5
HET SO4 L 106 5
HETNAM SO4 SULFATE ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 13 SO4 22(O4 S 2-)
FORMUL 15 MPD 2(C6 H14 O2)
FORMUL 37 HOH *284(H2 O)
SHEET 1 AA111 CYS B 2 ARG B 5 0
SHEET 2 AA111 VAL B 24 CYS B 30 -1 O THR B 27 N ARG B 5
SHEET 3 AA111 LEU B 14 ILE B 21 -1 N VAL B 16 O TYR B 28
SHEET 4 AA111 GLU A 13 ILE A 21 -1 N LEU A 20 O ASN B 18
SHEET 5 AA111 VAL A 24 THR A 31 -1 O CYS A 30 N LEU A 14
SHEET 6 AA111 CYS A 2 ARG A 5 -1 N ARG A 5 O THR A 27
SHEET 7 AA111 VAL D 24 CYS D 30 1 O SER D 25 N CYS A 4
SHEET 8 AA111 LEU D 14 ILE D 21 -1 N VAL D 16 O TYR D 28
SHEET 9 AA111 GLU C 13 ILE C 21 -1 N ASN C 18 O LEU D 20
SHEET 10 AA111 VAL C 24 THR C 31 -1 O PHE C 26 N CYS C 19
SHEET 11 AA111 CYS C 2 ARG C 5 -1 N ARG C 5 O THR C 27
SHEET 1 AA2 8 CYS B 2 ARG B 5 0
SHEET 2 AA2 8 VAL B 24 CYS B 30 -1 O THR B 27 N ARG B 5
SHEET 3 AA2 8 LEU B 14 ILE B 21 -1 N VAL B 16 O TYR B 28
SHEET 4 AA2 8 GLU A 13 ILE A 21 -1 N LEU A 20 O ASN B 18
SHEET 5 AA2 8 VAL A 24 THR A 31 -1 O CYS A 30 N LEU A 14
SHEET 6 AA2 8 CYS A 2 ARG A 5 -1 N ARG A 5 O THR A 27
SHEET 7 AA2 8 VAL D 24 CYS D 30 1 O SER D 25 N CYS A 4
SHEET 8 AA2 8 CYS D 2 ARG D 5 -1 N ARG D 5 O THR D 27
SHEET 1 AA3 6 CYS E 2 ARG E 5 0
SHEET 2 AA3 6 VAL E 24 THR E 31 -1 O THR E 27 N ARG E 5
SHEET 3 AA3 6 GLU E 13 ILE E 21 -1 N LEU E 14 O CYS E 30
SHEET 4 AA3 6 LEU F 14 ILE F 21 -1 O LEU F 20 N ASN E 18
SHEET 5 AA3 6 VAL F 24 CYS F 30 -1 O PHE F 26 N CYS F 19
SHEET 6 AA3 6 CYS F 2 ARG F 5 -1 N ARG F 5 O THR F 27
SHEET 1 AA4 6 CYS G 2 ARG G 5 0
SHEET 2 AA4 6 VAL G 24 CYS G 30 -1 O THR G 27 N ARG G 5
SHEET 3 AA4 6 LEU G 14 ILE G 21 -1 N CYS G 19 O PHE G 26
SHEET 4 AA4 6 GLU H 13 ILE H 21 -1 O LEU H 20 N ASN G 18
SHEET 5 AA4 6 VAL H 24 THR H 31 -1 O TYR H 28 N VAL H 16
SHEET 6 AA4 6 CYS H 2 ARG H 5 -1 N ARG H 5 O THR H 27
SHEET 1 AA5 6 CYS I 2 ARG I 5 0
SHEET 2 AA5 6 VAL I 24 THR I 31 -1 O THR I 27 N ARG I 5
SHEET 3 AA5 6 GLU I 13 ILE I 21 -1 N LEU I 14 O CYS I 30
SHEET 4 AA5 6 GLU J 13 ILE J 21 -1 O LEU J 20 N ASN I 18
SHEET 5 AA5 6 VAL J 24 THR J 31 -1 O CYS J 30 N LEU J 14
SHEET 6 AA5 6 CYS J 2 ARG J 5 -1 N ARG J 5 O THR J 27
SHEET 1 AA6 6 CYS K 2 ARG K 5 0
SHEET 2 AA6 6 VAL K 24 THR K 31 -1 O THR K 27 N ARG K 5
SHEET 3 AA6 6 GLU K 13 ILE K 21 -1 N CYS K 19 O PHE K 26
SHEET 4 AA6 6 GLU L 13 ILE L 21 -1 O LEU L 20 N ASN K 18
SHEET 5 AA6 6 VAL L 24 THR L 31 -1 O TYR L 28 N VAL L 16
SHEET 6 AA6 6 CYS L 2 ARG L 5 -1 N ARG L 5 O THR L 27
SSBOND 1 CYS A 2 CYS A 30 1555 1555 2.04
SSBOND 2 CYS A 4 CYS A 19 1555 1555 2.04
SSBOND 3 CYS A 9 CYS A 29 1555 1555 2.04
SSBOND 4 CYS B 2 CYS B 30 1555 1555 2.03
SSBOND 5 CYS B 4 CYS B 19 1555 1555 1.95
SSBOND 6 CYS B 9 CYS B 29 1555 1555 2.03
SSBOND 7 CYS C 2 CYS C 30 1555 1555 2.03
SSBOND 8 CYS C 4 CYS C 19 1555 1555 2.02
SSBOND 9 CYS C 9 CYS C 29 1555 1555 2.04
SSBOND 10 CYS D 2 CYS D 30 1555 1555 2.04
SSBOND 11 CYS D 4 CYS D 19 1555 1555 2.00
SSBOND 12 CYS D 9 CYS D 29 1555 1555 2.04
SSBOND 13 CYS E 2 CYS E 30 1555 1555 2.03
SSBOND 14 CYS E 4 CYS E 19 1555 1555 2.05
SSBOND 15 CYS E 9 CYS E 29 1555 1555 2.03
SSBOND 16 CYS F 2 CYS F 30 1555 1555 2.02
SSBOND 17 CYS F 4 CYS F 19 1555 1555 2.05
SSBOND 18 CYS F 9 CYS F 29 1555 1555 2.03
SSBOND 19 CYS G 2 CYS G 30 1555 1555 2.04
SSBOND 20 CYS G 4 CYS G 19 1555 1555 2.04
SSBOND 21 CYS G 9 CYS G 29 1555 1555 2.03
SSBOND 22 CYS H 2 CYS H 30 1555 1555 2.03
SSBOND 23 CYS H 4 CYS H 19 1555 1555 2.04
SSBOND 24 CYS H 9 CYS H 29 1555 1555 2.02
SSBOND 25 CYS I 2 CYS I 30 1555 1555 2.01
SSBOND 26 CYS I 4 CYS I 19 1555 1555 2.06
SSBOND 27 CYS I 9 CYS I 29 1555 1555 2.04
SSBOND 28 CYS J 2 CYS J 30 1555 1555 2.01
SSBOND 29 CYS J 4 CYS J 19 1555 1555 2.03
SSBOND 30 CYS J 9 CYS J 29 1555 1555 2.05
SSBOND 31 CYS K 2 CYS K 30 1555 1555 2.02
SSBOND 32 CYS K 4 CYS K 19 1555 1555 2.01
SSBOND 33 CYS K 9 CYS K 29 1555 1555 2.05
SSBOND 34 CYS L 2 CYS L 30 1555 1555 2.03
SSBOND 35 CYS L 4 CYS L 19 1555 1555 2.03
SSBOND 36 CYS L 9 CYS L 29 1555 1555 2.03
SITE 1 AC1 2 ARG A 10 ARG A 11
SITE 1 AC2 5 ARG A 32 ARG B 10 ARG B 11 HOH B 206
SITE 2 AC2 5 ARG K 15
SITE 1 AC3 4 PHE B 26 LEU E 6 PHE E 26 VAL H 24
SITE 1 AC4 8 ARG A 5 ARG A 10 GLU A 13 ARG D 15
SITE 2 AC4 8 ASN D 18 HOH D 203 HOH D 215 VAL I 1
SITE 1 AC5 4 ARG D 10 ARG D 11 ARG E 32 ARG I 15
SITE 1 AC6 4 VAL E 1 ASN H 18 HOH H 201 ARG K 10
SITE 1 AC7 3 ARG C 32 ARG F 10 ARG F 11
SITE 1 AC8 6 VAL C 1 ARG G 5 ARG G 10 HOH G 203
SITE 2 AC8 6 ASN J 18 HOH J 201
SITE 1 AC9 7 ARG C 5 ARG C 10 ASN F 18 SER F 25
SITE 2 AC9 7 THR F 27 HOH F 201 ARG G 11
SITE 1 AD1 8 HOH A 203 ARG H 15 ASN H 18 THR H 27
SITE 2 AD1 8 HOH H 205 HOH H 207 ARG K 10 HOH K 211
SITE 1 AD2 9 ARG D 10 VAL H 1 THR H 31 HOH H 220
SITE 2 AD2 9 HOH H 221 ARG I 15 ASN I 18 HOH I 212
SITE 3 AD2 9 HOH J 216
SITE 1 AD3 2 ARG H 5 ARG H 10
SITE 1 AD4 6 VAL A 1 THR A 31 ARG I 5 ARG I 10
SITE 2 AD4 6 ASN L 18 HOH L 207
SITE 1 AD5 3 ARG C 15 ARG J 10 ARG J 11
SITE 1 AD6 9 ARG G 10 ARG J 15 ASN J 18 THR J 27
SITE 2 AD6 9 HOH J 206 HOH J 207 HOH J 209 HOH J 217
SITE 3 AD6 9 HOH J 223
SITE 1 AD7 3 VAL B 1 ARG J 5 ARG J 10
SITE 1 AD8 1 VAL J 24
SITE 1 AD9 8 ARG B 10 VAL J 1 THR J 31 ARG K 15
SITE 2 AD9 8 GLY K 17 ASN K 18 HOH K 201 HOH K 209
SITE 1 AE1 6 ARG F 10 ARG G 15 ASN G 18 VAL L 1
SITE 2 AE1 6 THR L 31 HOH L 226
SITE 1 AE2 9 ARG I 10 ARG L 15 ASN L 18 THR L 27
SITE 2 AE2 9 HOH L 202 HOH L 212 HOH L 215 HOH L 218
SITE 3 AE2 9 HOH L 219
SITE 1 AE3 4 ARG K 32 ARG L 10 ARG L 11 HOH L 201
SITE 1 AE4 1 PHE D 26
SITE 1 AE5 8 ARG A 15 ASN A 18 THR A 27 ARG K 32
SITE 2 AE5 8 HOH K 206 ARG L 10 HOH L 205 HOH L 214
SITE 1 AE6 8 VAL F 1 THR F 31 HOH F 208 ARG L 5
SITE 2 AE6 8 ARG L 10 HOH L 204 HOH L 216 HOH L 223
CRYST1 41.629 65.894 124.064 90.00 90.00 90.00 P 21 21 21 48
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 0.024022 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015176 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008060 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
