HEADER CELL ADHESION 24-SEP-18 6MK0
TITLE INTEGRIN ALPHAVBETA3 ECTODOMAIN BOUND TO ANTAGONIST TDI-4161
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEGRIN ALPHA-V;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: VITRONECTIN RECEPTOR,VITRONECTIN RECEPTOR SUBUNIT ALPHA;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: INTEGRIN BETA-3;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA,GPIIIA;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ITGAV, MSK8, VNRA, VTNR;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: ITGB3, GP3A;
SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS HYBRID DOMAIN, PSI, EGF REPEATS, BETA TAIL, CALF, THIGH, BETA
KEYWDS 2 PROPELLER, RGD MOTIF, FIBRONECTIN, VITRONECTIN, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.VAN AGTHOVEN,M.A.ARNAOUT
REVDAT 7 11-OCT-23 6MK0 1 HETSYN LINK
REVDAT 6 29-JUL-20 6MK0 1 COMPND REMARK HETNAM LINK
REVDAT 6 2 1 SITE ATOM
REVDAT 5 12-FEB-20 6MK0 1 AUTHOR JRNL
REVDAT 4 18-DEC-19 6MK0 1 REMARK
REVDAT 3 20-NOV-19 6MK0 1 LINK
REVDAT 2 23-OCT-19 6MK0 1 REMARK HELIX SHEET SSBOND
REVDAT 2 2 1 LINK SITE ATOM
REVDAT 1 25-SEP-19 6MK0 0
JRNL AUTH J.LI,Y.FUKASE,Y.SHANG,W.ZOU,J.MUNOZ-FELIX,L.BUITRAGO,
JRNL AUTH 2 J.VAN AGTHOVEN,Y.ZHANG,R.HARA,Y.TANAKA,R.OKAMOTO,T.YASUI,
JRNL AUTH 3 T.NAKAHATA,T.IMAEDA,K.ASO,Y.ZHOU,C.LOCUSON,D.NESIC,M.DUGGAN,
JRNL AUTH 4 J.TAKAGI,R.D.VAUGHAN,T.WALZ,K.HODIVALA-DILKE,S.L.TEITELBAUM,
JRNL AUTH 5 M.A.ARNAOUT,M.FILIZOLA,M.A.FOLEY,B.S.COLLER
JRNL TITL NOVEL PURE ALPHAVBETA3 INTEGRIN ANTAGONISTS THAT DO NOT
JRNL TITL 2 INDUCE RECEPTOR EXTENSION, PRIME THE RECEPTOR, OR ENHANCE
JRNL TITL 3 ANGIOGENESIS AT LOW CONCENTRATIONS
JRNL REF ACS PHARMACOL TRANSL SCI V. 2 387 2019
JRNL REFN ESSN 2575-910
JRNL DOI 10.1021/ACSPTSCI.9B00041
REMARK 2
REMARK 2 RESOLUTION. 3.01 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) : 3.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 3 NUMBER OF REFLECTIONS : 56333
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 2857
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 49.0940 - 8.1441 1.00 3051 172 0.2100 0.2352
REMARK 3 2 8.1441 - 6.4689 1.00 2938 135 0.2327 0.2166
REMARK 3 3 6.4689 - 5.6526 1.00 2892 160 0.2277 0.2710
REMARK 3 4 5.6526 - 5.1364 1.00 2914 127 0.1984 0.2359
REMARK 3 5 5.1364 - 4.7685 1.00 2845 154 0.1775 0.2075
REMARK 3 6 4.7685 - 4.4876 1.00 2826 163 0.1733 0.2448
REMARK 3 7 4.4876 - 4.2630 1.00 2855 172 0.1876 0.1908
REMARK 3 8 4.2630 - 4.0775 1.00 2778 186 0.1915 0.2039
REMARK 3 9 4.0775 - 3.9206 1.00 2836 130 0.2115 0.2095
REMARK 3 10 3.9206 - 3.7854 1.00 2851 134 0.2242 0.2476
REMARK 3 11 3.7854 - 3.6670 1.00 2849 138 0.2276 0.2993
REMARK 3 12 3.6670 - 3.5623 0.99 2787 156 0.2338 0.3106
REMARK 3 13 3.5623 - 3.4685 0.98 2765 132 0.2477 0.3287
REMARK 3 14 3.4685 - 3.3839 0.96 2669 162 0.2664 0.2594
REMARK 3 15 3.3839 - 3.3070 0.94 2644 146 0.2632 0.2961
REMARK 3 16 3.3070 - 3.2366 0.92 2543 131 0.2762 0.3384
REMARK 3 17 3.2366 - 3.1719 0.87 2483 135 0.2789 0.3067
REMARK 3 18 3.1719 - 3.1120 0.80 2246 117 0.2795 0.3135
REMARK 3 19 3.1120 - 3.0565 0.73 2022 117 0.2856 0.3336
REMARK 3 20 3.0565 - 3.0050 0.60 1682 90 0.3112 0.3539
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) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.440
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.99
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 11
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 444 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2528 53.6821 19.5111
REMARK 3 T TENSOR
REMARK 3 T11: 0.3492 T22: 0.0180
REMARK 3 T33: 0.1467 T12: -0.3740
REMARK 3 T13: -0.0760 T23: 0.1041
REMARK 3 L TENSOR
REMARK 3 L11: 0.2575 L22: 0.5360
REMARK 3 L33: 0.0936 L12: 0.2203
REMARK 3 L13: -0.0575 L23: -0.0785
REMARK 3 S TENSOR
REMARK 3 S11: -0.0725 S12: 0.1069 S13: 0.0651
REMARK 3 S21: -0.1272 S22: 0.0901 S23: 0.2295
REMARK 3 S31: -0.0251 S32: -0.0810 S33: -0.0421
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 445 THROUGH 647 )
REMARK 3 ORIGIN FOR THE GROUP (A): -45.4787 46.4186 -0.4572
REMARK 3 T TENSOR
REMARK 3 T11: 0.6743 T22: 0.5306
REMARK 3 T33: 0.6210 T12: -0.2117
REMARK 3 T13: -0.3818 T23: 0.1793
REMARK 3 L TENSOR
REMARK 3 L11: 1.3664 L22: 0.4640
REMARK 3 L33: 0.7400 L12: -0.1105
REMARK 3 L13: 0.4831 L23: 0.0820
REMARK 3 S TENSOR
REMARK 3 S11: -0.2454 S12: 0.2419 S13: 0.1688
REMARK 3 S21: -0.1133 S22: 0.1471 S23: -0.0462
REMARK 3 S31: -0.0761 S32: 0.1757 S33: 0.0725
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 648 THROUGH 755 )
REMARK 3 ORIGIN FOR THE GROUP (A): -45.0696 40.9565 30.7352
REMARK 3 T TENSOR
REMARK 3 T11: 0.6976 T22: 0.4924
REMARK 3 T33: 0.4383 T12: 0.0943
REMARK 3 T13: -0.1665 T23: 0.0959
REMARK 3 L TENSOR
REMARK 3 L11: 1.4291 L22: 0.2047
REMARK 3 L33: 3.5562 L12: -0.3597
REMARK 3 L13: 2.1904 L23: -0.7084
REMARK 3 S TENSOR
REMARK 3 S11: -0.2887 S12: 0.2518 S13: 0.2653
REMARK 3 S21: -0.1539 S22: 0.0465 S23: 0.0749
REMARK 3 S31: -0.0515 S32: 0.2510 S33: 0.1980
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 756 THROUGH 954 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.5409 37.2451 73.5242
REMARK 3 T TENSOR
REMARK 3 T11: 0.4918 T22: 0.2011
REMARK 3 T33: 0.2213 T12: 0.2493
REMARK 3 T13: -0.0148 T23: -0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 1.1984 L22: 2.3251
REMARK 3 L33: 1.0264 L12: -0.4731
REMARK 3 L13: 0.1103 L23: -0.4673
REMARK 3 S TENSOR
REMARK 3 S11: -0.1377 S12: -0.2495 S13: -0.0895
REMARK 3 S21: 0.4028 S22: 0.1172 S23: -0.2268
REMARK 3 S31: -0.0505 S32: 0.0533 S33: 0.0333
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 43 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.5511 6.9770 7.3318
REMARK 3 T TENSOR
REMARK 3 T11: 1.1193 T22: 1.1559
REMARK 3 T33: 1.1124 T12: -0.0100
REMARK 3 T13: -0.1967 T23: -0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 1.7586 L22: 0.1870
REMARK 3 L33: 2.6846 L12: 0.4848
REMARK 3 L13: 2.1654 L23: 0.5659
REMARK 3 S TENSOR
REMARK 3 S11: -0.1094 S12: 0.4797 S13: -0.2112
REMARK 3 S21: -0.5112 S22: -0.0263 S23: 0.4712
REMARK 3 S31: 0.1638 S32: -0.5052 S33: 0.1286
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 44 THROUGH 111 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.7363 0.6541 23.1972
REMARK 3 T TENSOR
REMARK 3 T11: 0.6509 T22: 0.1642
REMARK 3 T33: 0.4201 T12: -0.1453
REMARK 3 T13: 0.0342 T23: 0.0446
REMARK 3 L TENSOR
REMARK 3 L11: 5.0843 L22: 1.6374
REMARK 3 L33: 2.1906 L12: 0.3845
REMARK 3 L13: 1.6825 L23: 0.1898
REMARK 3 S TENSOR
REMARK 3 S11: 0.0740 S12: 0.3250 S13: -0.4614
REMARK 3 S21: -0.2844 S22: 0.0410 S23: -0.0141
REMARK 3 S31: 0.2757 S32: -0.1338 S33: -0.1118
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 112 THROUGH 365 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8716 24.5243 34.4730
REMARK 3 T TENSOR
REMARK 3 T11: 0.4532 T22: 0.1573
REMARK 3 T33: 0.4366 T12: -0.2033
REMARK 3 T13: -0.1258 T23: 0.1484
REMARK 3 L TENSOR
REMARK 3 L11: 0.5337 L22: 1.7330
REMARK 3 L33: 0.6807 L12: 0.6608
REMARK 3 L13: -0.2745 L23: -0.1400
REMARK 3 S TENSOR
REMARK 3 S11: 0.1427 S12: -0.2101 S13: -0.3496
REMARK 3 S21: 0.2661 S22: -0.0552 S23: -0.4485
REMARK 3 S31: 0.1168 S32: 0.1247 S33: 0.1077
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 366 THROUGH 412 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.1240 11.0114 30.8911
REMARK 3 T TENSOR
REMARK 3 T11: 0.8474 T22: 0.2224
REMARK 3 T33: 0.4376 T12: 0.0008
REMARK 3 T13: 0.1150 T23: 0.0883
REMARK 3 L TENSOR
REMARK 3 L11: 2.3631 L22: 2.4706
REMARK 3 L33: 0.5347 L12: -0.4426
REMARK 3 L13: 0.5166 L23: 0.6843
REMARK 3 S TENSOR
REMARK 3 S11: -0.0713 S12: 0.0138 S13: 0.0051
REMARK 3 S21: -0.0865 S22: 0.0127 S23: 0.0931
REMARK 3 S31: -0.1991 S32: -0.1243 S33: 0.0505
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 413 THROUGH 538 )
REMARK 3 ORIGIN FOR THE GROUP (A): -38.6325 18.1794 4.1483
REMARK 3 T TENSOR
REMARK 3 T11: 1.0535 T22: 0.7175
REMARK 3 T33: 0.8920 T12: -0.2350
REMARK 3 T13: -0.2582 T23: 0.0585
REMARK 3 L TENSOR
REMARK 3 L11: 1.1895 L22: 0.5430
REMARK 3 L33: 1.3481 L12: -0.7875
REMARK 3 L13: 0.2729 L23: -0.2808
REMARK 3 S TENSOR
REMARK 3 S11: -0.1511 S12: 0.5919 S13: 0.0698
REMARK 3 S21: -0.4781 S22: -0.0518 S23: 0.4372
REMARK 3 S31: -0.1742 S32: -0.4606 S33: 0.1388
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 539 THROUGH 642 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.9378 19.9868 46.9545
REMARK 3 T TENSOR
REMARK 3 T11: 0.6729 T22: 0.3273
REMARK 3 T33: 0.5301 T12: 0.1654
REMARK 3 T13: 0.0043 T23: -0.0669
REMARK 3 L TENSOR
REMARK 3 L11: 0.0926 L22: 0.5897
REMARK 3 L33: 1.0107 L12: -0.1111
REMARK 3 L13: 0.1662 L23: -0.7712
REMARK 3 S TENSOR
REMARK 3 S11: -0.0843 S12: 0.1179 S13: -0.2001
REMARK 3 S21: -0.0686 S22: 0.0189 S23: -0.0091
REMARK 3 S31: 0.2218 S32: 0.0560 S33: 0.0503
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 643 THROUGH 690 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1842 16.6834 70.8581
REMARK 3 T TENSOR
REMARK 3 T11: 0.6728 T22: 0.2457
REMARK 3 T33: 0.7851 T12: 0.1622
REMARK 3 T13: -0.0145 T23: 0.0812
REMARK 3 L TENSOR
REMARK 3 L11: 3.0595 L22: 3.6768
REMARK 3 L33: 3.8502 L12: -0.0115
REMARK 3 L13: -1.1973 L23: -1.2325
REMARK 3 S TENSOR
REMARK 3 S11: 0.0294 S12: 0.0672 S13: 0.3035
REMARK 3 S21: -0.1428 S22: -0.0847 S23: -0.4916
REMARK 3 S31: -0.3363 S32: 0.2626 S33: 0.0717
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 6MK0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-SEP-18.
REMARK 100 THE DEPOSITION ID IS D_1000236813.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUL-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97895
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59916
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.13600
REMARK 200 R SYM (I) : 0.05200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 3IJE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM ACETATE PH 4.5, 800 MM
REMARK 280 SODIUM CHOLRIDE, 12% PEG 4000., VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 203.69000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 101.84500
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 101.84500
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 203.69000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 73390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 42.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, 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 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 836
REMARK 465 SER A 837
REMARK 465 LEU A 838
REMARK 465 GLN A 839
REMARK 465 THR A 840
REMARK 465 THR A 841
REMARK 465 GLU A 842
REMARK 465 LYS A 843
REMARK 465 ASN A 844
REMARK 465 ASP A 845
REMARK 465 THR A 846
REMARK 465 VAL A 847
REMARK 465 ALA A 848
REMARK 465 GLY A 849
REMARK 465 GLN A 850
REMARK 465 GLY A 851
REMARK 465 GLU A 852
REMARK 465 ARG A 853
REMARK 465 ASP A 854
REMARK 465 HIS A 855
REMARK 465 LEU A 856
REMARK 465 ILE A 857
REMARK 465 THR A 858
REMARK 465 LYS A 859
REMARK 465 ARG A 860
REMARK 465 ASP A 861
REMARK 465 LEU A 862
REMARK 465 ALA A 863
REMARK 465 LEU A 864
REMARK 465 SER A 865
REMARK 465 GLU A 866
REMARK 465 GLY A 867
REMARK 465 ASP A 868
REMARK 465 ILE A 869
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 ND2 ASN A 266 O5 NAG D 1 1.69
REMARK 500 O6 BMA D 3 C2 BMA D 4 1.98
REMARK 500 ND2 ASN A 458 O5 NAG E 1 2.00
REMARK 500 ND2 ASN A 950 C2 NAG A 1017 2.02
REMARK 500 ND2 ASN B 320 O5 NAG B 702 2.06
REMARK 500 O4 NAG D 2 C2 BMA D 3 2.07
REMARK 500 ND2 ASN A 943 O5 NAG A 1016 2.07
REMARK 500 ND2 ASN A 821 O5 NAG F 1 2.08
REMARK 500 ND2 ASN A 260 O5 NAG A 1003 2.08
REMARK 500 O4 NAG C 1 C2 NAG C 2 2.09
REMARK 500 O4 NAG H 2 O2 BMA H 3 2.09
REMARK 500 CG ASN A 44 C1 NAG C 1 2.17
REMARK 500 CG ASN A 950 C1 NAG A 1017 2.17
REMARK 500 OG SER B 130 O ASP B 336 2.18
REMARK 500 O4 NAG H 2 C2 BMA H 3 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 OG SER B 77 O SER B 641 5555 2.05
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 27 78.22 -118.94
REMARK 500 LYS A 42 -2.80 77.73
REMARK 500 SER A 62 4.03 -66.72
REMARK 500 SER A 63 -5.39 76.66
REMARK 500 ASP A 84 89.22 -151.02
REMARK 500 LYS A 89 -2.98 65.56
REMARK 500 THR A 116 -9.49 77.95
REMARK 500 ASP A 167 55.50 36.02
REMARK 500 ASP A 325 151.44 -48.28
REMARK 500 ALA A 426 -61.38 -93.96
REMARK 500 PHE A 427 -10.22 72.35
REMARK 500 LYS A 505 -17.12 73.50
REMARK 500 ALA A 507 175.28 173.23
REMARK 500 ARG A 510 -6.11 73.03
REMARK 500 GLU A 545 -9.83 -57.11
REMARK 500 ARG A 549 -3.38 67.60
REMARK 500 LEU A 552 -7.57 73.71
REMARK 500 TYR A 565 5.75 -68.06
REMARK 500 GLN A 634 54.45 -91.40
REMARK 500 SER A 705 -9.57 74.58
REMARK 500 GLU A 769 -9.19 72.14
REMARK 500 LEU A 808 -60.41 -101.42
REMARK 500 CYS A 874 7.60 -69.60
REMARK 500 MET A 909 -4.56 74.78
REMARK 500 ASN A 910 -70.85 -93.90
REMARK 500 LYS A 911 -51.47 -129.49
REMARK 500 ASN A 935 32.55 71.53
REMARK 500 ILE A 938 -64.38 -125.48
REMARK 500 GLU A 939 -21.24 76.01
REMARK 500 ASP A 940 171.42 167.13
REMARK 500 CYS B 5 -14.67 72.24
REMARK 500 GLN B 14 -8.92 75.17
REMARK 500 PRO B 21 0.27 -65.07
REMARK 500 GLU B 29 -0.13 64.29
REMARK 500 ALA B 30 -157.32 -163.75
REMARK 500 SER B 35 51.19 -146.44
REMARK 500 ARG B 37 -162.55 -78.33
REMARK 500 GLU B 42 -9.22 77.24
REMARK 500 LEU B 45 49.12 -88.63
REMARK 500 ASP B 47 -63.47 -102.53
REMARK 500 ASN B 48 -172.77 -174.10
REMARK 500 CYS B 49 37.17 74.24
REMARK 500 PRO B 51 59.42 -90.22
REMARK 500 VAL B 157 -67.53 -123.79
REMARK 500 CYS B 177 50.72 -91.70
REMARK 500 LYS B 208 -9.86 76.54
REMARK 500 SER B 213 -170.00 -124.70
REMARK 500 CYS B 232 36.85 -98.57
REMARK 500 LEU B 258 -4.87 78.44
REMARK 500 ILE B 325 78.56 -113.31
REMARK 500
REMARK 500 THIS ENTRY HAS 85 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY B 453 THR B 454 144.99
REMARK 500 GLU B 472 CYS B 473 140.11
REMARK 500 ARG B 479 PRO B 480 -149.70
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 MN A1018 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 230 OD1
REMARK 620 2 ASN A 232 OD1 88.0
REMARK 620 3 ASP A 234 OD1 67.0 79.4
REMARK 620 4 ASP A 234 OD2 124.4 76.7 57.8
REMARK 620 5 ILE A 236 O 76.2 160.1 83.3 102.2
REMARK 620 6 ASP A 238 OD1 85.2 94.5 151.5 148.2 96.0
REMARK 620 7 ASP A 238 OD2 138.5 98.7 154.5 96.9 101.2 53.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1019 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 284 OD1
REMARK 620 2 ASN A 286 OD1 67.5
REMARK 620 3 ASP A 288 OD1 61.8 65.2
REMARK 620 4 TYR A 290 O 71.5 137.6 103.9
REMARK 620 5 ASP A 292 OD1 143.4 126.6 152.6 82.7
REMARK 620 6 ASP A 292 OD2 101.0 73.8 139.0 104.7 60.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1020 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 349 OD1
REMARK 620 2 ASP A 351 OD1 85.9
REMARK 620 3 ASP A 353 OD1 83.1 72.1
REMARK 620 4 PHE A 355 O 64.9 147.4 89.5
REMARK 620 5 ASP A 357 OD1 130.8 125.6 138.1 86.0
REMARK 620 6 ASP A 357 OD2 98.3 78.4 150.3 118.1 60.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1021 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 413 OD1
REMARK 620 2 ASP A 415 OD1 68.1
REMARK 620 3 ASN A 417 OD1 58.3 66.7
REMARK 620 4 ASN A 417 ND2 111.0 86.1 52.7
REMARK 620 5 TYR A 419 O 77.6 144.7 88.5 98.8
REMARK 620 6 ASP A 421 OD1 147.2 116.1 154.5 101.7 97.3
REMARK 620 7 ASP A 421 OD2 91.3 79.6 140.7 146.7 110.2 59.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1022 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 596 O
REMARK 620 2 ASP A 599 OD1 65.8
REMARK 620 3 ASP A 599 OD2 126.6 61.2
REMARK 620 4 VAL A 601 O 70.4 74.6 89.3
REMARK 620 5 GLU A 636 OE1 88.0 142.2 132.3 71.1
REMARK 620 6 GLU A 636 OE2 85.1 136.6 140.7 126.5 61.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 708 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 121 OG
REMARK 620 2 GLU B 220 OE1 92.0
REMARK 620 3 JUY B 712 O03 97.5 64.0
REMARK 620 4 HOH B 801 O 88.9 158.1 94.2
REMARK 620 5 HOH B 802 O 74.7 116.0 172.2 85.3
REMARK 620 6 HOH B 804 O 149.1 115.4 107.0 71.2 80.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 709 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 123 O
REMARK 620 2 ASP B 126 OD1 74.3
REMARK 620 3 ASP B 126 OD2 123.5 56.6
REMARK 620 4 ASP B 127 OD1 85.7 68.9 99.5
REMARK 620 5 MET B 335 O 160.5 115.9 74.2 83.2
REMARK 620 6 HOH B 803 O 85.4 158.9 136.3 116.0 85.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 710 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 158 OD2
REMARK 620 2 ASN B 215 OD1 90.8
REMARK 620 3 ASP B 217 O 171.2 93.7
REMARK 620 4 ASP B 217 OD1 102.9 87.7 69.8
REMARK 620 5 PRO B 219 O 85.3 166.7 91.9 105.6
REMARK 620 6 GLU B 220 OE2 101.7 86.9 86.2 154.9 81.5
REMARK 620 N 1 2 3 4 5
DBREF 6MK0 A 1 954 UNP P06756 ITAV_HUMAN 31 984
DBREF 6MK0 B 4 690 UNP P05106 ITB3_HUMAN 30 716
SEQRES 1 A 954 PHE ASN LEU ASP VAL ASP SER PRO ALA GLU TYR SER GLY
SEQRES 2 A 954 PRO GLU GLY SER TYR PHE GLY PHE ALA VAL ASP PHE PHE
SEQRES 3 A 954 VAL PRO SER ALA SER SER ARG MET PHE LEU LEU VAL GLY
SEQRES 4 A 954 ALA PRO LYS ALA ASN THR THR GLN PRO GLY ILE VAL GLU
SEQRES 5 A 954 GLY GLY GLN VAL LEU LYS CYS ASP TRP SER SER THR ARG
SEQRES 6 A 954 ARG CYS GLN PRO ILE GLU PHE ASP ALA THR GLY ASN ARG
SEQRES 7 A 954 ASP TYR ALA LYS ASP ASP PRO LEU GLU PHE LYS SER HIS
SEQRES 8 A 954 GLN TRP PHE GLY ALA SER VAL ARG SER LYS GLN ASP LYS
SEQRES 9 A 954 ILE LEU ALA CYS ALA PRO LEU TYR HIS TRP ARG THR GLU
SEQRES 10 A 954 MET LYS GLN GLU ARG GLU PRO VAL GLY THR CYS PHE LEU
SEQRES 11 A 954 GLN ASP GLY THR LYS THR VAL GLU TYR ALA PRO CYS ARG
SEQRES 12 A 954 SER GLN ASP ILE ASP ALA ASP GLY GLN GLY PHE CYS GLN
SEQRES 13 A 954 GLY GLY PHE SER ILE ASP PHE THR LYS ALA ASP ARG VAL
SEQRES 14 A 954 LEU LEU GLY GLY PRO GLY SER PHE TYR TRP GLN GLY GLN
SEQRES 15 A 954 LEU ILE SER ASP GLN VAL ALA GLU ILE VAL SER LYS TYR
SEQRES 16 A 954 ASP PRO ASN VAL TYR SER ILE LYS TYR ASN ASN GLN LEU
SEQRES 17 A 954 ALA THR ARG THR ALA GLN ALA ILE PHE ASP ASP SER TYR
SEQRES 18 A 954 LEU GLY TYR SER VAL ALA VAL GLY ASP PHE ASN GLY ASP
SEQRES 19 A 954 GLY ILE ASP ASP PHE VAL SER GLY VAL PRO ARG ALA ALA
SEQRES 20 A 954 ARG THR LEU GLY MET VAL TYR ILE TYR ASP GLY LYS ASN
SEQRES 21 A 954 MET SER SER LEU TYR ASN PHE THR GLY GLU GLN MET ALA
SEQRES 22 A 954 ALA TYR PHE GLY PHE SER VAL ALA ALA THR ASP ILE ASN
SEQRES 23 A 954 GLY ASP ASP TYR ALA ASP VAL PHE ILE GLY ALA PRO LEU
SEQRES 24 A 954 PHE MET ASP ARG GLY SER ASP GLY LYS LEU GLN GLU VAL
SEQRES 25 A 954 GLY GLN VAL SER VAL SER LEU GLN ARG ALA SER GLY ASP
SEQRES 26 A 954 PHE GLN THR THR LYS LEU ASN GLY PHE GLU VAL PHE ALA
SEQRES 27 A 954 ARG PHE GLY SER ALA ILE ALA PRO LEU GLY ASP LEU ASP
SEQRES 28 A 954 GLN ASP GLY PHE ASN ASP ILE ALA ILE ALA ALA PRO TYR
SEQRES 29 A 954 GLY GLY GLU ASP LYS LYS GLY ILE VAL TYR ILE PHE ASN
SEQRES 30 A 954 GLY ARG SER THR GLY LEU ASN ALA VAL PRO SER GLN ILE
SEQRES 31 A 954 LEU GLU GLY GLN TRP ALA ALA ARG SER MET PRO PRO SER
SEQRES 32 A 954 PHE GLY TYR SER MET LYS GLY ALA THR ASP ILE ASP LYS
SEQRES 33 A 954 ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA PHE GLY VAL
SEQRES 34 A 954 ASP ARG ALA ILE LEU TYR ARG ALA ARG PRO VAL ILE THR
SEQRES 35 A 954 VAL ASN ALA GLY LEU GLU VAL TYR PRO SER ILE LEU ASN
SEQRES 36 A 954 GLN ASP ASN LYS THR CYS SER LEU PRO GLY THR ALA LEU
SEQRES 37 A 954 LYS VAL SER CYS PHE ASN VAL ARG PHE CYS LEU LYS ALA
SEQRES 38 A 954 ASP GLY LYS GLY VAL LEU PRO ARG LYS LEU ASN PHE GLN
SEQRES 39 A 954 VAL GLU LEU LEU LEU ASP LYS LEU LYS GLN LYS GLY ALA
SEQRES 40 A 954 ILE ARG ARG ALA LEU PHE LEU TYR SER ARG SER PRO SER
SEQRES 41 A 954 HIS SER LYS ASN MET THR ILE SER ARG GLY GLY LEU MET
SEQRES 42 A 954 GLN CYS GLU GLU LEU ILE ALA TYR LEU ARG ASP GLU SER
SEQRES 43 A 954 GLU PHE ARG ASP LYS LEU THR PRO ILE THR ILE PHE MET
SEQRES 44 A 954 GLU TYR ARG LEU ASP TYR ARG THR ALA ALA ASP THR THR
SEQRES 45 A 954 GLY LEU GLN PRO ILE LEU ASN GLN PHE THR PRO ALA ASN
SEQRES 46 A 954 ILE SER ARG GLN ALA HIS ILE LEU LEU ASP CYS GLY GLU
SEQRES 47 A 954 ASP ASN VAL CYS LYS PRO LYS LEU GLU VAL SER VAL ASP
SEQRES 48 A 954 SER ASP GLN LYS LYS ILE TYR ILE GLY ASP ASP ASN PRO
SEQRES 49 A 954 LEU THR LEU ILE VAL LYS ALA GLN ASN GLN GLY GLU GLY
SEQRES 50 A 954 ALA TYR GLU ALA GLU LEU ILE VAL SER ILE PRO LEU GLN
SEQRES 51 A 954 ALA ASP PHE ILE GLY VAL VAL ARG ASN ASN GLU ALA LEU
SEQRES 52 A 954 ALA ARG LEU SER CYS ALA PHE LYS THR GLU ASN GLN THR
SEQRES 53 A 954 ARG GLN VAL VAL CYS ASP LEU GLY ASN PRO MET LYS ALA
SEQRES 54 A 954 GLY THR GLN LEU LEU ALA GLY LEU ARG PHE SER VAL HIS
SEQRES 55 A 954 GLN GLN SER GLU MET ASP THR SER VAL LYS PHE ASP LEU
SEQRES 56 A 954 GLN ILE GLN SER SER ASN LEU PHE ASP LYS VAL SER PRO
SEQRES 57 A 954 VAL VAL SER HIS LYS VAL ASP LEU ALA VAL LEU ALA ALA
SEQRES 58 A 954 VAL GLU ILE ARG GLY VAL SER SER PRO ASP HIS VAL PHE
SEQRES 59 A 954 LEU PRO ILE PRO ASN TRP GLU HIS LYS GLU ASN PRO GLU
SEQRES 60 A 954 THR GLU GLU ASP VAL GLY PRO VAL VAL GLN HIS ILE TYR
SEQRES 61 A 954 GLU LEU ARG ASN ASN GLY PRO SER SER PHE SER LYS ALA
SEQRES 62 A 954 MET LEU HIS LEU GLN TRP PRO TYR LYS TYR ASN ASN ASN
SEQRES 63 A 954 THR LEU LEU TYR ILE LEU HIS TYR ASP ILE ASP GLY PRO
SEQRES 64 A 954 MET ASN CYS THR SER ASP MET GLU ILE ASN PRO LEU ARG
SEQRES 65 A 954 ILE LYS ILE SER SER LEU GLN THR THR GLU LYS ASN ASP
SEQRES 66 A 954 THR VAL ALA GLY GLN GLY GLU ARG ASP HIS LEU ILE THR
SEQRES 67 A 954 LYS ARG ASP LEU ALA LEU SER GLU GLY ASP ILE HIS THR
SEQRES 68 A 954 LEU GLY CYS GLY VAL ALA GLN CYS LEU LYS ILE VAL CYS
SEQRES 69 A 954 GLN VAL GLY ARG LEU ASP ARG GLY LYS SER ALA ILE LEU
SEQRES 70 A 954 TYR VAL LYS SER LEU LEU TRP THR GLU THR PHE MET ASN
SEQRES 71 A 954 LYS GLU ASN GLN ASN HIS SER TYR SER LEU LYS SER SER
SEQRES 72 A 954 ALA SER PHE ASN VAL ILE GLU PHE PRO TYR LYS ASN LEU
SEQRES 73 A 954 PRO ILE GLU ASP ILE THR ASN SER THR LEU VAL THR THR
SEQRES 74 A 954 ASN VAL THR TRP GLY
SEQRES 1 B 687 ILE CYS THR THR ARG GLY VAL SER SER CYS GLN GLN CYS
SEQRES 2 B 687 LEU ALA VAL SER PRO MET CYS ALA TRP CYS SER ASP GLU
SEQRES 3 B 687 ALA LEU PRO LEU GLY SER PRO ARG CYS ASP LEU LYS GLU
SEQRES 4 B 687 ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU SER ILE GLU
SEQRES 5 B 687 PHE PRO VAL SER GLU ALA ARG VAL LEU GLU ASP ARG PRO
SEQRES 6 B 687 LEU SER ASP LYS GLY SER GLY ASP SER SER GLN VAL THR
SEQRES 7 B 687 GLN VAL SER PRO GLN ARG ILE ALA LEU ARG LEU ARG PRO
SEQRES 8 B 687 ASP ASP SER LYS ASN PHE SER ILE GLN VAL ARG GLN VAL
SEQRES 9 B 687 GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU MET ASP LEU
SEQRES 10 B 687 SER TYR SER MET LYS ASP ASP LEU TRP SER ILE GLN ASN
SEQRES 11 B 687 LEU GLY THR LYS LEU ALA THR GLN MET ARG LYS LEU THR
SEQRES 12 B 687 SER ASN LEU ARG ILE GLY PHE GLY ALA PHE VAL ASP LYS
SEQRES 13 B 687 PRO VAL SER PRO TYR MET TYR ILE SER PRO PRO GLU ALA
SEQRES 14 B 687 LEU GLU ASN PRO CYS TYR ASP MET LYS THR THR CYS LEU
SEQRES 15 B 687 PRO MET PHE GLY TYR LYS HIS VAL LEU THR LEU THR ASP
SEQRES 16 B 687 GLN VAL THR ARG PHE ASN GLU GLU VAL LYS LYS GLN SER
SEQRES 17 B 687 VAL SER ARG ASN ARG ASP ALA PRO GLU GLY GLY PHE ASP
SEQRES 18 B 687 ALA ILE MET GLN ALA THR VAL CYS ASP GLU LYS ILE GLY
SEQRES 19 B 687 TRP ARG ASN ASP ALA SER HIS LEU LEU VAL PHE THR THR
SEQRES 20 B 687 ASP ALA LYS THR HIS ILE ALA LEU ASP GLY ARG LEU ALA
SEQRES 21 B 687 GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS HIS VAL GLY
SEQRES 22 B 687 SER ASP ASN HIS TYR SER ALA SER THR THR MET ASP TYR
SEQRES 23 B 687 PRO SER LEU GLY LEU MET THR GLU LYS LEU SER GLN LYS
SEQRES 24 B 687 ASN ILE ASN LEU ILE PHE ALA VAL THR GLU ASN VAL VAL
SEQRES 25 B 687 ASN LEU TYR GLN ASN TYR SER GLU LEU ILE PRO GLY THR
SEQRES 26 B 687 THR VAL GLY VAL LEU SER MET ASP SER SER ASN VAL LEU
SEQRES 27 B 687 GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE ARG SER LYS
SEQRES 28 B 687 VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU GLU LEU SER
SEQRES 29 B 687 LEU SER PHE ASN ALA THR CYS LEU ASN ASN GLU VAL ILE
SEQRES 30 B 687 PRO GLY LEU LYS SER CYS MET GLY LEU LYS ILE GLY ASP
SEQRES 31 B 687 THR VAL SER PHE SER ILE GLU ALA LYS VAL ARG GLY CYS
SEQRES 32 B 687 PRO GLN GLU LYS GLU LYS SER PHE THR ILE LYS PRO VAL
SEQRES 33 B 687 GLY PHE LYS ASP SER LEU ILE VAL GLN VAL THR PHE ASP
SEQRES 34 B 687 CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU PRO ASN SER
SEQRES 35 B 687 HIS ARG CYS ASN ASN GLY ASN GLY THR PHE GLU CYS GLY
SEQRES 36 B 687 VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY SER GLN CYS
SEQRES 37 B 687 GLU CYS SER GLU GLU ASP TYR ARG PRO SER GLN GLN ASP
SEQRES 38 B 687 GLU CYS SER PRO ARG GLU GLY GLN PRO VAL CYS SER GLN
SEQRES 39 B 687 ARG GLY GLU CYS LEU CYS GLY GLN CYS VAL CYS HIS SER
SEQRES 40 B 687 SER ASP PHE GLY LYS ILE THR GLY LYS TYR CYS GLU CYS
SEQRES 41 B 687 ASP ASP PHE SER CYS VAL ARG TYR LYS GLY GLU MET CYS
SEQRES 42 B 687 SER GLY HIS GLY GLN CYS SER CYS GLY ASP CYS LEU CYS
SEQRES 43 B 687 ASP SER ASP TRP THR GLY TYR TYR CYS ASN CYS THR THR
SEQRES 44 B 687 ARG THR ASP THR CYS MET SER SER ASN GLY LEU LEU CYS
SEQRES 45 B 687 SER GLY ARG GLY LYS CYS GLU CYS GLY SER CYS VAL CYS
SEQRES 46 B 687 ILE GLN PRO GLY SER TYR GLY ASP THR CYS GLU LYS CYS
SEQRES 47 B 687 PRO THR CYS PRO ASP ALA CYS THR PHE LYS LYS GLU CYS
SEQRES 48 B 687 VAL GLU CYS LYS LYS PHE ASP ARG GLY ALA LEU HIS ASP
SEQRES 49 B 687 GLU ASN THR CYS ASN ARG TYR CYS ARG ASP GLU ILE GLU
SEQRES 50 B 687 SER VAL LYS GLU LEU LYS ASP THR GLY LYS ASP ALA VAL
SEQRES 51 B 687 ASN CYS THR TYR LYS ASN GLU ASP ASP CYS VAL VAL ARG
SEQRES 52 B 687 PHE GLN TYR TYR GLU ASP SER SER GLY LYS SER ILE LEU
SEQRES 53 B 687 TYR VAL VAL GLU GLU PRO GLU CYS PRO LYS GLY
HET NAG C 1 14
HET NAG C 2 14
HET NAG D 1 14
HET NAG D 2 14
HET BMA D 3 11
HET BMA D 4 11
HET MAN D 5 11
HET MAN D 6 11
HET NAG E 1 14
HET NAG E 2 14
HET NAG F 1 14
HET NAG F 2 14
HET NAG G 1 14
HET NAG G 2 14
HET NAG H 1 14
HET NAG H 2 14
HET BMA H 3 11
HET NAG A1003 14
HET NAG A1012 14
HET NAG A1013 14
HET NAG A1016 14
HET NAG A1017 14
HET MN A1018 1
HET MN A1019 1
HET MN A1020 1
HET MN A1021 1
HET MN A1022 1
HET NAG B 701 14
HET NAG B 702 14
HET MN B 708 1
HET MN B 709 1
HET MN B 710 1
HET NAG B 711 14
HET JUY B 712 35
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM MN MANGANESE (II) ION
HETNAM JUY (2S)-2-[(1,3-BENZOTHIAZOLE-2-CARBONYL)AMINO]-4-{[5-(1,
HETNAM 2 JUY 8-NAPHTHYRIDIN-2-YL)PENTANOYL]AMINO}BUTANOIC ACID
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 3 NAG 20(C8 H15 N O6)
FORMUL 4 BMA 3(C6 H12 O6)
FORMUL 4 MAN 2(C6 H12 O6)
FORMUL 14 MN 8(MN 2+)
FORMUL 25 JUY C25 H25 N5 O4 S
FORMUL 26 HOH *4(H2 O)
HELIX 1 AA1 GLY A 175 GLN A 180 1 6
HELIX 2 AA2 VAL A 188 LYS A 194 1 7
HELIX 3 AA3 GLN A 214 ASP A 218 5 5
HELIX 4 AA4 ARG A 245 LEU A 250 1 6
HELIX 5 AA5 ARG A 339 SER A 342 5 4
HELIX 6 AA6 GLY A 366 LYS A 370 5 5
HELIX 7 AA7 SER B 121 SER B 123 5 3
HELIX 8 AA8 MET B 124 ILE B 131 1 8
HELIX 9 AA9 GLY B 135 ARG B 143 1 9
HELIX 10 AB1 PRO B 169 LEU B 173 5 5
HELIX 11 AB2 GLN B 199 VAL B 207 1 9
HELIX 12 AB3 GLY B 222 CYS B 232 1 11
HELIX 13 AB4 CYS B 232 GLY B 237 1 6
HELIX 14 AB5 LEU B 258 GLY B 264 5 7
HELIX 15 AB6 TYR B 281 THR B 286 5 6
HELIX 16 AB7 SER B 291 LYS B 302 1 12
HELIX 17 AB8 VAL B 314 GLU B 323 1 10
HELIX 18 AB9 ASN B 339 ARG B 352 1 14
HELIX 19 AC1 SER B 445 ASN B 449 5 5
HELIX 20 AC2 GLU B 534 GLY B 538 5 5
HELIX 21 AC3 THR B 564 MET B 568 5 5
HELIX 22 AC4 LEU B 573 GLY B 577 5 5
HELIX 23 AC5 ASP B 606 PHE B 620 1 15
HELIX 24 AC6 THR B 630 CYS B 635 1 6
SHEET 1 AA1 4 ALA A 9 SER A 12 0
SHEET 2 AA1 4 ARG A 431 TYR A 435 -1 O ALA A 432 N TYR A 11
SHEET 3 AA1 4 ASP A 421 GLY A 425 -1 N VAL A 424 O ILE A 433
SHEET 4 AA1 4 SER A 407 THR A 412 -1 N LYS A 409 O ILE A 423
SHEET 1 AA2 4 VAL A 23 PHE A 26 0
SHEET 2 AA2 4 PHE A 35 ALA A 40 -1 O LEU A 37 N ASP A 24
SHEET 3 AA2 4 GLN A 55 ASP A 60 -1 O CYS A 59 N LEU A 36
SHEET 4 AA2 4 CYS A 67 PRO A 69 -1 O GLN A 68 N LYS A 58
SHEET 1 AA3 2 ASP A 79 ALA A 81 0
SHEET 2 AA3 2 ASP A 84 PRO A 85 -1 O ASP A 84 N TYR A 80
SHEET 1 AA4 4 VAL A 98 SER A 100 0
SHEET 2 AA4 4 LYS A 104 ALA A 109 -1 O LEU A 106 N ARG A 99
SHEET 3 AA4 4 THR A 127 ASP A 132 -1 O THR A 127 N ALA A 109
SHEET 4 AA4 4 LYS A 135 TYR A 139 -1 O LYS A 135 N ASP A 132
SHEET 1 AA5 4 ILE A 161 PHE A 163 0
SHEET 2 AA5 4 ARG A 168 GLY A 173 -1 O LEU A 170 N ASP A 162
SHEET 3 AA5 4 GLN A 182 GLN A 187 -1 O ILE A 184 N LEU A 171
SHEET 4 AA5 4 LEU A 208 ALA A 209 -1 O LEU A 208 N SER A 185
SHEET 1 AA6 4 VAL A 226 GLY A 229 0
SHEET 2 AA6 4 ASP A 238 VAL A 243 -1 O ASP A 238 N GLY A 229
SHEET 3 AA6 4 MET A 252 TYR A 256 -1 O MET A 252 N VAL A 243
SHEET 4 AA6 4 SER A 263 THR A 268 -1 O LEU A 264 N ILE A 255
SHEET 1 AA7 4 VAL A 280 THR A 283 0
SHEET 2 AA7 4 ASP A 292 ALA A 297 -1 O PHE A 294 N ALA A 281
SHEET 3 AA7 4 GLN A 314 ARG A 321 -1 O SER A 318 N VAL A 293
SHEET 4 AA7 4 GLY A 324 ASN A 332 -1 O THR A 329 N VAL A 317
SHEET 1 AA8 2 MET A 301 ARG A 303 0
SHEET 2 AA8 2 LEU A 309 GLU A 311 -1 O GLN A 310 N ASP A 302
SHEET 1 AA9 4 ALA A 343 PRO A 346 0
SHEET 2 AA9 4 ILE A 358 ALA A 362 -1 O ALA A 359 N ALA A 345
SHEET 3 AA9 4 ILE A 372 PHE A 376 -1 O TYR A 374 N ILE A 360
SHEET 4 AA9 4 GLN A 389 GLU A 392 -1 O LEU A 391 N VAL A 373
SHEET 1 AB1 2 GLY A 378 ARG A 379 0
SHEET 2 AB1 2 GLY A 382 LEU A 383 -1 O GLY A 382 N ARG A 379
SHEET 1 AB2 4 LEU A 447 TYR A 450 0
SHEET 2 AB2 4 CYS A 472 ASP A 482 -1 O ASN A 474 N TYR A 450
SHEET 3 AB2 4 GLN A 534 LEU A 542 -1 O ALA A 540 N PHE A 473
SHEET 4 AB2 4 ALA A 511 PHE A 513 -1 N LEU A 512 O TYR A 541
SHEET 1 AB3 4 LEU A 447 TYR A 450 0
SHEET 2 AB3 4 CYS A 472 ASP A 482 -1 O ASN A 474 N TYR A 450
SHEET 3 AB3 4 VAL A 440 ASN A 444 -1 N THR A 442 O ASP A 482
SHEET 4 AB3 4 ILE A 577 LEU A 578 1 O ILE A 577 N ILE A 441
SHEET 1 AB4 5 ILE A 453 LEU A 454 0
SHEET 2 AB4 5 ASN A 585 ILE A 592 1 O HIS A 591 N LEU A 454
SHEET 3 AB4 5 ILE A 555 LEU A 563 -1 N ILE A 555 O ALA A 590
SHEET 4 AB4 5 LYS A 490 LEU A 499 -1 N GLU A 496 O GLU A 560
SHEET 5 AB4 5 SER A 520 SER A 528 -1 O ILE A 527 N LEU A 491
SHEET 1 AB5 2 CYS A 461 SER A 462 0
SHEET 2 AB5 2 LYS A 469 VAL A 470 -1 O VAL A 470 N CYS A 461
SHEET 1 AB6 3 LEU A 606 VAL A 610 0
SHEET 2 AB6 3 PRO A 624 ASN A 633 -1 O LYS A 630 N SER A 609
SHEET 3 AB6 3 GLY A 690 SER A 700 -1 O ALA A 695 N VAL A 629
SHEET 1 AB7 3 LYS A 616 TYR A 618 0
SHEET 2 AB7 3 VAL A 734 ALA A 737 1 O ALA A 737 N ILE A 617
SHEET 3 AB7 3 SER A 710 VAL A 711 -1 N VAL A 711 O VAL A 734
SHEET 1 AB8 5 CYS A 668 LYS A 671 0
SHEET 2 AB8 5 GLN A 678 GLY A 684 -1 O VAL A 680 N ALA A 669
SHEET 3 AB8 5 ALA A 641 SER A 646 -1 N VAL A 645 O VAL A 679
SHEET 4 AB8 5 ASP A 714 GLN A 718 -1 O ASP A 714 N SER A 646
SHEET 5 AB8 5 VAL A 730 SER A 731 -1 O VAL A 730 N LEU A 715
SHEET 1 AB9 4 VAL A 742 SER A 749 0
SHEET 2 AB9 4 VAL A 775 ASN A 784 -1 O GLU A 781 N ARG A 745
SHEET 3 AB9 4 SER A 894 LEU A 903 -1 O ALA A 895 N LEU A 782
SHEET 4 AB9 4 LEU A 809 ASP A 817 -1 N HIS A 813 O LYS A 900
SHEET 1 AC1 6 HIS A 752 LEU A 755 0
SHEET 2 AC1 6 THR A 942 TRP A 953 1 O THR A 952 N LEU A 755
SHEET 3 AC1 6 TYR A 918 GLU A 930 -1 N SER A 922 O VAL A 947
SHEET 4 AC1 6 LYS A 792 LYS A 802 -1 N HIS A 796 O SER A 925
SHEET 5 AC1 6 GLN A 878 VAL A 886 -1 O VAL A 886 N ALA A 793
SHEET 6 AC1 6 MET A 820 SER A 824 -1 N ASN A 821 O GLN A 885
SHEET 1 AC2 4 HIS A 752 LEU A 755 0
SHEET 2 AC2 4 THR A 942 TRP A 953 1 O THR A 952 N LEU A 755
SHEET 3 AC2 4 TYR A 918 GLU A 930 -1 N SER A 922 O VAL A 947
SHEET 4 AC2 4 THR A 871 LEU A 872 1 N LEU A 872 O LYS A 921
SHEET 1 AC3 6 VAL B 63 GLU B 65 0
SHEET 2 AC3 6 ARG B 87 LEU B 92 -1 O ARG B 87 N LEU B 64
SHEET 3 AC3 6 LEU B 425 PHE B 431 1 O GLN B 428 N LEU B 90
SHEET 4 AC3 6 SER B 413 PRO B 418 -1 N ILE B 416 O LEU B 425
SHEET 5 AC3 6 VAL B 355 ARG B 360 -1 N GLU B 358 O LYS B 417
SHEET 6 AC3 6 SER B 385 CYS B 386 -1 O CYS B 386 N VAL B 355
SHEET 1 AC4 5 VAL B 83 SER B 84 0
SHEET 2 AC4 5 SER B 97 ARG B 105 -1 O GLN B 103 N SER B 84
SHEET 3 AC4 5 THR B 394 VAL B 403 -1 O ILE B 399 N PHE B 100
SHEET 4 AC4 5 LEU B 366 THR B 373 -1 N THR B 373 O SER B 396
SHEET 5 AC4 5 VAL B 379 PRO B 381 -1 O ILE B 380 N ALA B 372
SHEET 1 AC5 6 TYR B 190 THR B 197 0
SHEET 2 AC5 6 LEU B 149 PHE B 156 -1 N ALA B 155 O LYS B 191
SHEET 3 AC5 6 VAL B 112 ASP B 119 1 N MET B 118 O GLY B 154
SHEET 4 AC5 6 SER B 243 THR B 250 1 O LEU B 245 N TYR B 115
SHEET 5 AC5 6 ILE B 304 THR B 311 1 O ALA B 309 N PHE B 248
SHEET 6 AC5 6 THR B 329 LEU B 333 1 O GLY B 331 N PHE B 308
SHEET 1 AC6 2 ILE B 516 THR B 517 0
SHEET 2 AC6 2 CYS B 523 ASP B 524 -1 O CYS B 523 N THR B 517
SHEET 1 AC7 2 GLY B 540 SER B 543 0
SHEET 2 AC7 2 ASP B 546 CYS B 549 -1 O ASP B 546 N SER B 543
SHEET 1 AC8 2 TRP B 553 THR B 554 0
SHEET 2 AC8 2 CYS B 560 THR B 561 -1 O CYS B 560 N THR B 554
SHEET 1 AC9 2 GLY B 579 GLU B 582 0
SHEET 2 AC9 2 SER B 585 CYS B 588 -1 O VAL B 587 N LYS B 580
SHEET 1 AD1 4 GLU B 638 VAL B 642 0
SHEET 2 AD1 4 SER B 677 VAL B 682 1 O LEU B 679 N GLU B 638
SHEET 3 AD1 4 VAL B 664 GLU B 671 -1 N ARG B 666 O VAL B 682
SHEET 4 AD1 4 ALA B 652 LYS B 658 -1 N TYR B 657 O VAL B 665
SSBOND 1 CYS A 59 CYS A 67 1555 1555 2.04
SSBOND 2 CYS A 108 CYS A 128 1555 1555 2.03
SSBOND 3 CYS A 142 CYS A 155 1555 1555 2.04
SSBOND 4 CYS A 461 CYS A 472 1555 1555 2.03
SSBOND 5 CYS A 478 CYS A 535 1555 1555 2.04
SSBOND 6 CYS A 596 CYS A 602 1555 1555 2.03
SSBOND 7 CYS A 668 CYS A 681 1555 1555 2.04
SSBOND 8 CYS A 822 CYS A 884 1555 1555 2.04
SSBOND 9 CYS A 874 CYS A 879 1555 1555 2.03
SSBOND 10 CYS B 5 CYS B 23 1555 1555 2.03
SSBOND 11 CYS B 13 CYS B 435 1555 1555 2.03
SSBOND 12 CYS B 16 CYS B 38 1555 1555 2.03
SSBOND 13 CYS B 26 CYS B 49 1555 1555 2.04
SSBOND 14 CYS B 177 CYS B 184 1555 1555 2.04
SSBOND 15 CYS B 232 CYS B 273 1555 1555 2.04
SSBOND 16 CYS B 374 CYS B 386 1555 1555 2.03
SSBOND 17 CYS B 406 CYS B 433 1555 1555 2.03
SSBOND 18 CYS B 437 CYS B 457 1555 1555 2.03
SSBOND 19 CYS B 448 CYS B 460 1555 1555 2.03
SSBOND 20 CYS B 462 CYS B 471 1555 1555 2.03
SSBOND 21 CYS B 473 CYS B 503 1555 1555 2.03
SSBOND 22 CYS B 486 CYS B 501 1555 1555 2.03
SSBOND 23 CYS B 495 CYS B 506 1555 1555 2.04
SSBOND 24 CYS B 508 CYS B 521 1555 1555 2.04
SSBOND 25 CYS B 523 CYS B 544 1555 1555 2.03
SSBOND 26 CYS B 528 CYS B 542 1555 1555 2.03
SSBOND 27 CYS B 536 CYS B 547 1555 1555 2.04
SSBOND 28 CYS B 549 CYS B 558 1555 1555 2.03
SSBOND 29 CYS B 560 CYS B 583 1555 1555 2.03
SSBOND 30 CYS B 567 CYS B 581 1555 1555 2.03
SSBOND 31 CYS B 575 CYS B 586 1555 1555 2.04
SSBOND 32 CYS B 588 CYS B 598 1555 1555 2.04
SSBOND 33 CYS B 601 CYS B 604 1555 1555 2.03
SSBOND 34 CYS B 608 CYS B 655 1555 1555 2.03
SSBOND 35 CYS B 614 CYS B 635 1555 1555 2.03
SSBOND 36 CYS B 617 CYS B 631 1555 1555 2.04
SSBOND 37 CYS B 663 CYS B 687 1555 1555 2.04
LINK ND2 ASN A 44 C1 NAG C 1 1555 1555 1.46
LINK ND2 ASN A 260 C1 NAG A1003 1555 1555 1.45
LINK ND2 ASN A 266 C1 NAG D 1 1555 1555 1.42
LINK ND2 ASN A 458 C1 NAG E 1 1555 1555 1.42
LINK ND2 ASN A 585 C1 NAG A1012 1555 1555 1.43
LINK ND2 ASN A 805 C1 NAG A1013 1555 1555 1.46
LINK ND2 ASN A 821 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN A 943 C1 NAG A1016 1555 1555 1.46
LINK ND2 ASN A 950 C1 NAG A1017 1555 1555 1.46
LINK ND2 ASN B 99 C1 NAG B 701 1555 1555 1.45
LINK ND2 ASN B 320 C1 NAG B 702 1555 1555 1.48
LINK ND2 ASN B 371 C1 NAG G 1 1555 1555 1.49
LINK ND2 ASN B 559 C1 NAG H 1 1555 1555 1.47
LINK ND2 ASN B 654 C1 NAG B 711 1555 1555 1.46
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.42
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.41
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.43
LINK O6 BMA D 3 C1 BMA D 4 1555 1555 1.45
LINK O3 BMA D 3 C1 MAN D 6 1555 1555 1.44
LINK O4 BMA D 4 C1 MAN D 5 1555 1555 1.46
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.43
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.46
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.47
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.45
LINK O4 NAG H 2 C1 BMA H 3 1555 1555 1.44
LINK OD1 ASP A 230 MN MN A1018 1555 1555 2.18
LINK OD1 ASN A 232 MN MN A1018 1555 1555 2.18
LINK OD1 ASP A 234 MN MN A1018 1555 1555 2.24
LINK OD2 ASP A 234 MN MN A1018 1555 1555 2.30
LINK O ILE A 236 MN MN A1018 1555 1555 2.51
LINK OD1 ASP A 238 MN MN A1018 1555 1555 2.16
LINK OD2 ASP A 238 MN MN A1018 1555 1555 2.62
LINK OD1 ASP A 284 MN MN A1019 1555 1555 2.18
LINK OD1 ASN A 286 MN MN A1019 1555 1555 2.14
LINK OD1 ASP A 288 MN MN A1019 1555 1555 2.18
LINK O TYR A 290 MN MN A1019 1555 1555 2.06
LINK OD1 ASP A 292 MN MN A1019 1555 1555 2.17
LINK OD2 ASP A 292 MN MN A1019 1555 1555 2.17
LINK OD1 ASP A 349 MN MN A1020 1555 1555 2.18
LINK OD1 ASP A 351 MN MN A1020 1555 1555 2.16
LINK OD1 ASP A 353 MN MN A1020 1555 1555 2.17
LINK O PHE A 355 MN MN A1020 1555 1555 2.26
LINK OD1 ASP A 357 MN MN A1020 1555 1555 2.17
LINK OD2 ASP A 357 MN MN A1020 1555 1555 2.18
LINK OD1 ASP A 413 MN MN A1021 1555 1555 2.41
LINK OD1 ASP A 415 MN MN A1021 1555 1555 2.19
LINK OD1 ASN A 417 MN MN A1021 1555 1555 2.20
LINK ND2 ASN A 417 MN MN A1021 1555 1555 2.74
LINK O TYR A 419 MN MN A1021 1555 1555 2.09
LINK OD1 ASP A 421 MN MN A1021 1555 1555 2.19
LINK OD2 ASP A 421 MN MN A1021 1555 1555 2.20
LINK O CYS A 596 MN MN A1022 1555 1555 2.33
LINK OD1 ASP A 599 MN MN A1022 1555 1555 2.14
LINK OD2 ASP A 599 MN MN A1022 1555 1555 2.17
LINK O VAL A 601 MN MN A1022 1555 1555 2.37
LINK OE1 GLU A 636 MN MN A1022 1555 1555 2.17
LINK OE2 GLU A 636 MN MN A1022 1555 1555 2.15
LINK OG SER B 121 MN MN B 708 1555 1555 2.17
LINK O SER B 123 MN MN B 709 1555 1555 2.70
LINK OD1 ASP B 126 MN MN B 709 1555 1555 2.27
LINK OD2 ASP B 126 MN MN B 709 1555 1555 2.36
LINK OD1 ASP B 127 MN MN B 709 1555 1555 2.41
LINK OD2 ASP B 158 MN MN B 710 1555 1555 2.15
LINK OD1 ASN B 215 MN MN B 710 1555 1555 2.04
LINK O ASP B 217 MN MN B 710 1555 1555 2.53
LINK OD1 ASP B 217 MN MN B 710 1555 1555 2.15
LINK O PRO B 219 MN MN B 710 1555 1555 2.10
LINK OE1 GLU B 220 MN MN B 708 1555 1555 2.19
LINK OE2 GLU B 220 MN MN B 710 1555 1555 2.17
LINK O MET B 335 MN MN B 709 1555 1555 2.35
LINK MN MN B 708 O03 JUY B 712 1555 1555 2.13
LINK MN MN B 708 O HOH B 801 1555 1555 2.25
LINK MN MN B 708 O HOH B 802 1555 1555 2.22
LINK MN MN B 708 O HOH B 804 1555 1555 2.30
LINK MN MN B 709 O HOH B 803 1555 1555 2.40
CISPEP 1 TYR A 450 PRO A 451 0 -10.46
CISPEP 2 ASN A 685 PRO A 686 0 1.56
CISPEP 3 SER A 749 PRO A 750 0 -1.06
CISPEP 4 LEU A 755 PRO A 756 0 0.54
CISPEP 5 SER B 84 PRO B 85 0 -0.73
CISPEP 6 SER B 162 PRO B 163 0 5.58
CISPEP 7 SER B 168 PRO B 169 0 1.17
CRYST1 129.406 129.406 305.535 90.00 90.00 120.00 P 32 2 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 0.007728 0.004462 0.000000 0.00000
SCALE2 0.000000 0.008923 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003273 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
