HEADER CELL ADHESION 14-AUG-16 5SZL
TITLE PROTOCADHERIN GAMMA A1 EXTRACELLULAR CADHERIN DOMAINS 1-4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTOCADHERIN GAMMA A1 EXTRACELLULAR CADHERIN DOMAINS 1-4,
COMPND 3 PROTEIN PCDHGA1;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PCDHGA1;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293F
KEYWDS CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR K.M.GOODMAN,F.BAHNA,S.MANNEPALLI,B.HONIG,L.SHAPIRO
REVDAT 6 04-OCT-23 5SZL 1 HETSYN LINK
REVDAT 5 29-JUL-20 5SZL 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 25-DEC-19 5SZL 1 REMARK
REVDAT 3 20-SEP-17 5SZL 1 REMARK
REVDAT 2 09-NOV-16 5SZL 1 JRNL
REVDAT 1 19-OCT-16 5SZL 0
JRNL AUTH K.M.GOODMAN,R.RUBINSTEIN,C.A.THU,S.MANNEPALLI,F.BAHNA,
JRNL AUTH 2 G.AHLSEN,C.RITTENHOUSE,T.MANIATIS,B.HONIG,L.SHAPIRO
JRNL TITL GAMMA-PROTOCADHERIN STRUCTURAL DIVERSITY AND FUNCTIONAL
JRNL TITL 2 IMPLICATIONS.
JRNL REF ELIFE V. 5 2016
JRNL REFN ESSN 2050-084X
JRNL PMID 27782885
JRNL DOI 10.7554/ELIFE.20930
REMARK 2
REMARK 2 RESOLUTION. 4.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 4.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.96
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 23652
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.288
REMARK 3 R VALUE (WORKING SET) : 0.287
REMARK 3 FREE R VALUE : 0.314
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1182
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 39.9618 - 8.3774 0.99 3042 133 0.2209 0.2264
REMARK 3 2 8.3774 - 6.6594 1.00 2872 148 0.2913 0.3207
REMARK 3 3 6.6594 - 5.8205 1.00 2846 135 0.3092 0.3384
REMARK 3 4 5.8205 - 5.2896 1.00 2814 148 0.3109 0.3447
REMARK 3 5 5.2896 - 4.9112 1.00 2751 143 0.3078 0.3367
REMARK 3 6 4.9112 - 4.6221 0.99 2807 142 0.3443 0.4017
REMARK 3 7 4.6221 - 4.3909 0.99 2726 162 0.3656 0.4002
REMARK 3 8 4.3909 - 4.2000 0.96 2612 171 0.3685 0.4161
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.810
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.070
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 133.8
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 : 0.004 12722
REMARK 3 ANGLE : 0.822 17450
REMARK 3 CHIRALITY : 0.054 2112
REMARK 3 PLANARITY : 0.005 2332
REMARK 3 DIHEDRAL : 11.669 7767
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 2:98 )
REMARK 3 ORIGIN FOR THE GROUP (A): 69.9907 73.7472 110.9653
REMARK 3 T TENSOR
REMARK 3 T11: 2.7241 T22: 1.6569
REMARK 3 T33: 2.3569 T12: 0.0662
REMARK 3 T13: -0.5288 T23: -0.3709
REMARK 3 L TENSOR
REMARK 3 L11: 0.0375 L22: 0.0105
REMARK 3 L33: 0.0177 L12: -0.0291
REMARK 3 L13: 0.0060 L23: -0.0317
REMARK 3 S TENSOR
REMARK 3 S11: 0.5170 S12: -0.2132 S13: 0.6457
REMARK 3 S21: -0.0514 S22: 0.3854 S23: -0.4214
REMARK 3 S31: 0.0111 S32: 0.1256 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN B AND RESID 2:98 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.8850 0.8301 35.2583
REMARK 3 T TENSOR
REMARK 3 T11: 2.1910 T22: 2.2320
REMARK 3 T33: 2.2804 T12: -0.1180
REMARK 3 T13: -0.5156 T23: -0.3051
REMARK 3 L TENSOR
REMARK 3 L11: -0.0205 L22: -0.0006
REMARK 3 L33: 0.0331 L12: 0.0791
REMARK 3 L13: -0.0154 L23: -0.1082
REMARK 3 S TENSOR
REMARK 3 S11: 0.2178 S12: 0.2411 S13: -0.2533
REMARK 3 S21: -0.1460 S22: -0.0242 S23: 0.3502
REMARK 3 S31: -0.0746 S32: 0.0306 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN C AND RESID 2:98 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.4848 48.4909 -8.8076
REMARK 3 T TENSOR
REMARK 3 T11: 1.5874 T22: 2.0899
REMARK 3 T33: 1.2379 T12: 0.2905
REMARK 3 T13: -0.1083 T23: 0.1558
REMARK 3 L TENSOR
REMARK 3 L11: 0.0552 L22: 0.0275
REMARK 3 L33: 0.0649 L12: 0.0925
REMARK 3 L13: -0.0359 L23: -0.1648
REMARK 3 S TENSOR
REMARK 3 S11: 0.1165 S12: 0.6798 S13: -0.1120
REMARK 3 S21: 0.1021 S22: -0.1339 S23: -0.1313
REMARK 3 S31: -0.2440 S32: -0.3881 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN D AND RESID 2:98 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3439 54.1856 130.1291
REMARK 3 T TENSOR
REMARK 3 T11: 2.9682 T22: 1.5728
REMARK 3 T33: 1.3386 T12: 0.0460
REMARK 3 T13: 0.1315 T23: -0.3359
REMARK 3 L TENSOR
REMARK 3 L11: -0.0187 L22: -0.0482
REMARK 3 L33: 0.0532 L12: 0.0913
REMARK 3 L13: 0.0563 L23: -0.0391
REMARK 3 S TENSOR
REMARK 3 S11: -1.0765 S12: 0.3113 S13: 0.2243
REMARK 3 S21: 0.0663 S22: 0.1978 S23: -0.2543
REMARK 3 S31: 0.0691 S32: -0.2472 S33: -0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN A AND RESID 99:207 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.0665 53.7700 81.8585
REMARK 3 T TENSOR
REMARK 3 T11: 1.3784 T22: 0.9731
REMARK 3 T33: 1.2814 T12: 0.2796
REMARK 3 T13: -0.1304 T23: -0.2176
REMARK 3 L TENSOR
REMARK 3 L11: 0.1737 L22: 0.1962
REMARK 3 L33: 0.1793 L12: -0.0233
REMARK 3 L13: -0.0252 L23: -0.2664
REMARK 3 S TENSOR
REMARK 3 S11: -0.1955 S12: 0.1479 S13: -0.4054
REMARK 3 S21: 0.1181 S22: 0.1302 S23: -0.3646
REMARK 3 S31: -0.2324 S32: 0.1092 S33: -0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN B AND RESID 99:207 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.4651 21.8809 63.2482
REMARK 3 T TENSOR
REMARK 3 T11: 1.5065 T22: 1.2959
REMARK 3 T33: 1.2528 T12: 0.0110
REMARK 3 T13: -0.1010 T23: -0.3181
REMARK 3 L TENSOR
REMARK 3 L11: 0.3442 L22: 0.2781
REMARK 3 L33: 0.1515 L12: -0.0992
REMARK 3 L13: -0.1623 L23: -0.1495
REMARK 3 S TENSOR
REMARK 3 S11: -0.4222 S12: 0.1688 S13: -0.0460
REMARK 3 S21: 0.6713 S22: 0.2989 S23: 0.0803
REMARK 3 S31: 0.3776 S32: -0.2309 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ( CHAIN C AND RESID 99:207 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1069 48.1560 35.1450
REMARK 3 T TENSOR
REMARK 3 T11: 1.4540 T22: 0.9619
REMARK 3 T33: 1.3406 T12: 0.2268
REMARK 3 T13: -0.0914 T23: -0.0471
REMARK 3 L TENSOR
REMARK 3 L11: 0.1628 L22: 0.3655
REMARK 3 L33: 0.0935 L12: -0.1919
REMARK 3 L13: -0.2289 L23: -0.1070
REMARK 3 S TENSOR
REMARK 3 S11: -0.3363 S12: 0.0430 S13: 0.2750
REMARK 3 S21: -0.2480 S22: 0.2986 S23: 0.2357
REMARK 3 S31: -0.0122 S32: -0.0438 S33: -0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: ( CHAIN D AND RESID 99:207 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.0255 46.1948 86.6191
REMARK 3 T TENSOR
REMARK 3 T11: 1.5827 T22: 1.3191
REMARK 3 T33: 1.2898 T12: 0.1040
REMARK 3 T13: -0.0711 T23: -0.2583
REMARK 3 L TENSOR
REMARK 3 L11: 0.3721 L22: 0.2204
REMARK 3 L33: 0.0775 L12: -0.0611
REMARK 3 L13: -0.0636 L23: 0.0229
REMARK 3 S TENSOR
REMARK 3 S11: 0.4589 S12: -0.1361 S13: 0.7208
REMARK 3 S21: 0.4572 S22: -0.0446 S23: 0.2350
REMARK 3 S31: 1.1159 S32: -0.1075 S33: 0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: ( CHAIN A AND RESID 208:312 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.6895 24.7057 46.6210
REMARK 3 T TENSOR
REMARK 3 T11: 1.3233 T22: 0.9457
REMARK 3 T33: 0.8614 T12: 0.7222
REMARK 3 T13: -0.1834 T23: -0.0872
REMARK 3 L TENSOR
REMARK 3 L11: 0.2146 L22: -0.0982
REMARK 3 L33: 0.1306 L12: 0.1008
REMARK 3 L13: -0.1034 L23: -0.0328
REMARK 3 S TENSOR
REMARK 3 S11: 0.7656 S12: 0.1364 S13: 0.0160
REMARK 3 S21: -0.3125 S22: -0.5624 S23: -0.2464
REMARK 3 S31: 0.0920 S32: 0.5522 S33: 0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: ( CHAIN B AND RESID 208:312 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.6078 37.7107 96.5637
REMARK 3 T TENSOR
REMARK 3 T11: -1.0848 T22: -4.4486
REMARK 3 T33: 0.9464 T12: 4.1606
REMARK 3 T13: 0.4359 T23: -1.7493
REMARK 3 L TENSOR
REMARK 3 L11: -0.0221 L22: -0.1796
REMARK 3 L33: 0.0467 L12: -0.1037
REMARK 3 L13: 0.0375 L23: 0.1223
REMARK 3 S TENSOR
REMARK 3 S11: -0.0023 S12: -0.0807 S13: -0.2162
REMARK 3 S21: -0.1942 S22: 0.7789 S23: 0.2053
REMARK 3 S31: -0.0044 S32: -0.2105 S33: 0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: ( CHAIN C AND RESID 208:312 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.3314 62.0804 84.0466
REMARK 3 T TENSOR
REMARK 3 T11: 1.2064 T22: 0.0457
REMARK 3 T33: 1.0232 T12: 1.1446
REMARK 3 T13: -0.2540 T23: 0.1622
REMARK 3 L TENSOR
REMARK 3 L11: 0.0134 L22: -0.0249
REMARK 3 L33: 0.0559 L12: 0.0075
REMARK 3 L13: -0.0511 L23: 0.0969
REMARK 3 S TENSOR
REMARK 3 S11: -0.3075 S12: 0.7131 S13: -0.1906
REMARK 3 S21: -0.0553 S22: 0.1410 S23: -0.1655
REMARK 3 S31: 0.5435 S32: -0.0345 S33: -0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: ( CHAIN D AND RESID 208:312 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.0408 48.4367 36.6976
REMARK 3 T TENSOR
REMARK 3 T11: 1.7145 T22: 1.1093
REMARK 3 T33: 1.3794 T12: 0.5080
REMARK 3 T13: -0.2326 T23: -0.2355
REMARK 3 L TENSOR
REMARK 3 L11: 0.2166 L22: 0.2727
REMARK 3 L33: 0.0415 L12: 0.0637
REMARK 3 L13: 0.1290 L23: -0.0523
REMARK 3 S TENSOR
REMARK 3 S11: -0.1300 S12: -0.6746 S13: 0.1997
REMARK 3 S21: -0.9443 S22: -0.8837 S23: -0.3379
REMARK 3 S31: -0.0271 S32: -0.0017 S33: -0.0000
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: ( CHAIN A AND RESID 313:414 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.0573 5.6340 13.4279
REMARK 3 T TENSOR
REMARK 3 T11: 1.8722 T22: 1.6005
REMARK 3 T33: 1.6990 T12: 0.0124
REMARK 3 T13: -0.3549 T23: -0.3403
REMARK 3 L TENSOR
REMARK 3 L11: -0.0472 L22: 0.1048
REMARK 3 L33: 0.0943 L12: 0.0756
REMARK 3 L13: 0.2451 L23: -0.2420
REMARK 3 S TENSOR
REMARK 3 S11: 0.2126 S12: 0.4910 S13: 0.5741
REMARK 3 S21: -0.0225 S22: 0.2926 S23: 0.2658
REMARK 3 S31: -0.8186 S32: -0.5468 S33: -0.0000
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: ( CHAIN B AND RESID 313:413 )
REMARK 3 ORIGIN FOR THE GROUP (A): 69.3829 56.2080 128.0153
REMARK 3 T TENSOR
REMARK 3 T11: 3.0588 T22: 1.7280
REMARK 3 T33: 2.7684 T12: 0.1708
REMARK 3 T13: -0.6825 T23: -0.2982
REMARK 3 L TENSOR
REMARK 3 L11: 0.1061 L22: 0.0444
REMARK 3 L33: 0.0986 L12: -0.1533
REMARK 3 L13: -0.2116 L23: 0.0885
REMARK 3 S TENSOR
REMARK 3 S11: 0.5632 S12: 0.7247 S13: -0.7600
REMARK 3 S21: 0.1981 S22: -0.1595 S23: 1.1801
REMARK 3 S31: -0.5575 S32: -0.0653 S33: 0.0000
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: ( CHAIN C AND RESID 313:419 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.9633 70.1768 129.8166
REMARK 3 T TENSOR
REMARK 3 T11: 1.5222 T22: 1.1476
REMARK 3 T33: 0.9797 T12: 0.2445
REMARK 3 T13: -0.1175 T23: 0.2237
REMARK 3 L TENSOR
REMARK 3 L11: 0.4411 L22: 0.0056
REMARK 3 L33: 0.0297 L12: -0.1266
REMARK 3 L13: -0.0698 L23: -0.0689
REMARK 3 S TENSOR
REMARK 3 S11: 0.0386 S12: 0.2677 S13: 0.1107
REMARK 3 S21: -0.3538 S22: 0.1265 S23: -0.0788
REMARK 3 S31: -0.8844 S32: 1.0302 S33: 0.0000
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: ( CHAIN D AND RESID 313:417 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.5560 40.0443 -7.8167
REMARK 3 T TENSOR
REMARK 3 T11: 0.0564 T22: 0.7109
REMARK 3 T33: -5.2870 T12: -0.4051
REMARK 3 T13: -0.9767 T23: -2.4015
REMARK 3 L TENSOR
REMARK 3 L11: -0.3031 L22: -0.0403
REMARK 3 L33: -0.0130 L12: 0.1184
REMARK 3 L13: 0.0062 L23: 0.0766
REMARK 3 S TENSOR
REMARK 3 S11: -0.6357 S12: -0.5462 S13: -0.2833
REMARK 3 S21: 0.0708 S22: 0.0932 S23: 0.2391
REMARK 3 S31: -0.1597 S32: -0.3201 S33: -0.0000
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 5SZL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-16.
REMARK 100 THE DEPOSITION ID IS D_1000223124.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23885
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.200
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.37900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 2.64600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
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: 4ZI9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% (W/V) PEG8000, 16% ETHYLENE GLYCOL,
REMARK 280 20% MORPHEUS AMINO ACIDS (MOLECULAR DIMENSIONS), 0.1 M MORPHEUS
REMARK 280 BUFFER SYSTEM 2 (HEPES/MOPS BUFFER; MOLECULAR DIMENSIONS) PH 7.0,
REMARK 280 BATCH MODE, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 154.36033
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 308.72067
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 308.72067
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 154.36033
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 5540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F, G
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 GLY A 1
REMARK 465 THR A 415
REMARK 465 ASP A 416
REMARK 465 ILE A 417
REMARK 465 ASN A 418
REMARK 465 ASP A 419
REMARK 465 HIS A 420
REMARK 465 HIS A 421
REMARK 465 HIS A 422
REMARK 465 HIS A 423
REMARK 465 HIS A 424
REMARK 465 HIS A 425
REMARK 465 HIS A 426
REMARK 465 HIS A 427
REMARK 465 GLY B 1
REMARK 465 VAL B 414
REMARK 465 THR B 415
REMARK 465 ASP B 416
REMARK 465 ILE B 417
REMARK 465 ASN B 418
REMARK 465 ASP B 419
REMARK 465 HIS B 420
REMARK 465 HIS B 421
REMARK 465 HIS B 422
REMARK 465 HIS B 423
REMARK 465 HIS B 424
REMARK 465 HIS B 425
REMARK 465 HIS B 426
REMARK 465 HIS B 427
REMARK 465 GLY C 1
REMARK 465 HIS C 420
REMARK 465 HIS C 421
REMARK 465 HIS C 422
REMARK 465 HIS C 423
REMARK 465 HIS C 424
REMARK 465 HIS C 425
REMARK 465 HIS C 426
REMARK 465 HIS C 427
REMARK 465 GLY D 1
REMARK 465 ASN D 418
REMARK 465 ASP D 419
REMARK 465 HIS D 420
REMARK 465 HIS D 421
REMARK 465 HIS D 422
REMARK 465 HIS D 423
REMARK 465 HIS D 424
REMARK 465 HIS D 425
REMARK 465 HIS D 426
REMARK 465 HIS D 427
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ILE A 20 CG1 CG2 CD1
REMARK 470 LYS A 22 CG CD CE NZ
REMARK 470 LEU A 26 CG CD1 CD2
REMARK 470 GLU A 27 CG CD OE1 OE2
REMARK 470 ARG A 29 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 33 CG CD OE1 OE2
REMARK 470 ARG A 43 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 47 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 49 CG CD1 CD2
REMARK 470 ARG A 52 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 56 CG CD1 CD2
REMARK 470 MET A 86 CG SD CE
REMARK 470 LYS A 87 CG CD CE NZ
REMARK 470 LEU A 88 CG CD1 CD2
REMARK 470 LYS A 113 CG CD CE NZ
REMARK 470 LEU A 132 CG CD1 CD2
REMARK 470 GLU A 159 CG CD OE1 OE2
REMARK 470 LEU A 182 CG CD1 CD2
REMARK 470 LYS A 216 CG CD CE NZ
REMARK 470 GLU A 218 CG CD OE1 OE2
REMARK 470 LYS A 255 CG CD CE NZ
REMARK 470 ARG A 262 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 318 CG CD OE1 OE2
REMARK 470 ILE A 321 CG1 CG2 CD1
REMARK 470 VAL A 324 CG1 CG2
REMARK 470 ASN A 326 CG OD1 ND2
REMARK 470 THR A 327 OG1 CG2
REMARK 470 VAL A 328 CG1 CG2
REMARK 470 ASN A 331 CG OD1 ND2
REMARK 470 PHE A 332 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR A 337 OG1 CG2
REMARK 470 ILE A 338 CG1 CG2 CD1
REMARK 470 ILE A 341 CG1 CG2 CD1
REMARK 470 SER A 342 OG
REMARK 470 GLN A 346 CG CD OE1 NE2
REMARK 470 ILE A 358 CG1 CG2 CD1
REMARK 470 LYS A 365 CG CD CE NZ
REMARK 470 LEU A 366 CG CD1 CD2
REMARK 470 ASP A 371 CG OD1 OD2
REMARK 470 ARG A 375 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 376 CG CD1 CD2
REMARK 470 VAL A 377 CG1 CG2
REMARK 470 ARG A 380 CG CD NE CZ NH1 NH2
REMARK 470 THR A 381 OG1 CG2
REMARK 470 LEU A 382 CG CD1 CD2
REMARK 470 GLU A 385 CG CD OE1 OE2
REMARK 470 GLN A 386 CG CD OE1 NE2
REMARK 470 ARG A 389 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 390 CG ND1 CD2 CE1 NE2
REMARK 470 ILE A 394 CG1 CG2 CD1
REMARK 470 GLN A 407 CG CD OE1 NE2
REMARK 470 ILE A 410 CG1 CG2 CD1
REMARK 470 SER A 411 OG
REMARK 470 LEU A 412 CG CD1 CD2
REMARK 470 LEU A 413 CG CD1 CD2
REMARK 470 ILE B 3 CG1 CG2 CD1
REMARK 470 ARG B 29 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 33 CG CD OE1 OE2
REMARK 470 ILE B 36 CG1 CG2 CD1
REMARK 470 ARG B 37 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 38 CG1 CG2 CD1
REMARK 470 ARG B 43 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 45 CG CD OE1 NE2
REMARK 470 VAL B 75 CG1 CG2
REMARK 470 VAL B 76 CG1 CG2
REMARK 470 ILE B 80 CG1 CG2 CD1
REMARK 470 MET B 86 CG SD CE
REMARK 470 LYS B 87 CG CD CE NZ
REMARK 470 LEU B 88 CG CD1 CD2
REMARK 470 LEU B 89 CG CD1 CD2
REMARK 470 GLN B 130 CG CD OE1 NE2
REMARK 470 GLU B 159 CG CD OE1 OE2
REMARK 470 LYS B 176 CG CD CE NZ
REMARK 470 ARG B 248 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 321 CG1 CG2 CD1
REMARK 470 VAL B 324 CG1 CG2
REMARK 470 THR B 325 OG1 CG2
REMARK 470 THR B 327 OG1 CG2
REMARK 470 VAL B 328 CG1 CG2
REMARK 470 ASN B 331 CG OD1 ND2
REMARK 470 PHE B 332 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR B 337 OG1 CG2
REMARK 470 ILE B 338 CG1 CG2 CD1
REMARK 470 ILE B 341 CG1 CG2 CD1
REMARK 470 SER B 342 OG
REMARK 470 GLN B 346 CG CD OE1 NE2
REMARK 470 HIS B 353 CG ND1 CD2 CE1 NE2
REMARK 470 CYS B 356 SG
REMARK 470 SER B 357 OG
REMARK 470 ILE B 358 CG1 CG2 CD1
REMARK 470 PHE B 364 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 365 CG CD CE NZ
REMARK 470 LEU B 366 CG CD1 CD2
REMARK 470 GLU B 367 CG CD OE1 OE2
REMARK 470 VAL B 370 CG1 CG2
REMARK 470 ASP B 371 CG OD1 OD2
REMARK 470 TYR B 374 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG B 375 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 376 CG CD1 CD2
REMARK 470 VAL B 377 CG1 CG2
REMARK 470 GLU B 379 CG CD OE1 OE2
REMARK 470 ARG B 380 CG CD NE CZ NH1 NH2
REMARK 470 THR B 381 OG1 CG2
REMARK 470 LEU B 382 CG CD1 CD2
REMARK 470 ARG B 384 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 385 CG CD OE1 OE2
REMARK 470 GLN B 386 CG CD OE1 NE2
REMARK 470 SER B 387 OG
REMARK 470 SER B 388 OG
REMARK 470 ARG B 389 CG CD NE CZ NH1 NH2
REMARK 470 HIS B 390 CG ND1 CD2 CE1 NE2
REMARK 470 ILE B 392 CG1 CG2 CD1
REMARK 470 ILE B 394 CG1 CG2 CD1
REMARK 470 GLN B 407 CG CD OE1 NE2
REMARK 470 HIS B 409 CG ND1 CD2 CE1 NE2
REMARK 470 ILE B 410 CG1 CG2 CD1
REMARK 470 LEU B 412 CG CD1 CD2
REMARK 470 LEU B 413 CG CD1 CD2
REMARK 470 ARG C 37 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 49 CG CD1 CD2
REMARK 470 LYS C 87 CG CD CE NZ
REMARK 470 LYS C 113 CG CD CE NZ
REMARK 470 GLN C 156 CG CD OE1 NE2
REMARK 470 GLU C 159 CG CD OE1 OE2
REMARK 470 ARG C 170 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 235 CG CD CE NZ
REMARK 470 LYS C 263 CG CD CE NZ
REMARK 470 LYS C 285 CG CD CE NZ
REMARK 470 ILE C 321 CG1 CG2 CD1
REMARK 470 VAL C 324 CG1 CG2
REMARK 470 ASN C 331 CG OD1 ND2
REMARK 470 PHE C 332 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE C 338 CG1 CG2 CD1
REMARK 470 ILE C 354 CG1 CG2 CD1
REMARK 470 ILE C 358 CG1 CG2 CD1
REMARK 470 LYS C 365 CG CD CE NZ
REMARK 470 GLU C 367 CG CD OE1 OE2
REMARK 470 LYS C 368 CG CD CE NZ
REMARK 470 ASP C 371 CG OD1 OD2
REMARK 470 LEU C 376 CG CD1 CD2
REMARK 470 GLU C 379 CG CD OE1 OE2
REMARK 470 ARG C 380 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 385 CG CD OE1 OE2
REMARK 470 GLN C 386 CG CD OE1 NE2
REMARK 470 ILE C 394 CG1 CG2 CD1
REMARK 470 GLN C 407 CG CD OE1 NE2
REMARK 470 HIS C 409 CG ND1 CD2 CE1 NE2
REMARK 470 LEU C 413 CG CD1 CD2
REMARK 470 ILE C 417 CG1 CG2 CD1
REMARK 470 ASN C 418 CG OD1 ND2
REMARK 470 LYS D 13 CG CD CE NZ
REMARK 470 LYS D 22 CG CD CE NZ
REMARK 470 ARG D 37 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 43 CG CD NE CZ NH1 NH2
REMARK 470 ILE D 62 CG1 CG2 CD1
REMARK 470 LYS D 87 CG CD CE NZ
REMARK 470 LEU D 89 CG CD1 CD2
REMARK 470 LYS D 113 CG CD CE NZ
REMARK 470 MET D 114 CG SD CE
REMARK 470 GLN D 155 CG CD OE1 NE2
REMARK 470 GLN D 156 CG CD OE1 NE2
REMARK 470 LYS D 235 CG CD CE NZ
REMARK 470 LYS D 255 CG CD CE NZ
REMARK 470 HIS D 258 CG ND1 CD2 CE1 NE2
REMARK 470 ASN D 331 CG OD1 ND2
REMARK 470 ILE D 341 CG1 CG2 CD1
REMARK 470 GLN D 346 CG CD OE1 NE2
REMARK 470 ASN D 350 CG OD1 ND2
REMARK 470 HIS D 353 CG ND1 CD2 CE1 NE2
REMARK 470 ILE D 354 CG1 CG2 CD1
REMARK 470 ILE D 358 CG1 CG2 CD1
REMARK 470 LEU D 366 CG CD1 CD2
REMARK 470 GLU D 367 CG CD OE1 OE2
REMARK 470 LEU D 369 CG CD1 CD2
REMARK 470 ARG D 375 CG CD NE CZ NH1 NH2
REMARK 470 VAL D 377 CG1 CG2
REMARK 470 ARG D 380 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 384 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 389 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 399 CG CD OE1 NE2
REMARK 470 LEU D 413 CG CD1 CD2
REMARK 470 ILE D 417 CG1 CG2 CD1
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 N ARG D 41 OG SER D 44 2.04
REMARK 500 ND2 ASN D 237 O5 NAG G 1 2.10
REMARK 500 O ILE B 193 O6 MAN B 502 2.19
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 46 CB - CG - CD2 ANGL. DEV. = -13.7 DEGREES
REMARK 500 CYS D 356 CA - CB - SG ANGL. DEV. = -11.7 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 GLU A 27 -166.75 -79.68
REMARK 500 ALA A 69 -96.66 55.90
REMARK 500 GLN A 163 70.21 51.18
REMARK 500 GLN A 169 -77.16 -96.13
REMARK 500 ASP A 188 -150.53 -88.36
REMARK 500 ASN A 208 91.34 -67.37
REMARK 500 ARG A 232 107.82 -57.94
REMARK 500 VAL A 256 -87.09 -116.78
REMARK 500 GLU A 283 -49.39 67.88
REMARK 500 ASP A 295 -149.44 -83.49
REMARK 500 ASP A 349 -148.12 61.96
REMARK 500 LEU A 369 -136.30 -113.81
REMARK 500 ASP A 371 -107.44 54.35
REMARK 500 ALA B 69 -96.84 58.21
REMARK 500 GLN B 169 -77.05 -97.09
REMARK 500 ASP B 188 -150.97 -88.29
REMARK 500 ASN B 208 91.26 -67.05
REMARK 500 ARG B 232 108.86 -58.41
REMARK 500 LYS B 255 96.09 -67.05
REMARK 500 VAL B 256 -91.56 -110.11
REMARK 500 ASP B 295 -150.15 -81.40
REMARK 500 ASP B 349 -149.59 62.50
REMARK 500 ASN B 372 16.80 53.79
REMARK 500 ALA C 69 -96.80 57.60
REMARK 500 GLN C 169 -79.10 -94.51
REMARK 500 ASP C 188 -152.18 -88.84
REMARK 500 ASN C 208 90.02 -69.33
REMARK 500 ARG C 232 109.95 -58.32
REMARK 500 VAL C 256 -82.52 -121.59
REMARK 500 ASP C 295 -149.78 -80.35
REMARK 500 ALA C 297 45.10 -140.11
REMARK 500 ASN C 313 102.00 -59.98
REMARK 500 ASP C 349 -149.61 61.69
REMARK 500 LEU C 369 -159.87 -115.45
REMARK 500 ASP C 371 -111.05 56.08
REMARK 500 ALA D 69 -97.44 57.14
REMARK 500 GLN D 163 71.15 55.51
REMARK 500 GLN D 169 -79.14 -95.62
REMARK 500 ASP D 188 -150.95 -88.70
REMARK 500 ARG D 232 104.30 -55.88
REMARK 500 LYS D 255 94.65 -69.61
REMARK 500 VAL D 256 -87.33 -116.39
REMARK 500 ASP D 295 -150.22 -79.27
REMARK 500 ASP D 349 -148.83 60.60
REMARK 500 ASP D 371 -149.51 62.86
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 CA A 506 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 9 OE2
REMARK 620 2 GLU A 65 OE2 71.4
REMARK 620 3 ASP A 97 OD1 59.8 57.2
REMARK 620 4 ILE A 98 O 71.4 120.0 63.6
REMARK 620 5 ASP A 100 OD1 112.2 127.2 170.5 109.9
REMARK 620 6 ASP A 133 OD1 179.2 109.1 120.9 108.6 67.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 508 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 10 OE2
REMARK 620 2 ASP A 63 OD1 81.8
REMARK 620 3 GLU A 65 OE1 129.5 67.2
REMARK 620 4 ASP A 100 OD2 95.4 163.3 125.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 507 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 99 OD1
REMARK 620 2 ASN A 101 O 92.3
REMARK 620 3 ASP A 131 OD1 140.3 89.4
REMARK 620 4 ASP A 131 OD2 160.0 104.5 52.3
REMARK 620 5 ASP A 133 OD2 62.8 76.7 79.1 131.1
REMARK 620 6 ASN A 137 O 84.8 169.9 86.8 80.4 93.5
REMARK 620 7 ASP A 188 OD2 82.4 88.7 137.3 87.2 141.1 100.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 116 OE1
REMARK 620 2 GLU A 175 OE1 86.3
REMARK 620 3 GLU A 175 OE2 90.6 43.9
REMARK 620 4 ASP A 206 OD1 81.8 130.1 87.8
REMARK 620 5 VAL A 207 O 72.9 125.1 161.8 97.0
REMARK 620 6 ASP A 209 OD1 93.5 62.0 105.3 166.2 69.2
REMARK 620 7 ASP A 242 OD1 168.6 86.3 90.0 109.6 104.7 75.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 505 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 116 OE2
REMARK 620 2 ASP A 173 OD1 115.1
REMARK 620 3 GLU A 175 OE1 73.8 81.1
REMARK 620 4 ASP A 209 OD2 74.5 152.7 77.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 208 OD1
REMARK 620 2 ASN A 210 O 99.1
REMARK 620 3 ASP A 240 OD1 152.2 57.6
REMARK 620 4 ASP A 240 OD2 142.4 96.2 42.3
REMARK 620 5 ASP A 242 OD2 85.6 74.0 74.1 65.9
REMARK 620 6 ASN A 246 O 110.8 147.8 90.3 52.5 96.0
REMARK 620 7 ASP A 295 OD2 80.5 99.4 115.6 130.4 163.5 97.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 509 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 225 OE1
REMARK 620 2 GLU A 282 OE2 117.8
REMARK 620 3 ASP A 311 OD1 92.7 128.2
REMARK 620 4 VAL A 312 O 55.8 140.9 90.7
REMARK 620 5 ASP A 314 OD1 72.9 70.8 160.8 70.8
REMARK 620 6 ASP A 347 OD1 165.6 54.3 101.5 120.8 92.6
REMARK 620 7 ASP A 347 OD2 131.0 89.8 100.6 76.9 80.6 44.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 510 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 225 OE2
REMARK 620 2 ASP A 280 OD1 105.1
REMARK 620 3 GLU A 282 OE1 90.9 69.0
REMARK 620 4 GLU A 282 OE2 103.6 112.7 51.1
REMARK 620 5 ASP A 314 OD1 90.1 157.3 128.6 78.9
REMARK 620 6 ASP A 314 OD2 79.6 115.9 170.1 128.4 49.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 511 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 313 OD1
REMARK 620 2 ASN A 315 O 94.2
REMARK 620 3 ASP A 345 OD1 141.7 62.1
REMARK 620 4 ASP A 345 OD2 123.6 96.7 41.5
REMARK 620 5 ASP A 347 OD2 82.7 104.2 130.0 145.1
REMARK 620 6 ASN A 351 O 94.6 147.2 92.5 52.7 108.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 9 OE2
REMARK 620 2 GLU B 65 OE1 81.8
REMARK 620 3 GLU B 65 OE2 87.2 44.9
REMARK 620 4 ASP B 97 OD1 59.7 109.3 74.2
REMARK 620 5 ILE B 98 O 84.5 165.0 140.4 68.2
REMARK 620 6 ASP B 133 OD1 172.7 96.9 96.9 127.2 96.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 505 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 10 OE2
REMARK 620 2 ASP B 63 OD1 61.6
REMARK 620 3 GLU B 65 OE1 120.9 65.5
REMARK 620 4 ASP B 100 OD1 119.3 173.9 116.1
REMARK 620 5 ASP B 100 OD2 76.8 131.2 162.1 46.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 99 OD1
REMARK 620 2 ASN B 101 O 87.1
REMARK 620 3 ASP B 131 OD1 148.4 108.6
REMARK 620 4 ASP B 131 OD2 155.2 94.3 53.5
REMARK 620 5 ASP B 133 OD2 65.0 89.2 87.3 139.7
REMARK 620 6 ASN B 137 O 97.4 175.2 66.7 82.5 91.0
REMARK 620 7 ASP B 188 OD2 82.4 95.5 121.6 72.9 146.8 87.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 507 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 116 OE1
REMARK 620 2 GLU B 175 OE2 102.0
REMARK 620 3 ASP B 206 OD1 93.4 129.2
REMARK 620 4 VAL B 207 O 81.8 134.1 95.6
REMARK 620 5 ASP B 209 OD1 90.4 69.2 159.5 65.0
REMARK 620 6 ASP B 242 OD1 164.3 70.9 101.9 93.2 74.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 508 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 116 OE2
REMARK 620 2 ASP B 173 OD1 95.9
REMARK 620 3 GLU B 175 OE1 81.2 62.3
REMARK 620 4 ASP B 209 OD2 84.0 178.8 116.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 506 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 208 OD1
REMARK 620 2 ASN B 210 O 110.3
REMARK 620 3 ASP B 240 OD1 148.7 74.6
REMARK 620 4 ASP B 240 OD2 154.1 90.5 50.3
REMARK 620 5 ASP B 242 OD2 76.3 77.2 74.8 124.9
REMARK 620 6 ASN B 246 O 92.6 156.0 82.1 69.9 102.2
REMARK 620 7 ASP B 295 OD2 82.6 100.0 127.9 78.5 156.1 89.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 509 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 225 OE2
REMARK 620 2 ASP B 280 OD1 81.0
REMARK 620 3 GLU B 282 OE2 106.8 86.8
REMARK 620 4 ASP B 314 OD1 72.1 138.9 130.2
REMARK 620 5 ASP B 314 OD2 64.8 96.5 170.2 44.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 510 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 225 OE1
REMARK 620 2 GLU B 225 OE2 47.9
REMARK 620 3 ASP B 311 OD1 93.1 95.1
REMARK 620 4 VAL B 312 O 49.6 96.2 101.2
REMARK 620 5 ASP B 314 OD1 68.1 74.5 161.0 65.0
REMARK 620 6 ASP B 347 OD1 164.9 120.0 97.4 137.4 101.5
REMARK 620 7 ASP B 347 OD2 131.6 149.2 114.9 85.2 78.4 52.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 511 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 313 OD1
REMARK 620 2 ASN B 315 O 85.2
REMARK 620 3 ASP B 345 OD1 158.6 73.4
REMARK 620 4 ASP B 345 OD2 146.2 116.8 50.0
REMARK 620 5 ASP B 347 OD2 70.5 76.2 104.7 136.9
REMARK 620 6 ASN B 351 O 90.2 174.4 111.2 68.8 99.2
REMARK 620 7 ASP B 398 OD2 65.0 96.3 115.3 86.2 135.3 84.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 506 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 9 OE2
REMARK 620 2 GLU C 65 OE2 75.4
REMARK 620 3 ASP C 97 OD1 65.3 63.1
REMARK 620 4 ILE C 98 O 96.5 142.6 80.2
REMARK 620 5 ASP C 100 OD1 106.4 114.3 171.5 103.1
REMARK 620 6 ASP C 133 OD1 156.5 81.4 107.6 104.5 79.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 508 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 9 OE1
REMARK 620 2 GLU C 10 OE2 107.9
REMARK 620 3 ASP C 63 OD1 98.2 73.3
REMARK 620 4 GLU C 65 OE1 70.4 143.9 71.4
REMARK 620 5 ASP C 100 OD2 123.5 105.5 134.8 104.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 507 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 99 OD1
REMARK 620 2 ASN C 101 O 100.7
REMARK 620 3 ASP C 131 OD2 162.7 92.9
REMARK 620 4 ASP C 133 OD2 82.5 96.0 106.8
REMARK 620 5 ASN C 137 O 97.3 160.8 70.8 79.9
REMARK 620 6 ASP C 188 OD2 81.1 85.1 89.5 163.5 104.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 116 OE1
REMARK 620 2 GLU C 175 OE1 76.2
REMARK 620 3 GLU C 175 OE2 97.8 47.8
REMARK 620 4 ASP C 206 OD1 95.8 126.8 82.8
REMARK 620 5 VAL C 207 O 86.1 135.5 175.8 95.0
REMARK 620 6 ASP C 209 OD1 81.6 71.6 116.7 160.5 65.5
REMARK 620 7 ASP C 242 OD1 160.6 97.2 90.8 102.6 86.2 79.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 505 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 116 OE2
REMARK 620 2 ASP C 173 OD1 83.5
REMARK 620 3 GLU C 175 OE1 79.3 90.7
REMARK 620 4 ASP C 209 OD2 75.6 157.4 93.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 208 OD1
REMARK 620 2 ASN C 210 O 98.1
REMARK 620 3 ASP C 240 OD1 148.9 74.0
REMARK 620 4 ASP C 240 OD2 156.0 94.4 54.7
REMARK 620 5 ASP C 242 OD2 66.3 70.9 82.8 137.5
REMARK 620 6 ASN C 246 O 92.5 162.5 89.8 80.9 101.2
REMARK 620 7 ASP C 295 OD2 79.4 108.5 131.6 77.2 145.0 87.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 509 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 225 OE2
REMARK 620 2 GLU C 282 OE2 104.7
REMARK 620 3 ASP C 311 OD1 82.7 92.5
REMARK 620 4 VAL C 312 O 69.0 170.6 93.5
REMARK 620 5 ASP C 314 OD1 100.7 88.0 176.3 86.4
REMARK 620 6 ASP C 347 OD1 179.4 75.9 97.4 110.4 79.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 510 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 225 OE1
REMARK 620 2 GLU C 225 OE2 47.9
REMARK 620 3 ASP C 280 OD1 82.6 129.1
REMARK 620 4 GLU C 282 OE1 81.1 111.5 62.6
REMARK 620 5 GLU C 282 OE2 103.2 91.9 113.8 53.9
REMARK 620 6 ASP C 314 OD1 130.7 83.2 141.3 131.6 80.8
REMARK 620 7 ASP C 314 OD2 121.2 100.9 94.9 147.5 130.0 53.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 511 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 313 OD1
REMARK 620 2 ASN C 315 O 87.6
REMARK 620 3 ASP C 345 OD1 146.9 60.2
REMARK 620 4 ASP C 345 OD2 166.4 101.9 45.0
REMARK 620 5 ASP C 347 OD2 69.1 77.7 94.8 122.1
REMARK 620 6 ASN C 351 O 101.4 169.5 110.0 70.2 100.4
REMARK 620 7 ASP C 398 OD2 69.6 105.8 123.6 98.2 138.3 82.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 9 OE2
REMARK 620 2 GLU D 65 OE2 71.4
REMARK 620 3 ASP D 97 OD1 67.8 72.7
REMARK 620 4 ILE D 98 O 108.4 153.0 82.2
REMARK 620 5 ASP D 100 OD1 106.2 110.3 172.4 95.9
REMARK 620 6 ASP D 133 OD1 151.8 80.9 109.5 98.7 78.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 505 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 9 OE1
REMARK 620 2 GLU D 10 OE2 106.2
REMARK 620 3 ASP D 63 OD1 88.1 62.0
REMARK 620 4 GLU D 65 OE1 75.4 122.4 60.5
REMARK 620 5 ASP D 100 OD2 126.4 96.5 144.6 129.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN D 99 OD1
REMARK 620 2 ASN D 101 O 83.9
REMARK 620 3 ASP D 131 OD1 158.7 90.7
REMARK 620 4 ASP D 131 OD2 150.9 98.3 50.4
REMARK 620 5 ASP D 133 OD2 77.2 91.7 82.3 131.4
REMARK 620 6 ASN D 137 O 94.6 177.2 91.5 81.8 90.3
REMARK 620 7 ASP D 188 OD2 68.3 90.1 132.5 82.6 145.1 87.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 507 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 116 OE1
REMARK 620 2 GLU D 175 OE1 93.9
REMARK 620 3 GLU D 175 OE2 113.8 46.0
REMARK 620 4 ASP D 206 OD1 91.5 137.7 94.0
REMARK 620 5 VAL D 207 O 78.2 135.3 167.9 86.8
REMARK 620 6 ASP D 209 OD1 92.7 72.6 112.1 149.0 64.1
REMARK 620 7 ASP D 242 OD1 169.5 90.8 76.0 91.4 91.9 79.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 508 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 116 OE2
REMARK 620 2 ASP D 173 OD1 102.5
REMARK 620 3 GLU D 175 OE1 91.4 84.7
REMARK 620 4 ASP D 209 OD2 81.1 175.9 93.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 506 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN D 208 OD1
REMARK 620 2 ASN D 210 O 117.0
REMARK 620 3 ASP D 240 OD1 137.5 74.3
REMARK 620 4 ASP D 240 OD2 151.2 91.3 51.7
REMARK 620 5 ASP D 242 OD2 71.2 74.7 73.5 125.1
REMARK 620 6 ASN D 246 O 81.8 152.6 78.4 73.8 94.9
REMARK 620 7 ASP D 295 OD2 84.2 98.3 136.9 86.9 146.8 103.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 509 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 225 OE2
REMARK 620 2 ASP D 311 OD1 95.5
REMARK 620 3 VAL D 312 O 53.5 77.7
REMARK 620 4 ASP D 314 OD1 70.6 151.2 73.8
REMARK 620 5 ASP D 347 OD1 148.7 94.0 100.0 87.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 510 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 225 OE1
REMARK 620 2 ASP D 280 OD1 129.0
REMARK 620 3 GLU D 282 OE1 123.7 53.9
REMARK 620 4 ASP D 314 OD2 67.2 149.3 145.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 511 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN D 313 OD1
REMARK 620 2 ASN D 315 O 79.6
REMARK 620 3 ASP D 345 OD1 148.4 69.9
REMARK 620 4 ASP D 345 OD2 158.4 117.6 52.3
REMARK 620 5 ASP D 347 OD2 65.3 86.4 104.1 125.4
REMARK 620 6 ASN D 351 O 98.9 177.4 111.4 64.4 91.1
REMARK 620 7 ASP D 398 OD2 68.9 104.3 125.7 93.0 129.9 76.9
REMARK 620 N 1 2 3 4 5 6
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5SZR RELATED DB: PDB
REMARK 900 RELATED ID: 5SZQ RELATED DB: PDB
REMARK 900 RELATED ID: 5SZP RELATED DB: PDB
REMARK 900 RELATED ID: 5SZO RELATED DB: PDB
REMARK 900 RELATED ID: 5SZN RELATED DB: PDB
REMARK 900 RELATED ID: 5SZM RELATED DB: PDB
DBREF1 5SZL A 1 419 UNP A0A0A6YW27_MOUSE
DBREF2 5SZL A A0A0A6YW27 29 447
DBREF1 5SZL B 1 419 UNP A0A0A6YW27_MOUSE
DBREF2 5SZL B A0A0A6YW27 29 447
DBREF1 5SZL C 1 419 UNP A0A0A6YW27_MOUSE
DBREF2 5SZL C A0A0A6YW27 29 447
DBREF1 5SZL D 1 419 UNP A0A0A6YW27_MOUSE
DBREF2 5SZL D A0A0A6YW27 29 447
SEQADV 5SZL HIS A 420 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS A 421 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS A 422 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS A 423 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS A 424 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS A 425 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS A 426 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS A 427 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS B 420 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS B 421 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS B 422 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS B 423 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS B 424 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS B 425 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS B 426 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS B 427 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS C 420 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS C 421 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS C 422 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS C 423 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS C 424 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS C 425 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS C 426 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS C 427 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS D 420 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS D 421 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS D 422 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS D 423 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS D 424 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS D 425 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS D 426 UNP A0A0A6YW2 EXPRESSION TAG
SEQADV 5SZL HIS D 427 UNP A0A0A6YW2 EXPRESSION TAG
SEQRES 1 A 427 GLY ASN ILE ARG TYR SER VAL PRO GLU GLU THR ASP LYS
SEQRES 2 A 427 GLY SER PHE VAL GLY SER ILE ALA LYS ASP LEU GLY LEU
SEQRES 3 A 427 GLU THR ARG GLU LEU MET GLU ARG GLY ILE ARG ILE VAL
SEQRES 4 A 427 SER ARG GLY ARG SER GLN LEU PHE SER LEU ASN PRO ARG
SEQRES 5 A 427 SER GLY SER LEU VAL THR ALA GLY ARG ILE ASP ARG GLU
SEQRES 6 A 427 GLU LEU CYS ALA GLN SER THR PRO CYS VAL VAL SER PHE
SEQRES 7 A 427 ASN ILE LEU MET GLU ASP GLU MET LYS LEU LEU PRO ILE
SEQRES 8 A 427 GLU VAL GLU ILE ILE ASP ILE ASN ASP ASN THR PRO GLN
SEQRES 9 A 427 PHE GLN LEU GLU GLU LEU GLU LEU LYS MET SER GLU ILE
SEQRES 10 A 427 THR THR PRO GLY THR ARG ILE PRO LEU PRO LEU GLY GLN
SEQRES 11 A 427 ASP LEU ASP VAL GLY ILE ASN SER LEU GLN SER TYR GLN
SEQRES 12 A 427 LEU SER ALA ASN PRO HIS PHE SER LEU ASP VAL GLN GLN
SEQRES 13 A 427 GLY PRO GLU GLY PRO GLN GLN PRO GLU MET VAL LEU GLN
SEQRES 14 A 427 ARG PRO LEU ASP ARG GLU LYS ASP ALA VAL HIS TYR LEU
SEQRES 15 A 427 VAL LEU THR ALA SER ASP GLY GLY SER PRO ILE HIS SER
SEQRES 16 A 427 GLY THR LEU GLN ILE HIS VAL GLN VAL VAL ASP VAL ASN
SEQRES 17 A 427 ASP ASN PRO PRO ALA PHE THR LYS ALA GLU TYR HIS VAL
SEQRES 18 A 427 SER VAL PRO GLU ASN VAL PRO LEU GLY THR ARG LEU LEU
SEQRES 19 A 427 LYS VAL ASN ALA THR ASP PRO ASP GLU GLY ALA ASN GLY
SEQRES 20 A 427 ARG VAL THR TYR SER PHE HIS LYS VAL ASP HIS SER VAL
SEQRES 21 A 427 VAL ARG LYS PHE GLN LEU ASP ALA TYR THR GLY GLU LEU
SEQRES 22 A 427 SER ASN LYS GLU PRO LEU ASP PHE GLU GLU TYR LYS VAL
SEQRES 23 A 427 TYR PRO MET GLU ILE GLN ALA GLN ASP GLY ALA GLY LEU
SEQRES 24 A 427 MET ALA ARG ALA LYS VAL LEU VAL THR VAL LEU ASP VAL
SEQRES 25 A 427 ASN ASP ASN ALA PRO GLU VAL GLY ILE THR SER VAL THR
SEQRES 26 A 427 ASN THR VAL PRO GLU ASN PHE PRO PRO GLY THR THR ILE
SEQRES 27 A 427 ALA LEU ILE SER VAL HIS ASP GLN ASP ALA ASP ASN ASN
SEQRES 28 A 427 GLY HIS ILE THR CYS SER ILE PRO GLY ASN LEU PRO PHE
SEQRES 29 A 427 LYS LEU GLU LYS LEU VAL ASP ASN TYR TYR ARG LEU VAL
SEQRES 30 A 427 THR GLU ARG THR LEU ASP ARG GLU GLN SER SER ARG HIS
SEQRES 31 A 427 ASN ILE THR ILE THR ALA THR ASP GLN GLY THR PRO PRO
SEQRES 32 A 427 LEU SER THR GLN ALA HIS ILE SER LEU LEU VAL THR ASP
SEQRES 33 A 427 ILE ASN ASP HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 427 GLY ASN ILE ARG TYR SER VAL PRO GLU GLU THR ASP LYS
SEQRES 2 B 427 GLY SER PHE VAL GLY SER ILE ALA LYS ASP LEU GLY LEU
SEQRES 3 B 427 GLU THR ARG GLU LEU MET GLU ARG GLY ILE ARG ILE VAL
SEQRES 4 B 427 SER ARG GLY ARG SER GLN LEU PHE SER LEU ASN PRO ARG
SEQRES 5 B 427 SER GLY SER LEU VAL THR ALA GLY ARG ILE ASP ARG GLU
SEQRES 6 B 427 GLU LEU CYS ALA GLN SER THR PRO CYS VAL VAL SER PHE
SEQRES 7 B 427 ASN ILE LEU MET GLU ASP GLU MET LYS LEU LEU PRO ILE
SEQRES 8 B 427 GLU VAL GLU ILE ILE ASP ILE ASN ASP ASN THR PRO GLN
SEQRES 9 B 427 PHE GLN LEU GLU GLU LEU GLU LEU LYS MET SER GLU ILE
SEQRES 10 B 427 THR THR PRO GLY THR ARG ILE PRO LEU PRO LEU GLY GLN
SEQRES 11 B 427 ASP LEU ASP VAL GLY ILE ASN SER LEU GLN SER TYR GLN
SEQRES 12 B 427 LEU SER ALA ASN PRO HIS PHE SER LEU ASP VAL GLN GLN
SEQRES 13 B 427 GLY PRO GLU GLY PRO GLN GLN PRO GLU MET VAL LEU GLN
SEQRES 14 B 427 ARG PRO LEU ASP ARG GLU LYS ASP ALA VAL HIS TYR LEU
SEQRES 15 B 427 VAL LEU THR ALA SER ASP GLY GLY SER PRO ILE HIS SER
SEQRES 16 B 427 GLY THR LEU GLN ILE HIS VAL GLN VAL VAL ASP VAL ASN
SEQRES 17 B 427 ASP ASN PRO PRO ALA PHE THR LYS ALA GLU TYR HIS VAL
SEQRES 18 B 427 SER VAL PRO GLU ASN VAL PRO LEU GLY THR ARG LEU LEU
SEQRES 19 B 427 LYS VAL ASN ALA THR ASP PRO ASP GLU GLY ALA ASN GLY
SEQRES 20 B 427 ARG VAL THR TYR SER PHE HIS LYS VAL ASP HIS SER VAL
SEQRES 21 B 427 VAL ARG LYS PHE GLN LEU ASP ALA TYR THR GLY GLU LEU
SEQRES 22 B 427 SER ASN LYS GLU PRO LEU ASP PHE GLU GLU TYR LYS VAL
SEQRES 23 B 427 TYR PRO MET GLU ILE GLN ALA GLN ASP GLY ALA GLY LEU
SEQRES 24 B 427 MET ALA ARG ALA LYS VAL LEU VAL THR VAL LEU ASP VAL
SEQRES 25 B 427 ASN ASP ASN ALA PRO GLU VAL GLY ILE THR SER VAL THR
SEQRES 26 B 427 ASN THR VAL PRO GLU ASN PHE PRO PRO GLY THR THR ILE
SEQRES 27 B 427 ALA LEU ILE SER VAL HIS ASP GLN ASP ALA ASP ASN ASN
SEQRES 28 B 427 GLY HIS ILE THR CYS SER ILE PRO GLY ASN LEU PRO PHE
SEQRES 29 B 427 LYS LEU GLU LYS LEU VAL ASP ASN TYR TYR ARG LEU VAL
SEQRES 30 B 427 THR GLU ARG THR LEU ASP ARG GLU GLN SER SER ARG HIS
SEQRES 31 B 427 ASN ILE THR ILE THR ALA THR ASP GLN GLY THR PRO PRO
SEQRES 32 B 427 LEU SER THR GLN ALA HIS ILE SER LEU LEU VAL THR ASP
SEQRES 33 B 427 ILE ASN ASP HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 C 427 GLY ASN ILE ARG TYR SER VAL PRO GLU GLU THR ASP LYS
SEQRES 2 C 427 GLY SER PHE VAL GLY SER ILE ALA LYS ASP LEU GLY LEU
SEQRES 3 C 427 GLU THR ARG GLU LEU MET GLU ARG GLY ILE ARG ILE VAL
SEQRES 4 C 427 SER ARG GLY ARG SER GLN LEU PHE SER LEU ASN PRO ARG
SEQRES 5 C 427 SER GLY SER LEU VAL THR ALA GLY ARG ILE ASP ARG GLU
SEQRES 6 C 427 GLU LEU CYS ALA GLN SER THR PRO CYS VAL VAL SER PHE
SEQRES 7 C 427 ASN ILE LEU MET GLU ASP GLU MET LYS LEU LEU PRO ILE
SEQRES 8 C 427 GLU VAL GLU ILE ILE ASP ILE ASN ASP ASN THR PRO GLN
SEQRES 9 C 427 PHE GLN LEU GLU GLU LEU GLU LEU LYS MET SER GLU ILE
SEQRES 10 C 427 THR THR PRO GLY THR ARG ILE PRO LEU PRO LEU GLY GLN
SEQRES 11 C 427 ASP LEU ASP VAL GLY ILE ASN SER LEU GLN SER TYR GLN
SEQRES 12 C 427 LEU SER ALA ASN PRO HIS PHE SER LEU ASP VAL GLN GLN
SEQRES 13 C 427 GLY PRO GLU GLY PRO GLN GLN PRO GLU MET VAL LEU GLN
SEQRES 14 C 427 ARG PRO LEU ASP ARG GLU LYS ASP ALA VAL HIS TYR LEU
SEQRES 15 C 427 VAL LEU THR ALA SER ASP GLY GLY SER PRO ILE HIS SER
SEQRES 16 C 427 GLY THR LEU GLN ILE HIS VAL GLN VAL VAL ASP VAL ASN
SEQRES 17 C 427 ASP ASN PRO PRO ALA PHE THR LYS ALA GLU TYR HIS VAL
SEQRES 18 C 427 SER VAL PRO GLU ASN VAL PRO LEU GLY THR ARG LEU LEU
SEQRES 19 C 427 LYS VAL ASN ALA THR ASP PRO ASP GLU GLY ALA ASN GLY
SEQRES 20 C 427 ARG VAL THR TYR SER PHE HIS LYS VAL ASP HIS SER VAL
SEQRES 21 C 427 VAL ARG LYS PHE GLN LEU ASP ALA TYR THR GLY GLU LEU
SEQRES 22 C 427 SER ASN LYS GLU PRO LEU ASP PHE GLU GLU TYR LYS VAL
SEQRES 23 C 427 TYR PRO MET GLU ILE GLN ALA GLN ASP GLY ALA GLY LEU
SEQRES 24 C 427 MET ALA ARG ALA LYS VAL LEU VAL THR VAL LEU ASP VAL
SEQRES 25 C 427 ASN ASP ASN ALA PRO GLU VAL GLY ILE THR SER VAL THR
SEQRES 26 C 427 ASN THR VAL PRO GLU ASN PHE PRO PRO GLY THR THR ILE
SEQRES 27 C 427 ALA LEU ILE SER VAL HIS ASP GLN ASP ALA ASP ASN ASN
SEQRES 28 C 427 GLY HIS ILE THR CYS SER ILE PRO GLY ASN LEU PRO PHE
SEQRES 29 C 427 LYS LEU GLU LYS LEU VAL ASP ASN TYR TYR ARG LEU VAL
SEQRES 30 C 427 THR GLU ARG THR LEU ASP ARG GLU GLN SER SER ARG HIS
SEQRES 31 C 427 ASN ILE THR ILE THR ALA THR ASP GLN GLY THR PRO PRO
SEQRES 32 C 427 LEU SER THR GLN ALA HIS ILE SER LEU LEU VAL THR ASP
SEQRES 33 C 427 ILE ASN ASP HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 D 427 GLY ASN ILE ARG TYR SER VAL PRO GLU GLU THR ASP LYS
SEQRES 2 D 427 GLY SER PHE VAL GLY SER ILE ALA LYS ASP LEU GLY LEU
SEQRES 3 D 427 GLU THR ARG GLU LEU MET GLU ARG GLY ILE ARG ILE VAL
SEQRES 4 D 427 SER ARG GLY ARG SER GLN LEU PHE SER LEU ASN PRO ARG
SEQRES 5 D 427 SER GLY SER LEU VAL THR ALA GLY ARG ILE ASP ARG GLU
SEQRES 6 D 427 GLU LEU CYS ALA GLN SER THR PRO CYS VAL VAL SER PHE
SEQRES 7 D 427 ASN ILE LEU MET GLU ASP GLU MET LYS LEU LEU PRO ILE
SEQRES 8 D 427 GLU VAL GLU ILE ILE ASP ILE ASN ASP ASN THR PRO GLN
SEQRES 9 D 427 PHE GLN LEU GLU GLU LEU GLU LEU LYS MET SER GLU ILE
SEQRES 10 D 427 THR THR PRO GLY THR ARG ILE PRO LEU PRO LEU GLY GLN
SEQRES 11 D 427 ASP LEU ASP VAL GLY ILE ASN SER LEU GLN SER TYR GLN
SEQRES 12 D 427 LEU SER ALA ASN PRO HIS PHE SER LEU ASP VAL GLN GLN
SEQRES 13 D 427 GLY PRO GLU GLY PRO GLN GLN PRO GLU MET VAL LEU GLN
SEQRES 14 D 427 ARG PRO LEU ASP ARG GLU LYS ASP ALA VAL HIS TYR LEU
SEQRES 15 D 427 VAL LEU THR ALA SER ASP GLY GLY SER PRO ILE HIS SER
SEQRES 16 D 427 GLY THR LEU GLN ILE HIS VAL GLN VAL VAL ASP VAL ASN
SEQRES 17 D 427 ASP ASN PRO PRO ALA PHE THR LYS ALA GLU TYR HIS VAL
SEQRES 18 D 427 SER VAL PRO GLU ASN VAL PRO LEU GLY THR ARG LEU LEU
SEQRES 19 D 427 LYS VAL ASN ALA THR ASP PRO ASP GLU GLY ALA ASN GLY
SEQRES 20 D 427 ARG VAL THR TYR SER PHE HIS LYS VAL ASP HIS SER VAL
SEQRES 21 D 427 VAL ARG LYS PHE GLN LEU ASP ALA TYR THR GLY GLU LEU
SEQRES 22 D 427 SER ASN LYS GLU PRO LEU ASP PHE GLU GLU TYR LYS VAL
SEQRES 23 D 427 TYR PRO MET GLU ILE GLN ALA GLN ASP GLY ALA GLY LEU
SEQRES 24 D 427 MET ALA ARG ALA LYS VAL LEU VAL THR VAL LEU ASP VAL
SEQRES 25 D 427 ASN ASP ASN ALA PRO GLU VAL GLY ILE THR SER VAL THR
SEQRES 26 D 427 ASN THR VAL PRO GLU ASN PHE PRO PRO GLY THR THR ILE
SEQRES 27 D 427 ALA LEU ILE SER VAL HIS ASP GLN ASP ALA ASP ASN ASN
SEQRES 28 D 427 GLY HIS ILE THR CYS SER ILE PRO GLY ASN LEU PRO PHE
SEQRES 29 D 427 LYS LEU GLU LYS LEU VAL ASP ASN TYR TYR ARG LEU VAL
SEQRES 30 D 427 THR GLU ARG THR LEU ASP ARG GLU GLN SER SER ARG HIS
SEQRES 31 D 427 ASN ILE THR ILE THR ALA THR ASP GLN GLY THR PRO PRO
SEQRES 32 D 427 LEU SER THR GLN ALA HIS ILE SER LEU LEU VAL THR ASP
SEQRES 33 D 427 ILE ASN ASP HIS HIS HIS HIS HIS HIS HIS HIS
HET NAG E 1 14
HET NAG E 2 14
HET BMA E 3 11
HET NAG F 1 14
HET NAG F 2 14
HET NAG G 1 14
HET NAG G 2 14
HET BMA G 3 11
HET FUC G 4 10
HET MAN A 501 11
HET MAN A 502 11
HET CA A 503 1
HET CA A 504 1
HET CA A 505 1
HET CA A 506 1
HET CA A 507 1
HET CA A 508 1
HET CA A 509 1
HET CA A 510 1
HET CA A 511 1
HET NAG A 515 14
HET MAN B 501 11
HET MAN B 502 11
HET CA B 503 1
HET CA B 504 1
HET CA B 505 1
HET CA B 506 1
HET CA B 507 1
HET CA B 508 1
HET CA B 509 1
HET CA B 510 1
HET CA B 511 1
HET NAG B 512 14
HET NAG B 513 14
HET MAN C 501 11
HET MAN C 502 11
HET CA C 503 1
HET CA C 504 1
HET CA C 505 1
HET CA C 506 1
HET CA C 507 1
HET CA C 508 1
HET CA C 509 1
HET CA C 510 1
HET CA C 511 1
HET NAG C 514 14
HET MAN D 501 11
HET MAN D 502 11
HET CA D 503 1
HET CA D 504 1
HET CA D 505 1
HET CA D 506 1
HET CA D 507 1
HET CA D 508 1
HET CA D 509 1
HET CA D 510 1
HET CA D 511 1
HET NAG D 516 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM CA CALCIUM ION
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 FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 5 NAG 11(C8 H15 N O6)
FORMUL 5 BMA 2(C6 H12 O6)
FORMUL 7 FUC C6 H12 O5
FORMUL 8 MAN 8(C6 H12 O6)
FORMUL 10 CA 36(CA 2+)
HELIX 1 AA1 ILE A 20 LEU A 24 1 5
HELIX 2 AA2 GLU A 27 GLY A 35 1 9
HELIX 3 AA3 ARG A 43 GLN A 45 5 3
HELIX 4 AA4 ASP A 63 CYS A 68 1 6
HELIX 5 AA5 VAL A 134 SER A 138 5 5
HELIX 6 AA6 GLU A 243 GLY A 247 5 5
HELIX 7 AA7 ASP A 257 ARG A 262 1 6
HELIX 8 AA8 ALA A 348 GLY A 352 5 5
HELIX 9 AA9 ILE B 20 GLY B 25 1 6
HELIX 10 AB1 GLU B 27 GLY B 35 1 9
HELIX 11 AB2 GLY B 42 GLN B 45 5 4
HELIX 12 AB3 ASP B 63 CYS B 68 1 6
HELIX 13 AB4 VAL B 134 SER B 138 5 5
HELIX 14 AB5 GLU B 243 ARG B 248 5 6
HELIX 15 AB6 ASP B 257 ARG B 262 1 6
HELIX 16 AB7 ALA B 348 GLY B 352 5 5
HELIX 17 AB8 SER C 19 GLY C 25 1 7
HELIX 18 AB9 GLU C 27 GLY C 35 1 9
HELIX 19 AC1 ARG C 43 GLN C 45 5 3
HELIX 20 AC2 ASP C 63 ALA C 69 1 7
HELIX 21 AC3 VAL C 134 SER C 138 5 5
HELIX 22 AC4 GLU C 243 ARG C 248 5 6
HELIX 23 AC5 ASP C 257 ARG C 262 1 6
HELIX 24 AC6 ALA C 348 GLY C 352 5 5
HELIX 25 AC7 ILE D 20 GLY D 25 1 6
HELIX 26 AC8 GLU D 27 GLY D 35 1 9
HELIX 27 AC9 ARG D 41 GLN D 45 5 5
HELIX 28 AD1 ASP D 63 CYS D 68 1 6
HELIX 29 AD2 VAL D 134 SER D 138 5 5
HELIX 30 AD3 GLU D 243 ARG D 248 5 6
HELIX 31 AD4 ASP D 257 ARG D 262 1 6
HELIX 32 AD5 ALA D 348 GLY D 352 5 5
SHEET 1 AA1 4 ILE A 3 PRO A 8 0
SHEET 2 AA1 4 LYS A 87 ILE A 96 1 O GLU A 92 N ILE A 3
SHEET 3 AA1 4 VAL A 75 MET A 82 -1 N PHE A 78 O ILE A 91
SHEET 4 AA1 4 ARG A 37 ILE A 38 -1 N ARG A 37 O LEU A 81
SHEET 1 AA2 3 GLY A 18 SER A 19 0
SHEET 2 AA2 3 SER A 55 THR A 58 -1 O LEU A 56 N GLY A 18
SHEET 3 AA2 3 PHE A 47 LEU A 49 -1 N SER A 48 O VAL A 57
SHEET 1 AA3 2 GLN A 104 PHE A 105 0
SHEET 2 AA3 2 GLY A 129 GLN A 130 -1 O GLN A 130 N GLN A 104
SHEET 1 AA4 4 GLU A 109 SER A 115 0
SHEET 2 AA4 4 SER A 195 VAL A 205 1 O GLN A 203 N LEU A 112
SHEET 3 AA4 4 VAL A 179 SER A 187 -1 N HIS A 180 O VAL A 202
SHEET 4 AA4 4 SER A 141 LEU A 144 -1 N GLN A 143 O THR A 185
SHEET 1 AA5 3 ARG A 123 PRO A 125 0
SHEET 2 AA5 3 PRO A 161 LEU A 168 -1 O MET A 166 N ILE A 124
SHEET 3 AA5 3 PHE A 150 GLN A 156 -1 N GLN A 155 O GLN A 162
SHEET 1 AA6 2 ALA A 213 PHE A 214 0
SHEET 2 AA6 2 ALA A 238 THR A 239 -1 O THR A 239 N ALA A 213
SHEET 1 AA7 4 GLU A 218 VAL A 223 0
SHEET 2 AA7 4 MET A 300 VAL A 309 1 O LEU A 306 N TYR A 219
SHEET 3 AA7 4 VAL A 286 GLN A 294 -1 N ILE A 291 O ALA A 303
SHEET 4 AA7 4 THR A 250 PHE A 253 -1 N THR A 250 O GLN A 294
SHEET 1 AA8 3 ARG A 232 LYS A 235 0
SHEET 2 AA8 3 GLU A 272 ASN A 275 -1 O LEU A 273 N LEU A 233
SHEET 3 AA8 3 PHE A 264 LEU A 266 -1 N GLN A 265 O SER A 274
SHEET 1 AA9 4 GLU A 318 VAL A 324 0
SHEET 2 AA9 4 THR A 337 HIS A 344 -1 O SER A 342 N GLY A 320
SHEET 3 AA9 4 TYR A 373 VAL A 377 -1 O TYR A 374 N ILE A 341
SHEET 4 AA9 4 LYS A 365 LYS A 368 -1 N GLU A 367 O ARG A 375
SHEET 1 AB1 3 ILE A 354 SER A 357 0
SHEET 2 AB1 3 ARG A 389 ASP A 398 -1 O THR A 397 N THR A 355
SHEET 3 AB1 3 SER A 405 LEU A 413 -1 O ILE A 410 N ILE A 392
SHEET 1 AB2 4 ILE B 3 PRO B 8 0
SHEET 2 AB2 4 LYS B 87 ILE B 96 1 O GLU B 92 N ILE B 3
SHEET 3 AB2 4 CYS B 74 MET B 82 -1 N CYS B 74 O ILE B 95
SHEET 4 AB2 4 ILE B 36 ILE B 38 -1 N ARG B 37 O LEU B 81
SHEET 1 AB3 3 PHE B 16 SER B 19 0
SHEET 2 AB3 3 SER B 55 THR B 58 -1 O LEU B 56 N GLY B 18
SHEET 3 AB3 3 PHE B 47 LEU B 49 -1 N SER B 48 O VAL B 57
SHEET 1 AB4 2 GLN B 104 PHE B 105 0
SHEET 2 AB4 2 GLY B 129 GLN B 130 -1 O GLN B 130 N GLN B 104
SHEET 1 AB5 4 GLU B 109 SER B 115 0
SHEET 2 AB5 4 SER B 195 VAL B 205 1 O HIS B 201 N LEU B 110
SHEET 3 AB5 4 VAL B 179 SER B 187 -1 N ALA B 186 O GLY B 196
SHEET 4 AB5 4 SER B 141 LEU B 144 -1 N SER B 141 O SER B 187
SHEET 1 AB6 3 ARG B 123 PRO B 125 0
SHEET 2 AB6 3 PRO B 161 LEU B 168 -1 O MET B 166 N ILE B 124
SHEET 3 AB6 3 PHE B 150 GLN B 156 -1 N SER B 151 O VAL B 167
SHEET 1 AB7 2 ALA B 213 PHE B 214 0
SHEET 2 AB7 2 ALA B 238 THR B 239 -1 O THR B 239 N ALA B 213
SHEET 1 AB8 4 GLU B 218 PRO B 224 0
SHEET 2 AB8 4 MET B 300 LEU B 310 1 O LYS B 304 N TYR B 219
SHEET 3 AB8 4 PRO B 288 GLN B 294 -1 N ILE B 291 O ALA B 303
SHEET 4 AB8 4 THR B 250 PHE B 253 -1 N SER B 252 O GLN B 292
SHEET 1 AB9 3 ARG B 232 LYS B 235 0
SHEET 2 AB9 3 GLU B 272 ASN B 275 -1 O LEU B 273 N LEU B 234
SHEET 3 AB9 3 PHE B 264 LEU B 266 -1 N GLN B 265 O SER B 274
SHEET 1 AC1 4 GLU B 318 GLY B 320 0
SHEET 2 AC1 4 THR B 337 HIS B 344 -1 O HIS B 344 N GLU B 318
SHEET 3 AC1 4 TYR B 373 VAL B 377 -1 O LEU B 376 N ILE B 338
SHEET 4 AC1 4 LYS B 365 GLU B 367 -1 N LYS B 365 O VAL B 377
SHEET 1 AC2 3 ILE B 354 SER B 357 0
SHEET 2 AC2 3 HIS B 390 ASP B 398 -1 O THR B 397 N THR B 355
SHEET 3 AC2 3 SER B 405 LEU B 412 -1 O ALA B 408 N ILE B 394
SHEET 1 AC3 4 ILE C 3 PRO C 8 0
SHEET 2 AC3 4 LYS C 87 ILE C 96 1 O GLU C 94 N VAL C 7
SHEET 3 AC3 4 VAL C 75 MET C 82 -1 N VAL C 76 O VAL C 93
SHEET 4 AC3 4 ILE C 36 ILE C 38 -1 N ARG C 37 O LEU C 81
SHEET 1 AC4 3 PHE C 16 GLY C 18 0
SHEET 2 AC4 3 SER C 55 THR C 58 -1 O LEU C 56 N GLY C 18
SHEET 3 AC4 3 PHE C 47 ASN C 50 -1 N SER C 48 O VAL C 57
SHEET 1 AC5 2 GLN C 104 PHE C 105 0
SHEET 2 AC5 2 GLY C 129 GLN C 130 -1 O GLN C 130 N GLN C 104
SHEET 1 AC6 4 GLU C 109 SER C 115 0
SHEET 2 AC6 4 SER C 195 VAL C 205 1 O GLN C 203 N LEU C 112
SHEET 3 AC6 4 VAL C 179 SER C 187 -1 N LEU C 184 O LEU C 198
SHEET 4 AC6 4 SER C 141 LEU C 144 -1 N SER C 141 O SER C 187
SHEET 1 AC7 3 ARG C 123 PRO C 125 0
SHEET 2 AC7 3 PRO C 161 LEU C 168 -1 O MET C 166 N ILE C 124
SHEET 3 AC7 3 PHE C 150 GLN C 156 -1 N ASP C 153 O GLU C 165
SHEET 1 AC8 2 ALA C 213 PHE C 214 0
SHEET 2 AC8 2 ALA C 238 THR C 239 -1 O THR C 239 N ALA C 213
SHEET 1 AC9 4 GLU C 218 PRO C 224 0
SHEET 2 AC9 4 MET C 300 LEU C 310 1 O THR C 308 N VAL C 221
SHEET 3 AC9 4 VAL C 286 GLN C 294 -1 N ILE C 291 O ALA C 303
SHEET 4 AC9 4 THR C 250 PHE C 253 -1 N SER C 252 O GLN C 292
SHEET 1 AD1 3 ARG C 232 LYS C 235 0
SHEET 2 AD1 3 GLU C 272 ASN C 275 -1 O LEU C 273 N LEU C 233
SHEET 3 AD1 3 PHE C 264 LEU C 266 -1 N GLN C 265 O SER C 274
SHEET 1 AD2 4 GLU C 318 VAL C 324 0
SHEET 2 AD2 4 THR C 337 HIS C 344 -1 O SER C 342 N GLY C 320
SHEET 3 AD2 4 TYR C 373 VAL C 377 -1 O LEU C 376 N ILE C 338
SHEET 4 AD2 4 LYS C 365 LYS C 368 -1 N LYS C 365 O VAL C 377
SHEET 1 AD3 4 THR C 327 PRO C 329 0
SHEET 2 AD3 4 SER C 405 THR C 415 1 O THR C 415 N VAL C 328
SHEET 3 AD3 4 ARG C 389 ASP C 398 -1 N HIS C 390 O LEU C 412
SHEET 4 AD3 4 ILE C 354 SER C 357 -1 N THR C 355 O THR C 397
SHEET 1 AD4 4 ILE D 3 PRO D 8 0
SHEET 2 AD4 4 LYS D 87 ILE D 96 1 O GLU D 92 N ILE D 3
SHEET 3 AD4 4 CYS D 74 MET D 82 -1 N CYS D 74 O ILE D 95
SHEET 4 AD4 4 ILE D 36 ILE D 38 -1 N ARG D 37 O LEU D 81
SHEET 1 AD5 3 PHE D 16 SER D 19 0
SHEET 2 AD5 3 SER D 55 THR D 58 -1 O LEU D 56 N GLY D 18
SHEET 3 AD5 3 PHE D 47 LEU D 49 -1 N SER D 48 O VAL D 57
SHEET 1 AD6 2 GLN D 104 PHE D 105 0
SHEET 2 AD6 2 GLY D 129 GLN D 130 -1 O GLN D 130 N GLN D 104
SHEET 1 AD7 4 GLU D 109 SER D 115 0
SHEET 2 AD7 4 SER D 195 VAL D 205 1 O HIS D 201 N LEU D 110
SHEET 3 AD7 4 VAL D 179 SER D 187 -1 N HIS D 180 O VAL D 202
SHEET 4 AD7 4 SER D 141 LEU D 144 -1 N SER D 141 O SER D 187
SHEET 1 AD8 3 ARG D 123 PRO D 125 0
SHEET 2 AD8 3 PRO D 161 LEU D 168 -1 O MET D 166 N ILE D 124
SHEET 3 AD8 3 PHE D 150 GLN D 156 -1 N ASP D 153 O GLU D 165
SHEET 1 AD9 2 ALA D 213 PHE D 214 0
SHEET 2 AD9 2 ALA D 238 THR D 239 -1 O THR D 239 N ALA D 213
SHEET 1 AE1 4 GLU D 218 PRO D 224 0
SHEET 2 AE1 4 MET D 300 LEU D 310 1 O LYS D 304 N TYR D 219
SHEET 3 AE1 4 PRO D 288 GLN D 294 -1 N ILE D 291 O ALA D 303
SHEET 4 AE1 4 THR D 250 PHE D 253 -1 N SER D 252 O GLN D 292
SHEET 1 AE2 3 ARG D 232 LYS D 235 0
SHEET 2 AE2 3 GLU D 272 ASN D 275 -1 O LEU D 273 N LEU D 234
SHEET 3 AE2 3 PHE D 264 LEU D 266 -1 N GLN D 265 O SER D 274
SHEET 1 AE3 4 GLU D 318 VAL D 324 0
SHEET 2 AE3 4 THR D 337 HIS D 344 -1 O SER D 342 N GLY D 320
SHEET 3 AE3 4 TYR D 373 VAL D 377 -1 O LEU D 376 N ILE D 338
SHEET 4 AE3 4 LYS D 365 LYS D 368 -1 N GLU D 367 O ARG D 375
SHEET 1 AE4 4 VAL D 328 PRO D 329 0
SHEET 2 AE4 4 SER D 405 THR D 415 1 O THR D 415 N VAL D 328
SHEET 3 AE4 4 ARG D 389 ASP D 398 -1 N ALA D 396 O THR D 406
SHEET 4 AE4 4 ILE D 354 SER D 357 -1 N THR D 355 O THR D 397
SSBOND 1 CYS A 68 CYS A 74 1555 1555 2.03
SSBOND 2 CYS B 68 CYS B 74 1555 1555 2.03
SSBOND 3 CYS C 68 CYS C 74 1555 1555 2.03
SSBOND 4 CYS D 68 CYS D 74 1555 1555 2.03
LINK OG SER A 195 C1 MAN A 501 1555 1555 1.44
LINK OG1 THR A 197 C1 MAN A 502 1555 1555 1.44
LINK ND2 ASN A 237 C1 NAG A 515 1555 1555 1.46
LINK ND2 ASN A 391 C1 NAG E 1 1555 1555 1.45
LINK OG SER B 195 C1 MAN B 502 1555 1555 1.44
LINK OG1 THR B 197 C1 MAN B 501 1555 1555 1.44
LINK ND2 ASN B 237 C1 NAG B 513 1555 1555 1.46
LINK ND2 ASN B 391 C1 NAG B 512 1555 1555 1.45
LINK OG SER C 195 C1 MAN C 501 1555 1555 1.44
LINK OG1 THR C 197 C1 MAN C 502 1555 1555 1.44
LINK ND2 ASN C 237 C1 NAG F 1 1555 1555 1.43
LINK ND2 ASN C 391 C1 NAG C 514 1555 1555 1.44
LINK OG SER D 195 C1 MAN D 502 1555 1555 1.44
LINK OG1 THR D 197 C1 MAN D 501 1555 1555 1.44
LINK ND2 ASN D 237 C1 NAG G 1 1555 1555 1.43
LINK ND2 ASN D 391 C1 NAG D 516 1555 1555 1.45
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.45
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.45
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45
LINK O6 NAG G 1 C1 FUC G 4 1555 1555 1.44
LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.45
LINK OE2 GLU A 9 CA CA A 506 1555 1555 2.55
LINK OE2 GLU A 10 CA CA A 508 1555 1555 2.40
LINK OD1 ASP A 63 CA CA A 508 1555 1555 2.35
LINK OE2 GLU A 65 CA CA A 506 1555 1555 2.36
LINK OE1 GLU A 65 CA CA A 508 1555 1555 2.38
LINK OD1 ASP A 97 CA CA A 506 1555 1555 3.16
LINK O ILE A 98 CA CA A 506 1555 1555 2.47
LINK OD1 ASN A 99 CA CA A 507 1555 1555 2.42
LINK OD1 ASP A 100 CA CA A 506 1555 1555 2.40
LINK OD2 ASP A 100 CA CA A 508 1555 1555 2.41
LINK O ASN A 101 CA CA A 507 1555 1555 2.29
LINK OE1 GLU A 116 CA CA A 504 1555 1555 2.47
LINK OE2 GLU A 116 CA CA A 505 1555 1555 2.39
LINK OD1 ASP A 131 CA CA A 507 1555 1555 2.64
LINK OD2 ASP A 131 CA CA A 507 1555 1555 2.30
LINK OD1 ASP A 133 CA CA A 506 1555 1555 2.47
LINK OD2 ASP A 133 CA CA A 507 1555 1555 2.41
LINK O ASN A 137 CA CA A 507 1555 1555 2.34
LINK OD1 ASP A 173 CA CA A 505 1555 1555 2.23
LINK OE1 GLU A 175 CA CA A 504 1555 1555 3.16
LINK OE2 GLU A 175 CA CA A 504 1555 1555 2.18
LINK OE1 GLU A 175 CA CA A 505 1555 1555 2.34
LINK OD2 ASP A 188 CA CA A 507 1555 1555 2.55
LINK OD1 ASP A 206 CA CA A 504 1555 1555 2.44
LINK O VAL A 207 CA CA A 504 1555 1555 2.29
LINK OD1 ASN A 208 CA CA A 503 1555 1555 2.41
LINK OD1 ASP A 209 CA CA A 504 1555 1555 2.40
LINK OD2 ASP A 209 CA CA A 505 1555 1555 2.24
LINK O ASN A 210 CA CA A 503 1555 1555 2.47
LINK OE1 GLU A 225 CA CA A 509 1555 1555 2.65
LINK OE2 GLU A 225 CA CA A 510 1555 1555 2.73
LINK OD1 ASP A 240 CA CA A 503 1555 1555 3.08
LINK OD2 ASP A 240 CA CA A 503 1555 1555 3.05
LINK OD2 ASP A 242 CA CA A 503 1555 1555 2.46
LINK OD1 ASP A 242 CA CA A 504 1555 1555 2.45
LINK O ASN A 246 CA CA A 503 1555 1555 2.55
LINK OD1 ASP A 280 CA CA A 510 1555 1555 2.35
LINK OE2 GLU A 282 CA CA A 509 1555 1555 3.10
LINK OE1 GLU A 282 CA CA A 510 1555 1555 2.28
LINK OE2 GLU A 282 CA CA A 510 1555 1555 2.71
LINK OD2 ASP A 295 CA CA A 503 1555 1555 2.43
LINK OD1 ASP A 311 CA CA A 509 1555 1555 2.57
LINK O VAL A 312 CA CA A 509 1555 1555 2.43
LINK OD1 ASN A 313 CA CA A 511 1555 1555 2.42
LINK OD1 ASP A 314 CA CA A 509 1555 1555 2.90
LINK OD1 ASP A 314 CA CA A 510 1555 1555 2.77
LINK OD2 ASP A 314 CA CA A 510 1555 1555 2.44
LINK O ASN A 315 CA CA A 511 1555 1555 2.61
LINK OD1 ASP A 345 CA CA A 511 1555 1555 3.10
LINK OD2 ASP A 345 CA CA A 511 1555 1555 3.10
LINK OD1 ASP A 347 CA CA A 509 1555 1555 2.65
LINK OD2 ASP A 347 CA CA A 509 1555 1555 3.10
LINK OD2 ASP A 347 CA CA A 511 1555 1555 2.55
LINK O ASN A 351 CA CA A 511 1555 1555 2.70
LINK OE2 GLU B 9 CA CA B 504 1555 1555 2.33
LINK OE2 GLU B 10 CA CA B 505 1555 1555 2.49
LINK OD1 ASP B 63 CA CA B 505 1555 1555 2.58
LINK OE1 GLU B 65 CA CA B 504 1555 1555 3.11
LINK OE2 GLU B 65 CA CA B 504 1555 1555 2.30
LINK OE1 GLU B 65 CA CA B 505 1555 1555 2.43
LINK OD1 ASP B 97 CA CA B 504 1555 1555 2.47
LINK O ILE B 98 CA CA B 504 1555 1555 2.32
LINK OD1 ASN B 99 CA CA B 503 1555 1555 2.34
LINK OD1 ASP B 100 CA CA B 505 1555 1555 2.68
LINK OD2 ASP B 100 CA CA B 505 1555 1555 2.87
LINK O ASN B 101 CA CA B 503 1555 1555 2.64
LINK OE1 GLU B 116 CA CA B 507 1555 1555 2.42
LINK OE2 GLU B 116 CA CA B 508 1555 1555 2.30
LINK OD1 ASP B 131 CA CA B 503 1555 1555 2.49
LINK OD2 ASP B 131 CA CA B 503 1555 1555 2.37
LINK OD2 ASP B 133 CA CA B 503 1555 1555 2.48
LINK OD1 ASP B 133 CA CA B 504 1555 1555 2.35
LINK O ASN B 137 CA CA B 503 1555 1555 2.58
LINK OD1 ASP B 173 CA CA B 508 1555 1555 2.53
LINK OE2 GLU B 175 CA CA B 507 1555 1555 2.24
LINK OE1 GLU B 175 CA CA B 508 1555 1555 2.37
LINK OD2 ASP B 188 CA CA B 503 1555 1555 2.61
LINK OD1 ASP B 206 CA CA B 507 1555 1555 2.29
LINK O VAL B 207 CA CA B 507 1555 1555 2.40
LINK OD1 ASN B 208 CA CA B 506 1555 1555 2.38
LINK OD1 ASP B 209 CA CA B 507 1555 1555 2.44
LINK OD2 ASP B 209 CA CA B 508 1555 1555 2.27
LINK O ASN B 210 CA CA B 506 1555 1555 2.33
LINK OE2 GLU B 225 CA CA B 509 1555 1555 3.11
LINK OE1 GLU B 225 CA CA B 510 1555 1555 2.26
LINK OE2 GLU B 225 CA CA B 510 1555 1555 2.94
LINK OD1 ASP B 240 CA CA B 506 1555 1555 2.72
LINK OD2 ASP B 240 CA CA B 506 1555 1555 2.39
LINK OD2 ASP B 242 CA CA B 506 1555 1555 2.45
LINK OD1 ASP B 242 CA CA B 507 1555 1555 2.56
LINK O ASN B 246 CA CA B 506 1555 1555 2.42
LINK OD1 ASP B 280 CA CA B 509 1555 1555 3.08
LINK OE2 GLU B 282 CA CA B 509 1555 1555 2.64
LINK OD2 ASP B 295 CA CA B 506 1555 1555 2.53
LINK OD1 ASP B 311 CA CA B 510 1555 1555 2.38
LINK O VAL B 312 CA CA B 510 1555 1555 3.06
LINK OD1 ASN B 313 CA CA B 511 1555 1555 2.78
LINK OD1 ASP B 314 CA CA B 509 1555 1555 2.61
LINK OD2 ASP B 314 CA CA B 509 1555 1555 3.12
LINK OD1 ASP B 314 CA CA B 510 1555 1555 2.66
LINK O ASN B 315 CA CA B 511 1555 1555 2.48
LINK OD1 ASP B 345 CA CA B 511 1555 1555 2.67
LINK OD2 ASP B 345 CA CA B 511 1555 1555 2.50
LINK OD1 ASP B 347 CA CA B 510 1555 1555 2.27
LINK OD2 ASP B 347 CA CA B 510 1555 1555 2.70
LINK OD2 ASP B 347 CA CA B 511 1555 1555 3.12
LINK O ASN B 351 CA CA B 511 1555 1555 2.36
LINK OD2 ASP B 398 CA CA B 511 1555 1555 2.74
LINK OE2 GLU C 9 CA CA C 506 1555 1555 2.39
LINK OE1 GLU C 9 CA CA C 508 1555 1555 2.49
LINK OE2 GLU C 10 CA CA C 508 1555 1555 2.46
LINK OD1 ASP C 63 CA CA C 508 1555 1555 2.38
LINK OE2 GLU C 65 CA CA C 506 1555 1555 2.33
LINK OE1 GLU C 65 CA CA C 508 1555 1555 2.40
LINK OD1 ASP C 97 CA CA C 506 1555 1555 2.52
LINK O ILE C 98 CA CA C 506 1555 1555 2.34
LINK OD1 ASN C 99 CA CA C 507 1555 1555 2.51
LINK OD1 ASP C 100 CA CA C 506 1555 1555 2.39
LINK OD2 ASP C 100 CA CA C 508 1555 1555 2.44
LINK O ASN C 101 CA CA C 507 1555 1555 2.41
LINK OE1 GLU C 116 CA CA C 504 1555 1555 2.40
LINK OE2 GLU C 116 CA CA C 505 1555 1555 2.37
LINK OD2 ASP C 131 CA CA C 507 1555 1555 2.45
LINK OD1 ASP C 133 CA CA C 506 1555 1555 2.45
LINK OD2 ASP C 133 CA CA C 507 1555 1555 2.47
LINK O ASN C 137 CA CA C 507 1555 1555 2.40
LINK OD1 ASP C 173 CA CA C 505 1555 1555 2.41
LINK OE1 GLU C 175 CA CA C 504 1555 1555 2.94
LINK OE2 GLU C 175 CA CA C 504 1555 1555 2.27
LINK OE1 GLU C 175 CA CA C 505 1555 1555 2.32
LINK OD2 ASP C 188 CA CA C 507 1555 1555 2.41
LINK OD1 ASP C 206 CA CA C 504 1555 1555 2.40
LINK O VAL C 207 CA CA C 504 1555 1555 2.36
LINK OD1 ASN C 208 CA CA C 503 1555 1555 2.37
LINK OD1 ASP C 209 CA CA C 504 1555 1555 2.42
LINK OD2 ASP C 209 CA CA C 505 1555 1555 2.45
LINK O ASN C 210 CA CA C 503 1555 1555 2.44
LINK OE2 GLU C 225 CA CA C 509 1555 1555 2.47
LINK OE1 GLU C 225 CA CA C 510 1555 1555 2.28
LINK OE2 GLU C 225 CA CA C 510 1555 1555 2.92
LINK OD1 ASP C 240 CA CA C 503 1555 1555 2.49
LINK OD2 ASP C 240 CA CA C 503 1555 1555 2.27
LINK OD2 ASP C 242 CA CA C 503 1555 1555 2.34
LINK OD1 ASP C 242 CA CA C 504 1555 1555 2.42
LINK O ASN C 246 CA CA C 503 1555 1555 2.50
LINK OD1 ASP C 280 CA CA C 510 1555 1555 2.54
LINK OE2 GLU C 282 CA CA C 509 1555 1555 2.31
LINK OE1 GLU C 282 CA CA C 510 1555 1555 2.49
LINK OE2 GLU C 282 CA CA C 510 1555 1555 2.32
LINK OD2 ASP C 295 CA CA C 503 1555 1555 2.47
LINK OD1 ASP C 311 CA CA C 509 1555 1555 2.33
LINK O VAL C 312 CA CA C 509 1555 1555 2.34
LINK OD1 ASN C 313 CA CA C 511 1555 1555 2.45
LINK OD1 ASP C 314 CA CA C 509 1555 1555 2.33
LINK OD1 ASP C 314 CA CA C 510 1555 1555 2.64
LINK OD2 ASP C 314 CA CA C 510 1555 1555 2.14
LINK O ASN C 315 CA CA C 511 1555 1555 2.50
LINK OD1 ASP C 345 CA CA C 511 1555 1555 3.08
LINK OD2 ASP C 345 CA CA C 511 1555 1555 2.43
LINK OD1 ASP C 347 CA CA C 509 1555 1555 2.72
LINK OD2 ASP C 347 CA CA C 511 1555 1555 2.46
LINK O ASN C 351 CA CA C 511 1555 1555 2.48
LINK OD2 ASP C 398 CA CA C 511 1555 1555 2.55
LINK OE2 GLU D 9 CA CA D 504 1555 1555 2.31
LINK OE1 GLU D 9 CA CA D 505 1555 1555 2.45
LINK OE2 GLU D 10 CA CA D 505 1555 1555 2.41
LINK OD1 ASP D 63 CA CA D 505 1555 1555 2.58
LINK OE2 GLU D 65 CA CA D 504 1555 1555 2.97
LINK OE1 GLU D 65 CA CA D 505 1555 1555 2.44
LINK OD1 ASP D 97 CA CA D 504 1555 1555 2.55
LINK O ILE D 98 CA CA D 504 1555 1555 2.41
LINK OD1 ASN D 99 CA CA D 503 1555 1555 2.53
LINK OD1 ASP D 100 CA CA D 504 1555 1555 2.54
LINK OD2 ASP D 100 CA CA D 505 1555 1555 2.56
LINK O ASN D 101 CA CA D 503 1555 1555 2.54
LINK OE1 GLU D 116 CA CA D 507 1555 1555 2.45
LINK OE2 GLU D 116 CA CA D 508 1555 1555 2.36
LINK OD1 ASP D 131 CA CA D 503 1555 1555 2.71
LINK OD2 ASP D 131 CA CA D 503 1555 1555 2.40
LINK OD2 ASP D 133 CA CA D 503 1555 1555 2.35
LINK OD1 ASP D 133 CA CA D 504 1555 1555 2.37
LINK O ASN D 137 CA CA D 503 1555 1555 2.46
LINK OD1 ASP D 173 CA CA D 508 1555 1555 2.31
LINK OE1 GLU D 175 CA CA D 507 1555 1555 3.04
LINK OE2 GLU D 175 CA CA D 507 1555 1555 2.30
LINK OE1 GLU D 175 CA CA D 508 1555 1555 2.32
LINK OD2 ASP D 188 CA CA D 503 1555 1555 2.57
LINK OD1 ASP D 206 CA CA D 507 1555 1555 2.38
LINK O VAL D 207 CA CA D 507 1555 1555 2.48
LINK OD1 ASN D 208 CA CA D 506 1555 1555 2.24
LINK OD1 ASP D 209 CA CA D 507 1555 1555 2.38
LINK OD2 ASP D 209 CA CA D 508 1555 1555 2.33
LINK O ASN D 210 CA CA D 506 1555 1555 2.24
LINK OE2 GLU D 225 CA CA D 509 1555 1555 3.15
LINK OE1 GLU D 225 CA CA D 510 1555 1555 2.50
LINK OD1 ASP D 240 CA CA D 506 1555 1555 2.70
LINK OD2 ASP D 240 CA CA D 506 1555 1555 2.24
LINK OD2 ASP D 242 CA CA D 506 1555 1555 2.41
LINK OD1 ASP D 242 CA CA D 507 1555 1555 2.54
LINK O ASN D 246 CA CA D 506 1555 1555 2.38
LINK OD1 ASP D 280 CA CA D 510 1555 1555 2.88
LINK OE1 GLU D 282 CA CA D 510 1555 1555 2.89
LINK OD2 ASP D 295 CA CA D 506 1555 1555 2.47
LINK OD1 ASP D 311 CA CA D 509 1555 1555 2.40
LINK O VAL D 312 CA CA D 509 1555 1555 2.89
LINK OD1 ASN D 313 CA CA D 511 1555 1555 2.37
LINK OD1 ASP D 314 CA CA D 509 1555 1555 2.36
LINK OD2 ASP D 314 CA CA D 510 1555 1555 2.52
LINK O ASN D 315 CA CA D 511 1555 1555 2.69
LINK OD1 ASP D 345 CA CA D 511 1555 1555 2.60
LINK OD2 ASP D 345 CA CA D 511 1555 1555 2.36
LINK OD1 ASP D 347 CA CA D 509 1555 1555 2.80
LINK OD2 ASP D 347 CA CA D 511 1555 1555 2.50
LINK O ASN D 351 CA CA D 511 1555 1555 2.71
LINK OD2 ASP D 398 CA CA D 511 1555 1555 2.59
CISPEP 1 THR A 72 PRO A 73 0 -0.38
CISPEP 2 SER A 191 PRO A 192 0 1.22
CISPEP 3 THR A 401 PRO A 402 0 -1.90
CISPEP 4 THR B 72 PRO B 73 0 0.48
CISPEP 5 SER B 191 PRO B 192 0 1.49
CISPEP 6 THR B 401 PRO B 402 0 -1.35
CISPEP 7 THR C 72 PRO C 73 0 0.31
CISPEP 8 SER C 191 PRO C 192 0 1.53
CISPEP 9 THR C 401 PRO C 402 0 -1.65
CISPEP 10 THR D 72 PRO D 73 0 0.07
CISPEP 11 SER D 191 PRO D 192 0 1.49
CISPEP 12 THR D 401 PRO D 402 0 -2.07
CRYST1 107.867 107.867 463.081 90.00 90.00 120.00 P 31 2 1 24
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 0.009271 0.005352 0.000000 0.00000
SCALE2 0.000000 0.010705 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002159 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
