HEADER IMMUNE SYSTEM 27-JUL-11 3T5O
TITLE CRYSTAL STRUCTURE OF HUMAN COMPLEMENT COMPONENT C6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COMPLEMENT COMPONENT C6;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS MACPF, MAC, MEMBRANE ATTACK COMPLEX, COMPLEMENT, INNATE IMMUNE
KEYWDS 2 SYSTEM, BLOOD, MEMBRANE, C7, C8, C9, CYTOLYSIN, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR A.E.ALESHIN,B.STEC,L.A.BANKSTON,R.G.DISCIPIO,R.C.LIDDINGTON
REVDAT 4 29-JUL-20 3T5O 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 11-APR-12 3T5O 1 JRNL
REVDAT 2 08-FEB-12 3T5O 1 JRNL
REVDAT 1 01-FEB-12 3T5O 0
JRNL AUTH A.E.ALESHIN,I.U.SCHRAUFSTATTER,B.STEC,L.A.BANKSTON,
JRNL AUTH 2 R.C.LIDDINGTON,R.G.DISCIPIO
JRNL TITL STRUCTURE OF COMPLEMENT C6 SUGGESTS A MECHANISM FOR
JRNL TITL 2 INITIATION AND UNIDIRECTIONAL, SEQUENTIAL ASSEMBLY OF
JRNL TITL 3 MEMBRANE ATTACK COMPLEX (MAC).
JRNL REF J.BIOL.CHEM. V. 287 10210 2012
JRNL REFN ISSN 0021-9258
JRNL PMID 22267737
JRNL DOI 10.1074/JBC.M111.327809
REMARK 2
REMARK 2 RESOLUTION. 2.87 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
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) : 2.87
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.06
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 3 NUMBER OF REFLECTIONS : 35743
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2179
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 43.0618 - 6.1756 0.99 3732 233 0.2403 0.2840
REMARK 3 2 6.1756 - 4.9040 1.00 3614 221 0.2021 0.2576
REMARK 3 3 4.9040 - 4.2848 1.00 3524 254 0.1694 0.2378
REMARK 3 4 4.2848 - 3.8933 1.00 3533 223 0.2036 0.2543
REMARK 3 5 3.8933 - 3.6144 1.00 3528 205 0.2357 0.2679
REMARK 3 6 3.6144 - 3.4014 1.00 3533 200 0.2411 0.3382
REMARK 3 7 3.4014 - 3.2311 1.00 3460 249 0.2448 0.2974
REMARK 3 8 3.2311 - 3.0905 1.00 3496 234 0.2552 0.3236
REMARK 3 9 3.0905 - 2.9715 0.95 3279 229 0.2681 0.3159
REMARK 3 10 2.9715 - 2.8690 0.54 1865 131 0.3180 0.3797
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.31
REMARK 3 B_SOL : 69.70
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.420
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.340
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.64170
REMARK 3 B22 (A**2) : 1.52510
REMARK 3 B33 (A**2) : 1.11670
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.010 7123
REMARK 3 ANGLE : 1.408 9572
REMARK 3 CHIRALITY : 0.087 1037
REMARK 3 PLANARITY : 0.006 1246
REMARK 3 DIHEDRAL : 17.342 2689
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID 1:57 OR RESID 1005:1008)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.4431 1.4421 23.0140
REMARK 3 T TENSOR
REMARK 3 T11: 0.2412 T22: 0.2917
REMARK 3 T33: 0.1882 T12: 0.0472
REMARK 3 T13: -0.0825 T23: 0.0397
REMARK 3 L TENSOR
REMARK 3 L11: 1.4048 L22: 3.8599
REMARK 3 L33: 1.2824 L12: -0.8374
REMARK 3 L13: -0.0206 L23: -1.0789
REMARK 3 S TENSOR
REMARK 3 S11: 0.3157 S12: 0.1241 S13: 0.2598
REMARK 3 S21: -0.4629 S22: -0.1834 S23: -0.8039
REMARK 3 S31: 0.5236 S32: 0.2378 S33: 0.0121
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESID 58:118
REMARK 3 ORIGIN FOR THE GROUP (A): -30.1121 21.4998 -7.8984
REMARK 3 T TENSOR
REMARK 3 T11: 0.0501 T22: 0.6259
REMARK 3 T33: 0.7771 T12: -0.1274
REMARK 3 T13: -0.0086 T23: 0.3764
REMARK 3 L TENSOR
REMARK 3 L11: 0.0758 L22: 0.4540
REMARK 3 L33: 0.3185 L12: -0.1393
REMARK 3 L13: 0.0568 L23: 0.3356
REMARK 3 S TENSOR
REMARK 3 S11: 0.3141 S12: -0.0380 S13: -0.6864
REMARK 3 S21: 0.4006 S22: 0.2010 S23: 0.9423
REMARK 3 S31: 0.0286 S32: -0.1227 S33: -0.2482
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESID 119:536 OR RESID 1001:1003 OR
REMARK 3 RESID 601:608)
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5118 39.9569 -18.2742
REMARK 3 T TENSOR
REMARK 3 T11: 0.1946 T22: 0.2224
REMARK 3 T33: 0.2946 T12: -0.0068
REMARK 3 T13: -0.0043 T23: 0.1983
REMARK 3 L TENSOR
REMARK 3 L11: 2.2258 L22: 1.1197
REMARK 3 L33: 1.3988 L12: -0.9197
REMARK 3 L13: 0.7589 L23: -0.8599
REMARK 3 S TENSOR
REMARK 3 S11: -0.0293 S12: -0.1152 S13: 0.3896
REMARK 3 S21: 0.2693 S22: 0.1830 S23: -0.0304
REMARK 3 S31: -0.2712 S32: -0.1991 S33: -0.0636
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESID 537:591 OR RESID 1009:1010)
REMARK 3 ORIGIN FOR THE GROUP (A): -11.8476 34.3441 12.1780
REMARK 3 T TENSOR
REMARK 3 T11: 1.1256 T22: 1.5472
REMARK 3 T33: 1.0328 T12: 0.1483
REMARK 3 T13: 0.0887 T23: -0.3649
REMARK 3 L TENSOR
REMARK 3 L11: 2.1003 L22: 1.5299
REMARK 3 L33: 0.1981 L12: -0.9746
REMARK 3 L13: -0.5842 L23: -0.1725
REMARK 3 S TENSOR
REMARK 3 S11: -0.1034 S12: 0.5319 S13: 0.7547
REMARK 3 S21: 1.1216 S22: -0.2714 S23: 0.3385
REMARK 3 S31: -0.8302 S32: -0.0821 S33: 0.3283
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND RESID 620:681
REMARK 3 ORIGIN FOR THE GROUP (A): -62.8182 76.1868 -27.7196
REMARK 3 T TENSOR
REMARK 3 T11: 0.4184 T22: 0.2653
REMARK 3 T33: 0.3701 T12: 0.0990
REMARK 3 T13: 0.0730 T23: 0.1417
REMARK 3 L TENSOR
REMARK 3 L11: 0.7590 L22: 0.3791
REMARK 3 L33: 0.2874 L12: -0.2583
REMARK 3 L13: -0.0218 L23: 0.1540
REMARK 3 S TENSOR
REMARK 3 S11: 0.2100 S12: -0.2159 S13: 0.1306
REMARK 3 S21: -0.4696 S22: -0.1962 S23: -0.2904
REMARK 3 S31: -0.0122 S32: 0.0589 S33: 0.1417
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND RESID 682:744
REMARK 3 ORIGIN FOR THE GROUP (A): -86.3530 93.2670 -50.4192
REMARK 3 T TENSOR
REMARK 3 T11: 1.3083 T22: 0.4940
REMARK 3 T33: 0.2644 T12: 0.2036
REMARK 3 T13: -0.4004 T23: -0.0513
REMARK 3 L TENSOR
REMARK 3 L11: 0.3251 L22: 0.7507
REMARK 3 L33: 1.5754 L12: 0.0954
REMARK 3 L13: -0.0648 L23: -1.0514
REMARK 3 S TENSOR
REMARK 3 S11: 0.0722 S12: 0.3230 S13: 0.0398
REMARK 3 S21: -1.3948 S22: -0.7285 S23: 0.0752
REMARK 3 S31: -0.3921 S32: 0.8743 S33: -0.0569
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A AND RESID 750:832
REMARK 3 ORIGIN FOR THE GROUP (A):-106.5545 85.8402 -80.4326
REMARK 3 T TENSOR
REMARK 3 T11: 0.5872 T22: 0.6685
REMARK 3 T33: 1.4047 T12: -0.2277
REMARK 3 T13: 0.1490 T23: -0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 0.4876 L22: 0.0855
REMARK 3 L33: 0.3890 L12: -0.0863
REMARK 3 L13: -0.2674 L23: 0.2042
REMARK 3 S TENSOR
REMARK 3 S11: -0.0245 S12: -0.5782 S13: -0.2931
REMARK 3 S21: 0.3663 S22: 0.4233 S23: 0.2658
REMARK 3 S31: 0.4020 S32: -0.4735 S33: 0.2786
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN A AND RESID 833:913
REMARK 3 ORIGIN FOR THE GROUP (A):-120.1517 68.5702 -74.1476
REMARK 3 T TENSOR
REMARK 3 T11: 1.2988 T22: 1.0751
REMARK 3 T33: 1.9244 T12: -0.1707
REMARK 3 T13: 0.0772 T23: -0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 0.6369 L22: 0.3082
REMARK 3 L33: 1.4331 L12: -0.0761
REMARK 3 L13: 0.8550 L23: 0.2340
REMARK 3 S TENSOR
REMARK 3 S11: 0.8534 S12: 0.5652 S13: -0.4158
REMARK 3 S21: -0.0968 S22: -0.0536 S23: -0.1551
REMARK 3 S31: 0.0520 S32: 0.5814 S33: -0.8808
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE LAST DOMAIN (RESIDUES 834-913) WAS
REMARK 3 BUILT BY THREADING THE AMINO ACID SEQUENCE ON THE NMR STRUCTURE
REMARK 3 OF SAME DOMAIN FROM C7 (PDB ENTRY 2WCY). SINCE THE ELECTRON
REMARK 3 DENSITY WAS WEAK, THE SEQUENCE ANNOTATION IS NOT RELIABLE.
REMARK 4
REMARK 4 3T5O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-AUG-11.
REMARK 100 THE DEPOSITION ID IS D_1000067068.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 180
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.991
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35745
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.860
REMARK 200 RESOLUTION RANGE LOW (A) : 49.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 200 DATA REDUNDANCY : 8.300
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : 0.06900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.04
REMARK 200 COMPLETENESS FOR SHELL (%) : 60.5
REMARK 200 DATA REDUNDANCY IN SHELL : 8.50
REMARK 200 R MERGE FOR SHELL (I) : 0.50000
REMARK 200 R SYM FOR SHELL (I) : 0.50000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5 MM MES, 89 MM SODIUM CHLORIDE, 0.01
REMARK 280 MM CADMIUM CHLORIDE, PH 5.8, EVAPORATION, TEMPERATURE 284K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 73.40500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 90.07500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 73.40500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 90.07500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASN A 243
REMARK 465 GLU A 244
REMARK 465 ASN A 245
REMARK 465 GLN A 246
REMARK 465 GLN A 247
REMARK 465 GLY A 248
REMARK 465 SER A 249
REMARK 465 PHE A 250
REMARK 465 SER A 251
REMARK 465 SER A 252
REMARK 465 GLN A 253
REMARK 465 GLY A 254
REMARK 465 GLY A 255
REMARK 465 SER A 256
REMARK 465 SER A 257
REMARK 465 PHE A 258
REMARK 465 SER A 259
REMARK 465 PHE A 592
REMARK 465 SER A 593
REMARK 465 ILE A 594
REMARK 465 MET A 595
REMARK 465 GLU A 596
REMARK 465 ASN A 597
REMARK 465 ASN A 598
REMARK 465 GLY A 599
REMARK 465 GLN A 600
REMARK 465 MET A 609
REMARK 465 LYS A 610
REMARK 465 GLU A 611
REMARK 465 VAL A 612
REMARK 465 ASP A 613
REMARK 465 LEU A 614
REMARK 465 PRO A 615
REMARK 465 GLU A 616
REMARK 465 ILE A 617
REMARK 465 GLU A 618
REMARK 465 ALA A 619
REMARK 465 LEU A 745
REMARK 465 THR A 746
REMARK 465 LYS A 747
REMARK 465 LEU A 748
REMARK 465 LYS A 749
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 851 CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLU A 567 OD1 ASN A 569 1.84
REMARK 500 CB CYS A 711 SG CYS A 740 1.95
REMARK 500 ND2 ASN A 303 C2 NAG B 1 2.18
REMARK 500 OD1 ASP A 126 NH2 ARG A 150 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 PRO A 58 C - N - CA ANGL. DEV. = 10.5 DEGREES
REMARK 500 PRO A 499 C - N - CA ANGL. DEV. = 9.9 DEGREES
REMARK 500 LEU A 652 CA - CB - CG ANGL. DEV. = -15.7 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 SER A 20 92.19 80.55
REMARK 500 ASN A 53 59.80 31.87
REMARK 500 ASP A 65 158.31 -49.06
REMARK 500 ASP A 73 29.72 -144.20
REMARK 500 LEU A 86 -70.11 -66.13
REMARK 500 PHE A 91 41.39 40.00
REMARK 500 THR A 97 -22.72 -145.60
REMARK 500 ASP A 118 -54.75 -144.27
REMARK 500 LYS A 120 -100.24 -88.11
REMARK 500 CYS A 137 58.58 30.55
REMARK 500 ASN A 141 89.33 -59.25
REMARK 500 ASN A 146 15.54 55.32
REMARK 500 ASP A 148 8.85 -65.75
REMARK 500 GLU A 149 -1.57 -140.94
REMARK 500 ARG A 150 -86.67 -37.54
REMARK 500 ARG A 184 -134.65 -113.78
REMARK 500 CYS A 197 74.58 -108.40
REMARK 500 THR A 205 57.93 -143.84
REMARK 500 SER A 206 -128.50 56.06
REMARK 500 ASP A 227 -39.02 -30.71
REMARK 500 ASN A 275 -35.86 -30.98
REMARK 500 LYS A 288 157.90 174.07
REMARK 500 LYS A 297 114.12 -166.77
REMARK 500 PHE A 304 140.52 -178.65
REMARK 500 LEU A 313 172.81 -57.23
REMARK 500 ASP A 315 -70.56 -53.25
REMARK 500 HIS A 323 11.17 -59.80
REMARK 500 THR A 342 -30.84 -138.75
REMARK 500 HIS A 408 39.37 -154.93
REMARK 500 GLN A 414 2.12 -65.37
REMARK 500 LYS A 438 131.53 -25.85
REMARK 500 GLU A 453 -72.44 -47.65
REMARK 500 ASN A 458 64.43 -152.40
REMARK 500 ASP A 471 1.16 -68.23
REMARK 500 ILE A 476 -163.26 -102.61
REMARK 500 CYS A 478 79.66 -110.62
REMARK 500 PRO A 506 -46.90 -24.11
REMARK 500 ASN A 508 19.76 57.67
REMARK 500 TYR A 527 -156.28 -144.13
REMARK 500 SER A 540 154.80 -32.38
REMARK 500 ASN A 541 26.38 -143.79
REMARK 500 ASN A 569 -127.83 -101.35
REMARK 500 ASN A 570 -122.56 57.82
REMARK 500 LEU A 652 170.90 -54.24
REMARK 500 ASP A 668 -34.44 -32.30
REMARK 500 ASP A 675 62.64 -69.65
REMARK 500 PRO A 686 162.21 -49.10
REMARK 500 VAL A 687 101.01 -53.13
REMARK 500 PRO A 712 -179.52 -43.47
REMARK 500 ASN A 728 19.87 58.45
REMARK 500
REMARK 500 THIS ENTRY HAS 76 RAMACHANDRAN OUTLIERS.
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 CD A1001 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 135 O
REMARK 620 2 ASN A 138 OD1 99.6
REMARK 620 3 GLU A 140 O 151.7 92.3
REMARK 620 4 ASP A 142 OD2 80.1 86.8 75.0
REMARK 620 5 ASP A 148 OD1 78.6 175.8 87.8 89.2
REMARK 620 6 GLU A 149 OE1 124.3 93.5 80.0 155.0 90.6
REMARK 620 N 1 2 3 4 5
DBREF 3T5O A 1 913 UNP P13671 CO6_HUMAN 22 934
SEQRES 1 A 913 CYS PHE CYS ASP HIS TYR ALA TRP THR GLN TRP THR SER
SEQRES 2 A 913 CYS SER LYS THR CYS ASN SER GLY THR GLN SER ARG HIS
SEQRES 3 A 913 ARG GLN ILE VAL VAL ASP LYS TYR TYR GLN GLU ASN PHE
SEQRES 4 A 913 CYS GLU GLN ILE CYS SER LYS GLN GLU THR ARG GLU CYS
SEQRES 5 A 913 ASN TRP GLN ARG CYS PRO ILE ASN CYS LEU LEU GLY ASP
SEQRES 6 A 913 PHE GLY PRO TRP SER ASP CYS ASP PRO CYS ILE GLU LYS
SEQRES 7 A 913 GLN SER LYS VAL ARG SER VAL LEU ARG PRO SER GLN PHE
SEQRES 8 A 913 GLY GLY GLN PRO CYS THR ALA PRO LEU VAL ALA PHE GLN
SEQRES 9 A 913 PRO CYS ILE PRO SER LYS LEU CYS LYS ILE GLU GLU ALA
SEQRES 10 A 913 ASP CYS LYS ASN LYS PHE ARG CYS ASP SER GLY ARG CYS
SEQRES 11 A 913 ILE ALA ARG LYS LEU GLU CYS ASN GLY GLU ASN ASP CYS
SEQRES 12 A 913 GLY ASP ASN SER ASP GLU ARG ASP CYS GLY ARG THR LYS
SEQRES 13 A 913 ALA VAL CYS THR ARG LYS TYR ASN PRO ILE PRO SER VAL
SEQRES 14 A 913 GLN LEU MET GLY ASN GLY PHE HIS PHE LEU ALA GLY GLU
SEQRES 15 A 913 PRO ARG GLY GLU VAL LEU ASP ASN SER PHE THR GLY GLY
SEQRES 16 A 913 ILE CYS LYS THR VAL LYS SER SER ARG THR SER ASN PRO
SEQRES 17 A 913 TYR ARG VAL PRO ALA ASN LEU GLU ASN VAL GLY PHE GLU
SEQRES 18 A 913 VAL GLN THR ALA GLU ASP ASP LEU LYS THR ASP PHE TYR
SEQRES 19 A 913 LYS ASP LEU THR SER LEU GLY HIS ASN GLU ASN GLN GLN
SEQRES 20 A 913 GLY SER PHE SER SER GLN GLY GLY SER SER PHE SER VAL
SEQRES 21 A 913 PRO ILE PHE TYR SER SER LYS ARG SER GLU ASN ILE ASN
SEQRES 22 A 913 HIS ASN SER ALA PHE LYS GLN ALA ILE GLN ALA SER HIS
SEQRES 23 A 913 LYS LYS ASP SER SER PHE ILE ARG ILE HIS LYS VAL MET
SEQRES 24 A 913 LYS VAL LEU ASN PHE THR THR LYS ALA LYS ASP LEU HIS
SEQRES 25 A 913 LEU SER ASP VAL PHE LEU LYS ALA LEU ASN HIS LEU PRO
SEQRES 26 A 913 LEU GLU TYR ASN SER ALA LEU TYR SER ARG ILE PHE ASP
SEQRES 27 A 913 ASP PHE GLY THR HIS TYR PHE THR SER GLY SER LEU GLY
SEQRES 28 A 913 GLY VAL TYR ASP LEU LEU TYR GLN PHE SER SER GLU GLU
SEQRES 29 A 913 LEU LYS ASN SER GLY LEU THR GLU GLU GLU ALA LYS HIS
SEQRES 30 A 913 CYS VAL ARG ILE GLU THR LYS LYS ARG VAL LEU PHE ALA
SEQRES 31 A 913 LYS LYS THR LYS VAL GLU HIS ARG CYS THR THR ASN LYS
SEQRES 32 A 913 LEU SER GLU LYS HIS GLU GLY SER PHE ILE GLN GLY ALA
SEQRES 33 A 913 GLU LYS SER ILE SER LEU ILE ARG GLY GLY ARG SER GLU
SEQRES 34 A 913 TYR GLY ALA ALA LEU ALA TRP GLU LYS GLY SER SER GLY
SEQRES 35 A 913 LEU GLU GLU LYS THR PHE SER GLU TRP LEU GLU SER VAL
SEQRES 36 A 913 LYS GLU ASN PRO ALA VAL ILE ASP PHE GLU LEU ALA PRO
SEQRES 37 A 913 ILE VAL ASP LEU VAL ARG ASN ILE PRO CYS ALA VAL THR
SEQRES 38 A 913 LYS ARG ASN ASN LEU ARG LYS ALA LEU GLN GLU TYR ALA
SEQRES 39 A 913 ALA LYS PHE ASP PRO CYS GLN CYS ALA PRO CYS PRO ASN
SEQRES 40 A 913 ASN GLY ARG PRO THR LEU SER GLY THR GLU CYS LEU CYS
SEQRES 41 A 913 VAL CYS GLN SER GLY THR TYR GLY GLU ASN CYS GLU LYS
SEQRES 42 A 913 GLN SER PRO ASP TYR LYS SER ASN ALA VAL ASP GLY GLN
SEQRES 43 A 913 TRP GLY CYS TRP SER SER TRP SER THR CYS ASP ALA THR
SEQRES 44 A 913 TYR LYS ARG SER ARG THR ARG GLU CYS ASN ASN PRO ALA
SEQRES 45 A 913 PRO GLN ARG GLY GLY LYS ARG CYS GLU GLY GLU LYS ARG
SEQRES 46 A 913 GLN GLU GLU ASP CYS THR PHE SER ILE MET GLU ASN ASN
SEQRES 47 A 913 GLY GLN PRO CYS ILE ASN ASP ASP GLU GLU MET LYS GLU
SEQRES 48 A 913 VAL ASP LEU PRO GLU ILE GLU ALA ASP SER GLY CYS PRO
SEQRES 49 A 913 GLN PRO VAL PRO PRO GLU ASN GLY PHE ILE ARG ASN GLU
SEQRES 50 A 913 LYS GLN LEU TYR LEU VAL GLY GLU ASP VAL GLU ILE SER
SEQRES 51 A 913 CYS LEU THR GLY PHE GLU THR VAL GLY TYR GLN TYR PHE
SEQRES 52 A 913 ARG CYS LEU PRO ASP GLY THR TRP ARG GLN GLY ASP VAL
SEQRES 53 A 913 GLU CYS GLN ARG THR GLU CYS ILE LYS PRO VAL VAL GLN
SEQRES 54 A 913 GLU VAL LEU THR ILE THR PRO PHE GLN ARG LEU TYR ARG
SEQRES 55 A 913 ILE GLY GLU SER ILE GLU LEU THR CYS PRO LYS GLY PHE
SEQRES 56 A 913 VAL VAL ALA GLY PRO SER ARG TYR THR CYS GLN GLY ASN
SEQRES 57 A 913 SER TRP THR PRO PRO ILE SER ASN SER LEU THR CYS GLU
SEQRES 58 A 913 LYS ASP THR LEU THR LYS LEU LYS GLY HIS CYS GLN LEU
SEQRES 59 A 913 GLY GLN LYS GLN SER GLY SER GLU CYS ILE CYS MET SER
SEQRES 60 A 913 PRO GLU GLU ASP CYS SER HIS HIS SER GLU ASP LEU CYS
SEQRES 61 A 913 VAL PHE ASP THR ASP SER ASN ASP TYR PHE THR SER PRO
SEQRES 62 A 913 ALA CYS LYS PHE LEU ALA GLU LYS CYS LEU ASN ASN GLN
SEQRES 63 A 913 GLN LEU HIS PHE LEU HIS ILE GLY SER CYS GLN ASP GLY
SEQRES 64 A 913 ARG GLN LEU GLU TRP GLY LEU GLU ARG THR ARG LEU SER
SEQRES 65 A 913 SER ASN SER THR LYS LYS GLU SER CYS GLY TYR ASP THR
SEQRES 66 A 913 CYS TYR ASP TRP GLU LYS CYS SER ALA SER THR SER LYS
SEQRES 67 A 913 CYS VAL CYS LEU LEU PRO PRO GLN CYS PHE LYS GLY GLY
SEQRES 68 A 913 ASN GLN LEU TYR CYS VAL LYS MET GLY SER SER THR SER
SEQRES 69 A 913 GLU LYS THR LEU ASN ILE CYS GLU VAL GLY THR ILE ARG
SEQRES 70 A 913 CYS ALA ASN ARG LYS MET GLU ILE LEU HIS PRO GLY LYS
SEQRES 71 A 913 CYS LEU ALA
MODRES 3T5O ASN A 303 ASN GLYCOSYLATION SITE
MODRES 3T5O THR A 17 THR GLYCOSYLATION SITE
MODRES 3T5O THR A 371 THR GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET FUC C 1 10
HET BGC C 2 11
HET CD A1001 1
HET FUL A1004 10
HET MAN A1007 11
HET MAN A1008 11
HET MAN A1009 11
HET MAN A1010 11
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM BGC BETA-D-GLUCOPYRANOSE
HETNAM CD CADMIUM ION
HETNAM FUL BETA-L-FUCOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 3 FUC C6 H12 O5
FORMUL 3 BGC C6 H12 O6
FORMUL 4 CD CD 2+
FORMUL 5 FUL C6 H12 O5
FORMUL 6 MAN 4(C6 H12 O6)
HELIX 1 1 PHE A 2 TYR A 6 5 5
HELIX 2 2 ASP A 32 ASN A 38 1 7
HELIX 3 3 PHE A 39 CYS A 44 1 6
HELIX 4 4 ALA A 132 GLU A 136 5 5
HELIX 5 5 ASN A 146 ARG A 150 5 5
HELIX 6 6 SER A 168 MET A 172 5 5
HELIX 7 7 ASP A 236 HIS A 242 5 7
HELIX 8 8 SER A 276 LYS A 287 1 12
HELIX 9 9 SER A 314 HIS A 323 1 10
HELIX 10 10 ASN A 329 GLY A 341 1 13
HELIX 11 11 SER A 362 GLY A 369 1 8
HELIX 12 12 THR A 371 VAL A 387 1 17
HELIX 13 13 GLU A 396 THR A 400 5 5
HELIX 14 14 LEU A 404 GLU A 409 5 6
HELIX 15 15 PHE A 412 ALA A 416 5 5
HELIX 16 16 ARG A 427 ALA A 435 1 9
HELIX 17 17 GLU A 444 ASN A 458 1 15
HELIX 18 18 VAL A 470 VAL A 473 5 4
HELIX 19 19 CYS A 478 LYS A 496 1 19
HELIX 20 20 PHE A 497 CYS A 502 5 6
HELIX 21 21 ASP A 785 ASN A 787 5 3
HELIX 22 22 ALA A 794 CYS A 802 1 9
HELIX 23 23 LEU A 803 GLN A 806 5 4
HELIX 24 24 GLY A 819 SER A 832 1 14
SHEET 1 A 2 GLY A 21 HIS A 26 0
SHEET 2 A 2 GLN A 47 CYS A 52 -1 O GLU A 48 N ARG A 25
SHEET 1 B 2 LEU A 62 LEU A 63 0
SHEET 2 B 2 VAL A 85 ARG A 87 -1 O ARG A 87 N LEU A 62
SHEET 1 C 2 LYS A 78 GLN A 79 0
SHEET 2 C 2 GLN A 104 PRO A 105 -1 O GLN A 104 N GLN A 79
SHEET 1 D 3 SER A 89 GLN A 90 0
SHEET 2 D 3 GLU A 517 VAL A 521 1 O CYS A 518 N SER A 89
SHEET 3 D 3 ARG A 510 SER A 514 -1 N SER A 514 O GLU A 517
SHEET 1 E 2 PHE A 123 ARG A 124 0
SHEET 2 E 2 CYS A 130 ILE A 131 -1 O ILE A 131 N PHE A 123
SHEET 1 F 2 ASN A 164 PRO A 165 0
SHEET 2 F 2 TYR A 209 ARG A 210 1 O ARG A 210 N ASN A 164
SHEET 1 G 5 LEU A 215 GLY A 219 0
SHEET 2 G 5 SER A 290 THR A 306 -1 O THR A 305 N ASN A 217
SHEET 3 G 5 HIS A 343 SER A 361 -1 O THR A 346 N THR A 306
SHEET 4 G 5 ASN A 174 HIS A 177 -1 N PHE A 176 O HIS A 343
SHEET 5 G 5 GLU A 182 GLU A 186 -1 O ARG A 184 N GLY A 175
SHEET 1 H 4 LEU A 229 TYR A 234 0
SHEET 2 H 4 SER A 290 THR A 306 -1 O PHE A 292 N TYR A 234
SHEET 3 H 4 HIS A 343 SER A 361 -1 O THR A 346 N THR A 306
SHEET 4 H 4 LYS A 418 SER A 421 -1 O ILE A 420 N LEU A 357
SHEET 1 I 4 ALA A 460 PRO A 468 0
SHEET 2 I 4 HIS A 343 SER A 361 -1 N GLY A 351 O ALA A 460
SHEET 3 I 4 SER A 290 THR A 306 -1 N THR A 306 O THR A 346
SHEET 4 I 4 LEU A 215 GLY A 219 -1 N ASN A 217 O THR A 305
SHEET 1 J 2 ARG A 562 THR A 565 0
SHEET 2 J 2 ARG A 585 GLU A 588 -1 O GLN A 586 N ARG A 564
SHEET 1 K 4 GLY A 632 ILE A 634 0
SHEET 2 K 4 ASP A 646 CYS A 651 -1 O SER A 650 N PHE A 633
SHEET 3 K 4 TYR A 662 CYS A 665 -1 O PHE A 663 N VAL A 647
SHEET 4 K 4 TRP A 671 ARG A 672 -1 O ARG A 672 N ARG A 664
SHEET 1 L 2 PHE A 655 VAL A 658 0
SHEET 2 L 2 GLU A 677 ARG A 680 -1 O GLN A 679 N GLU A 656
SHEET 1 M 2 GLU A 682 ILE A 684 0
SHEET 2 M 2 LEU A 700 ARG A 702 -1 O TYR A 701 N CYS A 683
SHEET 1 N 2 SER A 706 GLU A 708 0
SHEET 2 N 2 ARG A 722 THR A 724 -1 O TYR A 723 N ILE A 707
SHEET 1 O 2 PHE A 715 VAL A 716 0
SHEET 2 O 2 GLU A 741 LYS A 742 -1 O GLU A 741 N VAL A 716
SHEET 1 P 2 GLN A 756 SER A 759 0
SHEET 2 P 2 GLU A 762 CYS A 765 -1 O ILE A 764 N LYS A 757
SHEET 1 Q 3 ASP A 788 PRO A 793 0
SHEET 2 Q 3 ASP A 778 ASP A 783 -1 N LEU A 779 O SER A 792
SHEET 3 Q 3 LEU A 808 ILE A 813 -1 O HIS A 809 N PHE A 782
SSBOND 1 CYS A 1 CYS A 40 1555 1555 2.04
SSBOND 2 CYS A 3 CYS A 44 1555 1555 2.02
SSBOND 3 CYS A 14 CYS A 52 1555 1555 2.03
SSBOND 4 CYS A 18 CYS A 57 1555 1555 2.02
SSBOND 5 CYS A 61 CYS A 96 1555 1555 2.03
SSBOND 6 CYS A 72 CYS A 106 1555 1555 2.03
SSBOND 7 CYS A 75 CYS A 112 1555 1555 2.04
SSBOND 8 CYS A 119 CYS A 130 1555 1555 2.03
SSBOND 9 CYS A 125 CYS A 143 1555 1555 2.04
SSBOND 10 CYS A 137 CYS A 152 1555 1555 2.03
SSBOND 11 CYS A 159 CYS A 197 1555 1555 2.04
SSBOND 12 CYS A 378 CYS A 399 1555 1555 2.07
SSBOND 13 CYS A 478 CYS A 602 1555 1555 2.02
SSBOND 14 CYS A 500 CYS A 549 1555 1555 2.05
SSBOND 15 CYS A 502 CYS A 518 1555 1555 2.03
SSBOND 16 CYS A 505 CYS A 520 1555 1555 2.05
SSBOND 17 CYS A 522 CYS A 531 1555 1555 2.06
SSBOND 18 CYS A 556 CYS A 590 1555 1555 2.04
SSBOND 19 CYS A 568 CYS A 580 1555 1555 2.03
SSBOND 20 CYS A 623 CYS A 665 1555 1555 2.03
SSBOND 21 CYS A 651 CYS A 678 1555 1555 2.08
SSBOND 22 CYS A 683 CYS A 725 1555 1555 2.03
SSBOND 23 CYS A 711 CYS A 740 1555 1555 2.03
SSBOND 24 CYS A 752 CYS A 763 1555 1555 1.94
SSBOND 25 CYS A 765 CYS A 802 1555 1555 2.03
SSBOND 26 CYS A 772 CYS A 795 1555 1555 2.04
SSBOND 27 CYS A 780 CYS A 816 1555 1555 2.04
SSBOND 28 CYS A 841 CYS A 852 1555 1555 2.04
SSBOND 29 CYS A 846 CYS A 859 1555 1555 2.03
SSBOND 30 CYS A 861 CYS A 898 1555 1555 2.03
SSBOND 31 CYS A 867 CYS A 891 1555 1555 2.03
SSBOND 32 CYS A 876 CYS A 911 1555 1555 2.03
LINK CD1 TRP A 8 C1 MAN A1008 1555 1555 1.44
LINK CD1 TRP A 11 C1 MAN A1007 1555 1555 1.44
LINK OG1 THR A 17 C1 FUC C 1 1555 1555 1.44
LINK ND2 ASN A 303 C1 NAG B 1 1555 1555 1.43
LINK OG1 THR A 371 C1 FUL A1004 1555 1555 1.46
LINK CD1 TRP A 547 C1 MAN A1010 1555 1555 1.46
LINK CD1 TRP A 550 C1 MAN A1009 1555 1555 1.45
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.45
LINK O3 FUC C 1 C1 BGC C 2 1555 1555 1.43
LINK O LEU A 135 CD CD A1001 1555 1555 2.41
LINK OD1 ASN A 138 CD CD A1001 1555 1555 2.40
LINK O GLU A 140 CD CD A1001 1555 1555 2.39
LINK OD2 ASP A 142 CD CD A1001 1555 1555 2.41
LINK OD1 ASP A 148 CD CD A1001 1555 1555 2.42
LINK OE1 GLU A 149 CD CD A1001 1555 1555 2.42
CISPEP 1 THR A 695 PRO A 696 0 2.85
CISPEP 2 THR A 731 PRO A 732 0 -16.81
CISPEP 3 TYR A 843 ASP A 844 0 -3.38
CRYST1 146.810 180.150 60.530 90.00 90.00 90.00 P 21 21 2 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006812 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005551 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016521 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
