HEADER IMMUNE SYSTEM 24-SEP-13 4MWF
TITLE STRUCTURE OF HEPATITIS C VIRUS ENVELOPE GLYCOPROTEIN E2 CORE BOUND TO
TITLE 2 BROADLY NEUTRALIZING ANTIBODY AR3C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FAB AR3C HEAVY CHAIN;
COMPND 3 CHAIN: A, H;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: FAB AR3C LIGHT CHAIN;
COMPND 7 CHAIN: B, L;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: ENVELOPE GLYCOPROTEIN E2;
COMPND 11 CHAIN: C, D;
COMPND 12 ENGINEERED: YES;
COMPND 13 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS (ISOLATE H);
SOURCE 15 ORGANISM_COMMON: HCV;
SOURCE 16 ORGANISM_TAXID: 11108;
SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 18 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 20 EXPRESSION_SYSTEM_CELL_LINE: HEK 293 FREESTYLE
KEYWDS IMMUNOGLOBULIN FOLD, HCV E2, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR L.KONG,I.A.WILSON,M.LAW
REVDAT 4 29-JUL-20 4MWF 1 COMPND REMARK SEQADV HETNAM
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 02-AUG-17 4MWF 1 SOURCE REMARK
REVDAT 2 24-SEP-14 4MWF 1 KEYWDS
REVDAT 1 11-DEC-13 4MWF 0
JRNL AUTH L.KONG,E.GIANG,T.NIEUSMA,R.U.KADAM,K.E.COGBURN,Y.HUA,X.DAI,
JRNL AUTH 2 R.L.STANFIELD,D.R.BURTON,A.B.WARD,I.A.WILSON,M.LAW
JRNL TITL HEPATITIS C VIRUS E2 ENVELOPE GLYCOPROTEIN CORE STRUCTURE.
JRNL REF SCIENCE V. 342 1090 2013
JRNL REFN ISSN 0036-8075
JRNL PMID 24288331
JRNL DOI 10.1126/SCIENCE.1243876
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
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) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.08
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 3 NUMBER OF REFLECTIONS : 45926
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 2312
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.0860 - 6.7941 0.93 2784 151 0.2353 0.2658
REMARK 3 2 6.7941 - 5.3949 0.96 2758 142 0.2175 0.2401
REMARK 3 3 5.3949 - 4.7135 0.96 2681 148 0.1765 0.2182
REMARK 3 4 4.7135 - 4.2829 0.97 2681 158 0.1766 0.2143
REMARK 3 5 4.2829 - 3.9760 0.96 2666 155 0.2030 0.2203
REMARK 3 6 3.9760 - 3.7417 0.96 2716 114 0.2179 0.2912
REMARK 3 7 3.7417 - 3.5544 0.96 2641 142 0.2399 0.2859
REMARK 3 8 3.5544 - 3.3997 0.97 2626 152 0.2579 0.2948
REMARK 3 9 3.3997 - 3.2688 0.97 2687 147 0.2569 0.3084
REMARK 3 10 3.2688 - 3.1561 0.97 2618 153 0.2622 0.2868
REMARK 3 11 3.1561 - 3.0574 0.96 2661 158 0.2698 0.3228
REMARK 3 12 3.0574 - 2.9700 0.96 2617 115 0.2757 0.3084
REMARK 3 13 2.9700 - 2.8918 0.92 2531 126 0.2993 0.3217
REMARK 3 14 2.8918 - 2.8213 0.90 2448 123 0.3197 0.4044
REMARK 3 15 2.8213 - 2.7571 0.87 2338 131 0.3176 0.3715
REMARK 3 16 2.7571 - 2.6985 0.82 2260 107 0.3185 0.4037
REMARK 3 17 2.6985 - 2.6445 0.70 1901 90 0.3130 0.3948
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.390
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.710
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 9721
REMARK 3 ANGLE : 1.275 13227
REMARK 3 CHIRALITY : 0.054 1512
REMARK 3 PLANARITY : 0.014 1666
REMARK 3 DIHEDRAL : 17.670 3489
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 4MWF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-OCT-13.
REMARK 100 THE DEPOSITION ID IS D_1000082450.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JAN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 5
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46174
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 49.090
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG 4000, 10% (V/V)
REMARK 280 ISOPROPANOL, AND 0.1 M HEPES PH 7.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 23.56600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 104.98150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 83.27650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 104.98150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.56600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 83.27650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, H, L, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 GLU A 0
REMARK 465 VAL A 1
REMARK 465 GLN A 2
REMARK 465 SER A 130
REMARK 465 THR A 131
REMARK 465 SER A 132
REMARK 465 SER A 215
REMARK 465 CYS A 216
REMARK 465 GLY A 217
REMARK 465 SER A 218
REMARK 465 GLU B 1
REMARK 465 ILE B 2
REMARK 465 CYS B 214
REMARK 465 GLN C 412
REMARK 465 LEU C 413
REMARK 465 ILE C 414
REMARK 465 ASN C 415
REMARK 465 THR C 416
REMARK 465 ASN C 417
REMARK 465 GLY C 418
REMARK 465 SER C 419
REMARK 465 TRP C 420
REMARK 465 PRO C 453
REMARK 465 GLU C 454
REMARK 465 ARG C 455
REMARK 465 LEU C 456
REMARK 465 ALA C 457
REMARK 465 SER C 458
REMARK 465 CYS C 459
REMARK 465 GLY C 482
REMARK 465 SER C 483
REMARK 465 SER C 484
REMARK 465 GLY C 485
REMARK 465 CYS C 486
REMARK 465 TRP C 487
REMARK 465 HIS C 488
REMARK 465 TYR C 489
REMARK 465 PRO C 490
REMARK 465 PRO C 491
REMARK 465 THR C 542
REMARK 465 ARG C 543
REMARK 465 PRO C 544
REMARK 465 PRO C 545
REMARK 465 LEU C 546
REMARK 465 GLY C 547
REMARK 465 PHE C 586
REMARK 465 ARG C 587
REMARK 465 LYS C 588
REMARK 465 HIS C 589
REMARK 465 PRO C 590
REMARK 465 GLU C 591
REMARK 465 ALA C 592
REMARK 465 THR C 593
REMARK 465 TYR C 594
REMARK 465 SER C 595
REMARK 465 ARG C 596
REMARK 465 GLN D 412
REMARK 465 LEU D 413
REMARK 465 ILE D 414
REMARK 465 ASN D 415
REMARK 465 THR D 416
REMARK 465 ASN D 417
REMARK 465 GLY D 418
REMARK 465 SER D 419
REMARK 465 TRP D 420
REMARK 465 PRO D 453
REMARK 465 GLU D 454
REMARK 465 ARG D 455
REMARK 465 LEU D 456
REMARK 465 ALA D 457
REMARK 465 SER D 458
REMARK 465 CYS D 459
REMARK 465 GLY D 482
REMARK 465 SER D 483
REMARK 465 SER D 484
REMARK 465 GLY D 485
REMARK 465 CYS D 486
REMARK 465 TRP D 487
REMARK 465 HIS D 488
REMARK 465 TYR D 489
REMARK 465 PRO D 490
REMARK 465 PRO D 491
REMARK 465 VAL D 574
REMARK 465 GLY D 575
REMARK 465 ASP D 576
REMARK 465 ASN D 577
REMARK 465 PHE D 586
REMARK 465 ARG D 587
REMARK 465 LYS D 588
REMARK 465 HIS D 589
REMARK 465 PRO D 590
REMARK 465 GLU D 591
REMARK 465 ALA D 592
REMARK 465 THR D 593
REMARK 465 TYR D 594
REMARK 465 SER D 595
REMARK 465 ARG D 596
REMARK 465 GLU H 0
REMARK 465 VAL H 1
REMARK 465 CYS H 216
REMARK 465 GLY H 217
REMARK 465 SER H 218
REMARK 465 GLU L 1
REMARK 465 CYS L 214
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 SG CYS C 452 SG CYS C 620 1.65
REMARK 500 SG CYS C 429 SG CYS C 503 1.67
REMARK 500 O3 BMA E 3 O5 MAN E 4 2.01
REMARK 500 OG1 THR C 578 O CYS C 581 2.07
REMARK 500 ND2 ASN D 556 C2 NAG G 1 2.11
REMARK 500 ND2 ASN C 556 C2 NAG F 1 2.11
REMARK 500 C6 MAN E 7 C1 MAN E 8 2.14
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 ILE A 48 -60.03 -93.75
REMARK 500 SER A 82B 61.11 61.29
REMARK 500 THR A 97 101.13 90.30
REMARK 500 SER B 30 -118.42 54.19
REMARK 500 ALA B 51 -39.03 67.59
REMARK 500 TYR B 92 -68.62 -130.70
REMARK 500 SER C 599 -125.12 60.39
REMARK 500 ALA D 531 -120.58 59.09
REMARK 500 LEU D 539 -70.28 -100.52
REMARK 500 PRO D 582 154.98 -47.99
REMARK 500 LEU H 45 151.56 -48.32
REMARK 500 THR H 97 72.76 58.04
REMARK 500 SER L 30 -130.65 55.91
REMARK 500 ALA L 51 -45.48 72.60
REMARK 500 ASP L 82 0.28 -69.68
REMARK 500 SER L 83 98.91 -69.79
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4MWF C 412 459 UNP P27958 POLG_HCVH 412 459
DBREF 4MWF C 486 645 UNP P27958 POLG_HCVH 486 645
DBREF 4MWF D 412 459 UNP P27958 POLG_HCVH 412 459
DBREF 4MWF D 486 645 UNP P27958 POLG_HCVH 486 645
DBREF 4MWF A 0 218 PDB 4MWF 4MWF 0 218
DBREF 4MWF H 0 218 PDB 4MWF 4MWF 0 218
DBREF 4MWF B 1 214 PDB 4MWF 4MWF 1 214
DBREF 4MWF L 1 214 PDB 4MWF 4MWF 1 214
SEQADV 4MWF ASP C 448 UNP P27958 ASN 448 ENGINEERED MUTATION
SEQADV 4MWF GLY C 482 UNP P27958 LINKER
SEQADV 4MWF SER C 483 UNP P27958 LINKER
SEQADV 4MWF SER C 484 UNP P27958 LINKER
SEQADV 4MWF GLY C 485 UNP P27958 LINKER
SEQADV 4MWF ASP C 576 UNP P27958 ASN 576 ENGINEERED MUTATION
SEQADV 4MWF HIS C 589 UNP P27958 TYR 589 VARIANT
SEQADV 4MWF TRP C 602 UNP P27958 ARG 602 VARIANT
SEQADV 4MWF ASP D 448 UNP P27958 ASN 448 ENGINEERED MUTATION
SEQADV 4MWF GLY D 482 UNP P27958 LINKER
SEQADV 4MWF SER D 483 UNP P27958 LINKER
SEQADV 4MWF SER D 484 UNP P27958 LINKER
SEQADV 4MWF GLY D 485 UNP P27958 LINKER
SEQADV 4MWF ASP D 576 UNP P27958 ASN 576 ENGINEERED MUTATION
SEQADV 4MWF HIS D 589 UNP P27958 TYR 589 VARIANT
SEQADV 4MWF TRP D 602 UNP P27958 ARG 602 VARIANT
SEQRES 1 A 233 GLU VAL GLN LEU LEU GLU GLN SER GLY ALA GLU VAL LYS
SEQRES 2 A 233 LYS PRO GLY SER SER VAL LYS VAL SER CYS GLU THR SER
SEQRES 3 A 233 GLY GLY THR PHE ASP ASN TYR ALA LEU ASN TRP VAL ARG
SEQRES 4 A 233 GLN ALA PRO GLY GLN GLY LEU GLU TRP ILE GLY GLY VAL
SEQRES 5 A 233 VAL PRO LEU PHE GLY THR THR ARG ASN ALA GLN LYS PHE
SEQRES 6 A 233 GLN GLY ARG VAL THR ILE SER ASP ASP LYS SER THR GLY
SEQRES 7 A 233 THR GLY HIS MET GLU LEU ARG SER LEU ARG SER GLU ASP
SEQRES 8 A 233 THR ALA VAL TYR TYR CYS VAL ARG SER VAL THR PRO ARG
SEQRES 9 A 233 TYR CYS GLY GLY GLY PHE CYS TYR GLY GLU PHE ASP TYR
SEQRES 10 A 233 TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER
SEQRES 11 A 233 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER
SEQRES 12 A 233 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU
SEQRES 13 A 233 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP
SEQRES 14 A 233 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO
SEQRES 15 A 233 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER
SEQRES 16 A 233 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR
SEQRES 17 A 233 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS
SEQRES 18 A 233 VAL ASP LYS LYS VAL GLU PRO LYS SER CYS GLY SER
SEQRES 1 B 214 GLU ILE GLU LEU THR GLN SER PRO ALA THR LEU SER VAL
SEQRES 2 B 214 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER
SEQRES 3 B 214 GLN SER VAL SER SER ASN LEU ALA TRP TYR GLN GLN LYS
SEQRES 4 B 214 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER
SEQRES 5 B 214 THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER
SEQRES 6 B 214 GLY SER GLY THR GLU PHE THR LEU THR VAL SER ARG LEU
SEQRES 7 B 214 GLU PRO GLU ASP SER ALA VAL TYR PHE CYS GLN GLN TYR
SEQRES 8 B 214 TYR ARG SER PRO LEU THR PHE GLY GLY GLY THR LYS VAL
SEQRES 9 B 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 B 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 B 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 B 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 B 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 B 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 B 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU
SEQRES 16 B 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 B 214 PHE ASN ARG GLY GLU CYS
SEQRES 1 C 212 GLN LEU ILE ASN THR ASN GLY SER TRP HIS ILE ASN SER
SEQRES 2 C 212 THR ALA LEU ASN CYS ASN GLU SER LEU ASN THR GLY TRP
SEQRES 3 C 212 LEU ALA GLY LEU PHE TYR GLN HIS LYS PHE ASP SER SER
SEQRES 4 C 212 GLY CYS PRO GLU ARG LEU ALA SER CYS GLY SER SER GLY
SEQRES 5 C 212 CYS TRP HIS TYR PRO PRO ARG PRO CYS GLY ILE VAL PRO
SEQRES 6 C 212 ALA LYS SER VAL CYS GLY PRO VAL TYR CYS PHE THR PRO
SEQRES 7 C 212 SER PRO VAL VAL VAL GLY THR THR ASP ARG SER GLY ALA
SEQRES 8 C 212 PRO THR TYR SER TRP GLY ALA ASN ASP THR ASP VAL PHE
SEQRES 9 C 212 VAL LEU ASN ASN THR ARG PRO PRO LEU GLY ASN TRP PHE
SEQRES 10 C 212 GLY CYS THR TRP MET ASN SER THR GLY PHE THR LYS VAL
SEQRES 11 C 212 CYS GLY ALA PRO PRO CYS VAL ILE GLY GLY VAL GLY ASP
SEQRES 12 C 212 ASN THR LEU LEU CYS PRO THR ASP CYS PHE ARG LYS HIS
SEQRES 13 C 212 PRO GLU ALA THR TYR SER ARG CYS GLY SER GLY PRO TRP
SEQRES 14 C 212 ILE THR PRO ARG CYS MET VAL ASP TYR PRO TYR ARG LEU
SEQRES 15 C 212 TRP HIS TYR PRO CYS THR ILE ASN TYR THR ILE PHE LYS
SEQRES 16 C 212 VAL ARG MET TYR VAL GLY GLY VAL GLU HIS ARG LEU GLU
SEQRES 17 C 212 ALA ALA CYS ASN
SEQRES 1 D 212 GLN LEU ILE ASN THR ASN GLY SER TRP HIS ILE ASN SER
SEQRES 2 D 212 THR ALA LEU ASN CYS ASN GLU SER LEU ASN THR GLY TRP
SEQRES 3 D 212 LEU ALA GLY LEU PHE TYR GLN HIS LYS PHE ASP SER SER
SEQRES 4 D 212 GLY CYS PRO GLU ARG LEU ALA SER CYS GLY SER SER GLY
SEQRES 5 D 212 CYS TRP HIS TYR PRO PRO ARG PRO CYS GLY ILE VAL PRO
SEQRES 6 D 212 ALA LYS SER VAL CYS GLY PRO VAL TYR CYS PHE THR PRO
SEQRES 7 D 212 SER PRO VAL VAL VAL GLY THR THR ASP ARG SER GLY ALA
SEQRES 8 D 212 PRO THR TYR SER TRP GLY ALA ASN ASP THR ASP VAL PHE
SEQRES 9 D 212 VAL LEU ASN ASN THR ARG PRO PRO LEU GLY ASN TRP PHE
SEQRES 10 D 212 GLY CYS THR TRP MET ASN SER THR GLY PHE THR LYS VAL
SEQRES 11 D 212 CYS GLY ALA PRO PRO CYS VAL ILE GLY GLY VAL GLY ASP
SEQRES 12 D 212 ASN THR LEU LEU CYS PRO THR ASP CYS PHE ARG LYS HIS
SEQRES 13 D 212 PRO GLU ALA THR TYR SER ARG CYS GLY SER GLY PRO TRP
SEQRES 14 D 212 ILE THR PRO ARG CYS MET VAL ASP TYR PRO TYR ARG LEU
SEQRES 15 D 212 TRP HIS TYR PRO CYS THR ILE ASN TYR THR ILE PHE LYS
SEQRES 16 D 212 VAL ARG MET TYR VAL GLY GLY VAL GLU HIS ARG LEU GLU
SEQRES 17 D 212 ALA ALA CYS ASN
SEQRES 1 H 233 GLU VAL GLN LEU LEU GLU GLN SER GLY ALA GLU VAL LYS
SEQRES 2 H 233 LYS PRO GLY SER SER VAL LYS VAL SER CYS GLU THR SER
SEQRES 3 H 233 GLY GLY THR PHE ASP ASN TYR ALA LEU ASN TRP VAL ARG
SEQRES 4 H 233 GLN ALA PRO GLY GLN GLY LEU GLU TRP ILE GLY GLY VAL
SEQRES 5 H 233 VAL PRO LEU PHE GLY THR THR ARG ASN ALA GLN LYS PHE
SEQRES 6 H 233 GLN GLY ARG VAL THR ILE SER ASP ASP LYS SER THR GLY
SEQRES 7 H 233 THR GLY HIS MET GLU LEU ARG SER LEU ARG SER GLU ASP
SEQRES 8 H 233 THR ALA VAL TYR TYR CYS VAL ARG SER VAL THR PRO ARG
SEQRES 9 H 233 TYR CYS GLY GLY GLY PHE CYS TYR GLY GLU PHE ASP TYR
SEQRES 10 H 233 TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER
SEQRES 11 H 233 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER
SEQRES 12 H 233 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU
SEQRES 13 H 233 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP
SEQRES 14 H 233 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO
SEQRES 15 H 233 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER
SEQRES 16 H 233 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR
SEQRES 17 H 233 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS
SEQRES 18 H 233 VAL ASP LYS LYS VAL GLU PRO LYS SER CYS GLY SER
SEQRES 1 L 214 GLU ILE GLU LEU THR GLN SER PRO ALA THR LEU SER VAL
SEQRES 2 L 214 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER
SEQRES 3 L 214 GLN SER VAL SER SER ASN LEU ALA TRP TYR GLN GLN LYS
SEQRES 4 L 214 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER
SEQRES 5 L 214 THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER
SEQRES 6 L 214 GLY SER GLY THR GLU PHE THR LEU THR VAL SER ARG LEU
SEQRES 7 L 214 GLU PRO GLU ASP SER ALA VAL TYR PHE CYS GLN GLN TYR
SEQRES 8 L 214 TYR ARG SER PRO LEU THR PHE GLY GLY GLY THR LYS VAL
SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE
SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA
SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU
SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER
SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS
SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER
SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU
SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER
SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS
MODRES 4MWF ASN D 556 ASN GLYCOSYLATION SITE
MODRES 4MWF ASN D 532 ASN GLYCOSYLATION SITE
MODRES 4MWF ASN D 430 ASN GLYCOSYLATION SITE
MODRES 4MWF ASN C 430 ASN GLYCOSYLATION SITE
MODRES 4MWF ASN C 532 ASN GLYCOSYLATION SITE
MODRES 4MWF ASN D 623 ASN GLYCOSYLATION SITE
MODRES 4MWF ASN D 540 ASN GLYCOSYLATION SITE
MODRES 4MWF ASN C 556 ASN GLYCOSYLATION SITE
MODRES 4MWF ASN C 623 ASN GLYCOSYLATION SITE
MODRES 4MWF ASN C 540 ASN GLYCOSYLATION SITE
HET NAG E 1 14
HET NAG E 2 14
HET BMA E 3 11
HET MAN E 4 11
HET MAN E 5 11
HET MAN E 6 11
HET MAN E 7 11
HET MAN E 8 11
HET NAG F 1 14
HET NAG F 2 14
HET NAG G 1 14
HET NAG G 2 14
HET NAG C 711 14
HET NAG C 712 14
HET NAG C 713 14
HET NAG D 701 14
HET NAG D 702 14
HET NAG D 703 14
HET NAG D 706 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
FORMUL 7 NAG 13(C8 H15 N O6)
FORMUL 7 BMA C6 H12 O6
FORMUL 7 MAN 5(C6 H12 O6)
HELIX 1 1 ARG A 83 THR A 87 5 5
HELIX 2 2 SER A 156 ALA A 158 5 3
HELIX 3 3 SER A 187 LEU A 189 5 3
HELIX 4 4 LYS A 201 ASN A 204 5 4
HELIX 5 5 GLU B 79 SER B 83 5 5
HELIX 6 6 SER B 121 LYS B 126 1 6
HELIX 7 7 LYS B 183 GLU B 187 1 5
HELIX 8 8 HIS C 421 THR C 425 5 5
HELIX 9 9 LEU C 438 TYR C 443 1 6
HELIX 10 10 PRO C 567 GLY C 572 5 6
HELIX 11 11 TYR C 613 TYR C 618 1 6
HELIX 12 12 PRO C 619 ILE C 622 5 4
HELIX 13 13 GLY D 436 PHE D 442 5 7
HELIX 14 14 PRO D 567 GLY D 572 5 6
HELIX 15 15 TYR D 613 TYR D 618 1 6
HELIX 16 16 PRO D 619 TYR D 624 5 6
HELIX 17 17 GLN H 61 GLN H 64 5 4
HELIX 18 18 ARG H 83 THR H 87 5 5
HELIX 19 19 SER H 156 ALA H 158 5 3
HELIX 20 20 SER H 187 LEU H 189 5 3
HELIX 21 21 LYS H 201 ASN H 204 5 4
HELIX 22 22 GLU L 79 SER L 83 5 5
HELIX 23 23 SER L 121 SER L 127 1 7
HELIX 24 24 LYS L 183 HIS L 189 1 7
SHEET 1 A 4 LEU A 4 GLN A 6 0
SHEET 2 A 4 SER A 17 THR A 24 -1 O GLU A 23 N GLU A 5
SHEET 3 A 4 THR A 77 ARG A 82A-1 O MET A 80 N VAL A 20
SHEET 4 A 4 THR A 68 ASP A 72 -1 N ASP A 72 O THR A 77
SHEET 1 B 6 GLU A 10 LYS A 12 0
SHEET 2 B 6 THR A 107 VAL A 111 1 O THR A 110 N GLU A 10
SHEET 3 B 6 ALA A 88 SER A 95 -1 N ALA A 88 O VAL A 109
SHEET 4 B 6 ALA A 33 GLN A 39 -1 N ASN A 35 O VAL A 93
SHEET 5 B 6 LEU A 45 VAL A 51 -1 O VAL A 51 N LEU A 34
SHEET 6 B 6 THR A 57 ASN A 59 -1 O ARG A 58 N GLY A 50
SHEET 1 C 4 GLU A 10 LYS A 12 0
SHEET 2 C 4 THR A 107 VAL A 111 1 O THR A 110 N GLU A 10
SHEET 3 C 4 ALA A 88 SER A 95 -1 N ALA A 88 O VAL A 109
SHEET 4 C 4 TYR A 102 TRP A 103 -1 O TYR A 102 N ARG A 94
SHEET 1 D 2 TYR A 100 CYS A 100A 0
SHEET 2 D 2 CYS A 100F TYR A 100G-1 O TYR A 100G N TYR A 100
SHEET 1 E 4 SER A 120 LEU A 124 0
SHEET 2 E 4 THR A 135 TYR A 145 -1 O LYS A 143 N SER A 120
SHEET 3 E 4 TYR A 176 PRO A 185 -1 O LEU A 178 N VAL A 142
SHEET 4 E 4 VAL A 163 THR A 165 -1 N HIS A 164 O VAL A 181
SHEET 1 F 4 SER A 120 LEU A 124 0
SHEET 2 F 4 THR A 135 TYR A 145 -1 O LYS A 143 N SER A 120
SHEET 3 F 4 TYR A 176 PRO A 185 -1 O LEU A 178 N VAL A 142
SHEET 4 F 4 VAL A 169 LEU A 170 -1 N VAL A 169 O SER A 177
SHEET 1 G 3 THR A 151 TRP A 154 0
SHEET 2 G 3 ILE A 195 HIS A 200 -1 O ASN A 199 N THR A 151
SHEET 3 G 3 THR A 205 LYS A 210 -1 O VAL A 207 N VAL A 198
SHEET 1 H 4 LEU B 4 SER B 7 0
SHEET 2 H 4 ALA B 19 ALA B 25 -1 O SER B 22 N SER B 7
SHEET 3 H 4 GLU B 70 VAL B 75 -1 O LEU B 73 N LEU B 21
SHEET 4 H 4 PHE B 62 SER B 67 -1 N SER B 67 O GLU B 70
SHEET 1 I 6 THR B 10 VAL B 13 0
SHEET 2 I 6 THR B 102 ILE B 106 1 O LYS B 103 N LEU B 11
SHEET 3 I 6 VAL B 85 GLN B 90 -1 N TYR B 86 O THR B 102
SHEET 4 I 6 LEU B 33 GLN B 38 -1 N TYR B 36 O PHE B 87
SHEET 5 I 6 ARG B 45 TYR B 49 -1 O ARG B 45 N GLN B 37
SHEET 6 I 6 THR B 53 ARG B 54 -1 O THR B 53 N TYR B 49
SHEET 1 J 4 THR B 10 VAL B 13 0
SHEET 2 J 4 THR B 102 ILE B 106 1 O LYS B 103 N LEU B 11
SHEET 3 J 4 VAL B 85 GLN B 90 -1 N TYR B 86 O THR B 102
SHEET 4 J 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90
SHEET 1 K 4 SER B 114 PHE B 118 0
SHEET 2 K 4 THR B 129 PHE B 139 -1 O LEU B 135 N PHE B 116
SHEET 3 K 4 TYR B 173 SER B 182 -1 O LEU B 175 N LEU B 136
SHEET 4 K 4 SER B 159 VAL B 163 -1 N GLN B 160 O THR B 178
SHEET 1 L 4 ALA B 153 LEU B 154 0
SHEET 2 L 4 LYS B 145 VAL B 150 -1 N VAL B 150 O ALA B 153
SHEET 3 L 4 VAL B 191 THR B 197 -1 O GLU B 195 N GLN B 147
SHEET 4 L 4 VAL B 205 ASN B 210 -1 O VAL B 205 N VAL B 196
SHEET 1 M 2 ALA C 426 LEU C 427 0
SHEET 2 M 2 CYS C 503 GLY C 504 -1 O GLY C 504 N ALA C 426
SHEET 1 N 2 ILE C 496 PRO C 498 0
SHEET 2 N 2 VAL C 536 VAL C 538 -1 O PHE C 537 N VAL C 497
SHEET 1 O 4 PRO C 513 VAL C 515 0
SHEET 2 O 4 TYR C 507 PHE C 509 -1 N CYS C 508 O VAL C 514
SHEET 3 O 4 GLY C 551 MET C 555 -1 O THR C 553 N TYR C 507
SHEET 4 O 4 THR C 561 GLY C 565 -1 O LYS C 562 N TRP C 554
SHEET 1 P 4 TRP C 602 THR C 604 0
SHEET 2 P 4 CYS C 607 VAL C 609 -1 O CYS C 607 N ILE C 603
SHEET 3 P 4 VAL C 636 CYS C 644 -1 O ALA C 643 N MET C 608
SHEET 4 P 4 THR C 625 VAL C 633 -1 N THR C 625 O CYS C 644
SHEET 1 Q 2 ALA D 426 LEU D 427 0
SHEET 2 Q 2 CYS D 503 GLY D 504 -1 O GLY D 504 N ALA D 426
SHEET 1 R 2 ILE D 496 PRO D 498 0
SHEET 2 R 2 VAL D 536 VAL D 538 -1 O PHE D 537 N VAL D 497
SHEET 1 S 4 PRO D 513 VAL D 515 0
SHEET 2 S 4 TYR D 507 PHE D 509 -1 N CYS D 508 O VAL D 514
SHEET 3 S 4 GLY D 551 MET D 555 -1 O THR D 553 N TYR D 507
SHEET 4 S 4 THR D 561 GLY D 565 -1 O CYS D 564 N CYS D 552
SHEET 1 T 3 CYS D 607 VAL D 609 0
SHEET 2 T 3 VAL D 636 CYS D 644 -1 O ALA D 643 N MET D 608
SHEET 3 T 3 THR D 625 VAL D 633 -1 N THR D 625 O CYS D 644
SHEET 1 U 4 GLU H 5 GLN H 6 0
SHEET 2 U 4 VAL H 18 GLU H 23 -1 O GLU H 23 N GLU H 5
SHEET 3 U 4 THR H 77 LEU H 82 -1 O MET H 80 N VAL H 20
SHEET 4 U 4 VAL H 67 ASP H 72 -1 N ASP H 72 O THR H 77
SHEET 1 V 6 GLU H 10 LYS H 12 0
SHEET 2 V 6 THR H 107 VAL H 111 1 O THR H 110 N LYS H 12
SHEET 3 V 6 ALA H 88 SER H 95 -1 N TYR H 90 O THR H 107
SHEET 4 V 6 ALA H 33 GLN H 39 -1 N VAL H 37 O TYR H 91
SHEET 5 V 6 GLU H 46 VAL H 52 -1 O GLY H 49 N TRP H 36
SHEET 6 V 6 THR H 56 ASN H 59 -1 O THR H 56 N VAL H 52
SHEET 1 W 4 GLU H 10 LYS H 12 0
SHEET 2 W 4 THR H 107 VAL H 111 1 O THR H 110 N LYS H 12
SHEET 3 W 4 ALA H 88 SER H 95 -1 N TYR H 90 O THR H 107
SHEET 4 W 4 TYR H 102 TRP H 103 -1 O TYR H 102 N ARG H 94
SHEET 1 X 2 TYR H 100 GLY H 100B 0
SHEET 2 X 2 PHE H 100E TYR H 100G-1 O TYR H 100G N TYR H 100
SHEET 1 Y 4 SER H 120 LEU H 124 0
SHEET 2 Y 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122
SHEET 3 Y 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142
SHEET 4 Y 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181
SHEET 1 Z 4 SER H 120 LEU H 124 0
SHEET 2 Z 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122
SHEET 3 Z 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142
SHEET 4 Z 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177
SHEET 1 AA 3 THR H 151 TRP H 154 0
SHEET 2 AA 3 TYR H 194 HIS H 200 -1 O ASN H 199 N THR H 151
SHEET 3 AA 3 THR H 205 VAL H 211 -1 O THR H 205 N HIS H 200
SHEET 1 AB 4 LEU L 4 THR L 5 0
SHEET 2 AB 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5
SHEET 3 AB 4 GLU L 70 VAL L 75 -1 O LEU L 73 N LEU L 21
SHEET 4 AB 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74
SHEET 1 AC 6 THR L 10 VAL L 13 0
SHEET 2 AC 6 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11
SHEET 3 AC 6 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104
SHEET 4 AC 6 LEU L 33 GLN L 38 -1 N TYR L 36 O PHE L 87
SHEET 5 AC 6 ARG L 45 TYR L 49 -1 O LEU L 47 N TRP L 35
SHEET 6 AC 6 THR L 53 ARG L 54 -1 O THR L 53 N TYR L 49
SHEET 1 AD 4 THR L 10 VAL L 13 0
SHEET 2 AD 4 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11
SHEET 3 AD 4 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104
SHEET 4 AD 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90
SHEET 1 AE 4 SER L 114 PHE L 118 0
SHEET 2 AE 4 THR L 129 PHE L 139 -1 O VAL L 133 N PHE L 118
SHEET 3 AE 4 TYR L 173 SER L 182 -1 O LEU L 175 N LEU L 136
SHEET 4 AE 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176
SHEET 1 AF 4 ALA L 153 LEU L 154 0
SHEET 2 AF 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153
SHEET 3 AF 4 VAL L 191 THR L 197 -1 O ALA L 193 N LYS L 149
SHEET 4 AF 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196
SSBOND 1 CYS A 100A CYS A 100F 1555 1555 2.03
SSBOND 2 CYS B 23 CYS B 88 1555 1555 2.04
SSBOND 3 CYS B 134 CYS B 194 1555 1555 2.03
SSBOND 4 CYS C 494 CYS C 564 1555 1555 2.05
SSBOND 5 CYS C 508 CYS C 552 1555 1555 2.05
SSBOND 6 CYS C 569 CYS C 581 1555 1555 2.03
SSBOND 7 CYS C 585 CYS C 597 1555 1555 2.04
SSBOND 8 CYS C 607 CYS C 644 1555 1555 2.05
SSBOND 9 CYS D 429 CYS D 503 1555 1555 2.02
SSBOND 10 CYS D 452 CYS D 620 1555 1555 2.04
SSBOND 11 CYS D 494 CYS D 564 1555 1555 2.03
SSBOND 12 CYS D 508 CYS D 552 1555 1555 2.03
SSBOND 13 CYS D 569 CYS D 581 1555 1555 2.04
SSBOND 14 CYS D 585 CYS D 597 1555 1555 2.03
SSBOND 15 CYS D 607 CYS D 644 1555 1555 2.05
SSBOND 16 CYS H 22 CYS H 92 1555 1555 2.04
SSBOND 17 CYS H 100A CYS H 100F 1555 1555 2.03
SSBOND 18 CYS H 140 CYS H 196 1555 1555 2.03
SSBOND 19 CYS L 23 CYS L 88 1555 1555 2.06
SSBOND 20 CYS L 134 CYS L 194 1555 1555 2.05
LINK ND2 ASN C 430 C1 NAG E 1 1555 1555 1.45
LINK ND2 ASN C 532 C1 NAG C 711 1555 1555 1.45
LINK ND2 ASN C 540 C1 NAG C 712 1555 1555 1.46
LINK ND2 ASN C 556 C1 NAG F 1 1555 1555 1.45
LINK ND2 ASN C 623 C1 NAG C 713 1555 1555 1.45
LINK ND2 ASN D 430 C1 NAG D 701 1555 1555 1.44
LINK ND2 ASN D 532 C1 NAG D 702 1555 1555 1.43
LINK ND2 ASN D 540 C1 NAG D 703 1555 1555 1.45
LINK ND2 ASN D 556 C1 NAG G 1 1555 1555 1.42
LINK ND2 ASN D 623 C1 NAG D 706 1555 1555 1.45
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.43
LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.58
LINK O6 BMA E 3 C1 MAN E 7 1555 1555 1.53
LINK O2 MAN E 4 C1 MAN E 5 1555 1555 1.43
LINK O2 MAN E 5 C1 MAN E 6 1555 1555 1.43
LINK O6 MAN E 7 C1 MAN E 8 1555 1555 1.46
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.45
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44
CISPEP 1 SER A 25 GLY A 26 0 0.50
CISPEP 2 GLY A 27 THR A 28 0 0.09
CISPEP 3 GLY A 100C GLY A 100D 0 -7.03
CISPEP 4 PHE A 146 PRO A 147 0 -10.46
CISPEP 5 GLU A 148 PRO A 149 0 0.05
CISPEP 6 SER B 7 PRO B 8 0 -0.40
CISPEP 7 TYR B 140 PRO B 141 0 1.80
CISPEP 8 CYS C 494 GLY C 495 0 0.52
CISPEP 9 CYS C 503 GLY C 504 0 -13.45
CISPEP 10 THR C 510 PRO C 511 0 13.87
CISPEP 11 ARG C 521 SER C 522 0 -0.69
CISPEP 12 SER C 522 GLY C 523 0 3.69
CISPEP 13 THR C 583 ASP C 584 0 8.17
CISPEP 14 ASN D 430 GLU D 431 0 1.40
CISPEP 15 SER D 449 SER D 450 0 2.11
CISPEP 16 CYS D 503 GLY D 504 0 -14.64
CISPEP 17 THR D 510 PRO D 511 0 1.24
CISPEP 18 ARG D 521 SER D 522 0 -5.01
CISPEP 19 SER D 522 GLY D 523 0 -9.22
CISPEP 20 GLY D 530 ALA D 531 0 22.12
CISPEP 21 PRO D 545 LEU D 546 0 -11.22
CISPEP 22 GLY D 572 GLY D 573 0 -0.93
CISPEP 23 GLN H 2 LEU H 3 0 1.88
CISPEP 24 GLY H 26 GLY H 27 0 -14.96
CISPEP 25 GLY H 100C GLY H 100D 0 -5.89
CISPEP 26 PHE H 146 PRO H 147 0 -8.26
CISPEP 27 GLU H 148 PRO H 149 0 7.27
CISPEP 28 SER L 7 PRO L 8 0 -1.01
CISPEP 29 SER L 94 PRO L 95 0 1.03
CISPEP 30 TYR L 140 PRO L 141 0 2.46
CRYST1 47.132 166.553 209.963 90.00 90.00 90.00 P 21 21 21 8
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 0.021217 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006004 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004763 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
