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pdb7bbv.ent
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HEADER LYASE 18-DEC-20 7BBV
TITLE PECTATE LYASE B FROM VERTICILLIUM DAHLIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PECTATE LYASE B;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VERTICILLIUM DAHLIAE (STRAIN VDLS.17 / ATCC
SOURCE 3 MYA-4575 / FGSC 10137);
SOURCE 4 ORGANISM_COMMON: VERTICILLIUM WILT;
SOURCE 5 ORGANISM_TAXID: 498257;
SOURCE 6 STRAIN: VDLS.17 / ATCC MYA-4575 / FGSC 10137;
SOURCE 7 GENE: VDAG_04718;
SOURCE 8 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS PECTINASE, BETA-SHEETS, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SAFRAN,O.HABRYLO,J.BOUCKAERT,C.PAU ROBLOT,F.SENECHAL,J.PELLOUX
REVDAT 4 23-OCT-24 7BBV 1 REMARK
REVDAT 3 07-FEB-24 7BBV 1 REMARK
REVDAT 2 01-FEB-23 7BBV 1 JRNL
REVDAT 1 13-JUL-22 7BBV 0
JRNL AUTH J.SAFRAN,V.UNG,J.BOUCKAERT,O.HABRYLO,R.MOLINIE,J.X.FONTAINE,
JRNL AUTH 2 A.LEMAIRE,A.VOXEUR,S.PILARD,C.PAU-ROBLOT,D.MERCADANTE,
JRNL AUTH 3 J.PELLOUX,F.SENECHAL
JRNL TITL THE SPECIFICITY OF PECTATE LYASE VDPELB FROM VERTICILIUM
JRNL TITL 2 DAHLIAE IS HIGHLIGHTED BY STRUCTURAL, DYNAMICAL AND
JRNL TITL 3 BIOCHEMICAL CHARACTERIZATIONS.
JRNL REF INT.J.BIOL.MACROMOL. V. 231 23137 2023
JRNL REFN ISSN 0141-8130
JRNL PMID 36639075
JRNL DOI 10.1016/J.IJBIOMAC.2023.123137
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18.2_3874
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 60.52
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 207382
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 10374
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 60.5200 - 3.7200 1.00 6827 360 0.1343 0.1606
REMARK 3 2 3.7200 - 2.9500 1.00 6728 354 0.1269 0.1508
REMARK 3 3 2.9500 - 2.5800 1.00 6678 351 0.1333 0.1466
REMARK 3 4 2.5800 - 2.3500 1.00 6668 351 0.1432 0.1648
REMARK 3 5 2.3400 - 2.1800 1.00 6670 351 0.1469 0.1698
REMARK 3 6 2.1800 - 2.0500 1.00 6677 351 0.1573 0.1892
REMARK 3 7 2.0500 - 1.9500 1.00 6647 350 0.1651 0.1991
REMARK 3 8 1.9500 - 1.8600 1.00 6623 349 0.1630 0.1858
REMARK 3 9 1.8600 - 1.7900 1.00 6644 350 0.1604 0.2006
REMARK 3 10 1.7900 - 1.7300 1.00 6665 350 0.1800 0.2089
REMARK 3 11 1.7300 - 1.6700 1.00 6579 346 0.2323 0.2788
REMARK 3 12 1.6700 - 1.6300 1.00 6653 350 0.2638 0.2969
REMARK 3 13 1.6300 - 1.5800 1.00 6624 347 0.3009 0.3137
REMARK 3 14 1.5800 - 1.5400 1.00 6634 349 0.3103 0.3417
REMARK 3 15 1.5400 - 1.5100 1.00 6619 349 0.3189 0.3109
REMARK 3 16 1.5100 - 1.4800 1.00 6578 346 0.3209 0.3351
REMARK 3 17 1.4800 - 1.4500 0.99 6569 346 0.3406 0.3559
REMARK 3 18 1.4500 - 1.4200 1.00 6586 347 0.3496 0.3689
REMARK 3 19 1.4200 - 1.4000 0.99 6567 346 0.3513 0.3521
REMARK 3 20 1.4000 - 1.3700 0.99 6583 347 0.3619 0.4008
REMARK 3 21 1.3700 - 1.3500 0.99 6575 347 0.3749 0.3984
REMARK 3 22 1.3500 - 1.3300 0.99 6574 346 0.4004 0.4151
REMARK 3 23 1.3300 - 1.3100 0.99 6563 345 0.4244 0.4366
REMARK 3 24 1.3100 - 1.2900 1.00 6562 346 0.4232 0.4297
REMARK 3 25 1.2900 - 1.2700 0.99 6564 345 0.4202 0.4303
REMARK 3 26 1.2700 - 1.2600 0.99 6517 343 0.4212 0.4093
REMARK 3 27 1.2600 - 1.2400 0.99 6495 342 0.4238 0.4378
REMARK 3 28 1.2400 - 1.2300 0.98 6521 344 0.4343 0.4290
REMARK 3 29 1.2300 - 1.2100 0.96 6354 336 0.4447 0.4435
REMARK 3 30 1.2100 - 1.2000 0.83 5464 290 0.4585 0.4613
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) : 0.356
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.872
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.23
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.19
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 : 0.013 4798
REMARK 3 ANGLE : 1.400 6510
REMARK 3 CHIRALITY : 0.101 765
REMARK 3 PLANARITY : 0.009 810
REMARK 3 DIHEDRAL : 13.404 1796
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 : 1
REMARK 3 NCS GROUP : ens_1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "A" and (resid 19 through 23 or
REMARK 3 resid 25 through 77 or resid 79 through
REMARK 3 91 or resid 93 through 103 or resid 105
REMARK 3 through 211 or resid 213 through 228 or
REMARK 3 resid 230 through 251 or resid 253
REMARK 3 through 259 or resid 261 through 266 or
REMARK 3 resid 268 through 286 or resid 288
REMARK 3 through 292 or resid 294 or resid 296
REMARK 3 through 316 or resid 401 through 407))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "B" and (resid 19 through 23 or
REMARK 3 resid 25 through 77 or resid 79 through
REMARK 3 91 or resid 93 through 103 or resid 105
REMARK 3 through 211 or resid 213 through 228 or
REMARK 3 resid 230 through 251 or resid 253
REMARK 3 through 259 or resid 261 through 266 or
REMARK 3 resid 268 through 286 or resid 288
REMARK 3 through 292 or resid 294 or resid 296
REMARK 3 through 316 or resid 401 through 407))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7BBV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-DEC-20.
REMARK 100 THE DEPOSITION ID IS D_1292112561.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-18
REMARK 200 TEMPERATURE (KELVIN) : 100.15
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.980
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : POINTLESS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 207729
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 60.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.01400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.8
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: 3VMV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MIB 8.0 25 % W/V PEG 1500 (B5
REMARK 280 CONDITION PACT PREMIER PLATE), PH 8.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 29.84500
REMARK 290 SMTRY3 2 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 THR A 1
REMARK 465 PRO A 2
REMARK 465 THR A 3
REMARK 465 PRO A 4
REMARK 465 THR A 5
REMARK 465 ILE A 6
REMARK 465 GLN A 7
REMARK 465 GLU A 8
REMARK 465 ASP A 9
REMARK 465 GLY A 10
REMARK 465 SER A 11
REMARK 465 PRO A 12
REMARK 465 ALA A 13
REMARK 465 LEU A 14
REMARK 465 ILE A 15
REMARK 465 ALA A 16
REMARK 465 LYS A 17
REMARK 465 ARG A 18
REMARK 465 ALA A 317
REMARK 465 ALA A 318
REMARK 465 ALA A 319
REMARK 465 SER A 320
REMARK 465 PHE A 321
REMARK 465 LEU A 322
REMARK 465 GLU A 323
REMARK 465 GLN A 324
REMARK 465 LYS A 325
REMARK 465 LEU A 326
REMARK 465 ILE A 327
REMARK 465 SER A 328
REMARK 465 GLU A 329
REMARK 465 GLU A 330
REMARK 465 ASP A 331
REMARK 465 LEU A 332
REMARK 465 ASN A 333
REMARK 465 SER A 334
REMARK 465 ALA A 335
REMARK 465 VAL A 336
REMARK 465 ASP A 337
REMARK 465 HIS A 338
REMARK 465 HIS A 339
REMARK 465 HIS A 340
REMARK 465 HIS A 341
REMARK 465 HIS A 342
REMARK 465 HIS A 343
REMARK 465 THR B 1
REMARK 465 PRO B 2
REMARK 465 THR B 3
REMARK 465 PRO B 4
REMARK 465 THR B 5
REMARK 465 ILE B 6
REMARK 465 GLN B 7
REMARK 465 GLU B 8
REMARK 465 ASP B 9
REMARK 465 GLY B 10
REMARK 465 SER B 11
REMARK 465 PRO B 12
REMARK 465 ALA B 13
REMARK 465 LEU B 14
REMARK 465 ILE B 15
REMARK 465 ALA B 16
REMARK 465 LYS B 17
REMARK 465 ARG B 18
REMARK 465 ALA B 317
REMARK 465 ALA B 318
REMARK 465 ALA B 319
REMARK 465 SER B 320
REMARK 465 PHE B 321
REMARK 465 LEU B 322
REMARK 465 GLU B 323
REMARK 465 GLN B 324
REMARK 465 LYS B 325
REMARK 465 LEU B 326
REMARK 465 ILE B 327
REMARK 465 SER B 328
REMARK 465 GLU B 329
REMARK 465 GLU B 330
REMARK 465 ASP B 331
REMARK 465 LEU B 332
REMARK 465 ASN B 333
REMARK 465 SER B 334
REMARK 465 ALA B 335
REMARK 465 VAL B 336
REMARK 465 ASP B 337
REMARK 465 HIS B 338
REMARK 465 HIS B 339
REMARK 465 HIS B 340
REMARK 465 HIS B 341
REMARK 465 HIS B 342
REMARK 465 HIS B 343
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 HZ1 LYS A 190 O HOH A 502 1.46
REMARK 500 OG SER B 48 C2 MAN B 404 1.90
REMARK 500 CB SER B 48 C1 MAN B 404 1.94
REMARK 500 CB SER A 48 C1 MAN A 404 1.99
REMARK 500 OG1 THR A 54 O5 MAN A 405 2.00
REMARK 500 O HOH B 705 O HOH B 822 2.05
REMARK 500 CB THR B 54 C1 MAN B 408 2.07
REMARK 500 OG SER A 48 C2 MAN A 404 2.08
REMARK 500 O HOH A 592 O HOH B 900 2.09
REMARK 500 O HOH A 607 O HOH A 873 2.09
REMARK 500 O HOH B 528 O HOH B 827 2.11
REMARK 500 O HOH B 741 O HOH B 845 2.11
REMARK 500 O HOH A 860 O HOH A 913 2.11
REMARK 500 OG SER A 48 O5 MAN A 404 2.11
REMARK 500 O HOH A 524 O HOH A 870 2.11
REMARK 500 O HOH A 755 O HOH A 845 2.12
REMARK 500 O HOH B 727 O HOH B 850 2.12
REMARK 500 O HOH A 1005 O HOH B 866 2.13
REMARK 500 O HOH B 659 O HOH B 868 2.13
REMARK 500 O HOH B 870 O HOH B 922 2.14
REMARK 500 O HOH B 689 O HOH B 743 2.15
REMARK 500 O HOH A 767 O HOH A 837 2.15
REMARK 500 CB THR A 54 C1 MAN A 405 2.15
REMARK 500 O HOH A 656 O HOH B 793 2.15
REMARK 500 CB THR A 45 C1 MAN A 407 2.15
REMARK 500 O HOH B 518 O HOH B 881 2.16
REMARK 500 O HOH A 596 O HOH A 597 2.16
REMARK 500 OE1 GLU B 262 O HOH B 501 2.16
REMARK 500 O HOH A 982 O HOH A 1034 2.16
REMARK 500 O HOH A 838 O HOH A 991 2.17
REMARK 500 O HOH A 861 O HOH A 933 2.17
REMARK 500 O HOH B 899 O HOH B 950 2.18
REMARK 500 O HOH B 907 O HOH B 921 2.18
REMARK 500 O HOH A 870 O HOH A 922 2.18
REMARK 500 OG1 THR B 54 O5 MAN B 408 2.18
REMARK 500 O HOH A 794 O HOH A 839 2.18
REMARK 500 OG1 THR A 45 O5 MAN A 407 2.18
REMARK 500 O HOH B 649 O HOH B 862 2.19
REMARK 500 CB THR A 46 C1 MAN A 402 2.19
REMARK 500 O HOH B 689 O HOH B 799 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 910 O HOH B 942 2454 2.11
REMARK 500 O HOH A 899 O HOH B 669 1655 2.14
REMARK 500 O HOH A 1010 O HOH B 962 2455 2.18
REMARK 500 O HOH A 742 O HOH B 886 2455 2.19
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 92 148.64 -171.86
REMARK 500 ASN A 105 71.26 62.88
REMARK 500 ASN A 105 71.26 66.11
REMARK 500 ASN A 131 76.90 63.97
REMARK 500 SER A 141 -117.98 -140.20
REMARK 500 ASP A 151 -113.39 -100.84
REMARK 500 TRP A 162 65.01 60.21
REMARK 500 LYS A 192 -159.79 -117.32
REMARK 500 ARG A 208 67.83 63.31
REMARK 500 PHE A 214 -37.02 72.00
REMARK 500 ALA A 231 -97.65 -98.47
REMARK 500 THR A 251 153.10 -47.14
REMARK 500 PRO A 291 31.34 -89.70
REMARK 500 ASN B 105 70.89 66.63
REMARK 500 ASN B 131 74.85 63.94
REMARK 500 SER B 141 -114.87 -138.22
REMARK 500 ASP B 151 -110.79 -97.46
REMARK 500 PHE B 174 -73.69 -75.05
REMARK 500 LYS B 192 -158.13 -117.11
REMARK 500 ARG B 208 63.93 62.10
REMARK 500 PHE B 214 -37.14 72.33
REMARK 500 ALA B 231 -96.49 -98.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1043 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH B1005 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH B1006 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH B1007 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH B1008 DISTANCE = 6.40 ANGSTROMS
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 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 122 OD1
REMARK 620 2 ASP A 122 OD2 51.9
REMARK 620 3 ASP A 151 OD2 73.1 113.8
REMARK 620 4 ASP A 155 OD2 79.3 80.6 125.9
REMARK 620 5 HOH A 568 O 94.6 139.1 67.7 69.2
REMARK 620 6 HOH A 830 O 131.9 80.6 145.6 86.1 122.5
REMARK 620 7 SER B 288 OG 95.2 82.9 66.9 162.5 128.1 85.3
REMARK 620 8 HOH B 790 O 153.9 149.8 81.5 112.4 70.0 73.6 79.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 122 OD1
REMARK 620 2 ASP B 122 OD2 52.6
REMARK 620 3 ASP B 151 OD2 76.9 125.7
REMARK 620 4 ASP B 155 OD2 84.2 85.0 111.1
REMARK 620 5 HOH B 505 O 80.2 87.1 63.3 164.2
REMARK 620 6 HOH B 623 O 109.2 147.4 61.0 64.8 118.7
REMARK 620 7 HOH B 742 O 130.0 77.4 147.4 91.9 99.7 113.8
REMARK 620 8 HOH B 789 O 154.9 152.4 79.0 97.8 95.5 51.3 75.1
REMARK 620 N 1 2 3 4 5 6 7
DBREF 7BBV A 1 316 UNP G2X3Y1 G2X3Y1_VERDV 18 333
DBREF 7BBV B 1 316 UNP G2X3Y1 G2X3Y1_VERDV 18 333
SEQADV 7BBV ALA A 317 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV ALA A 318 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV ALA A 319 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV SER A 320 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV PHE A 321 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV LEU A 322 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV GLU A 323 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV GLN A 324 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV LYS A 325 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV LEU A 326 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV ILE A 327 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV SER A 328 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV GLU A 329 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV GLU A 330 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV ASP A 331 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV LEU A 332 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV ASN A 333 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV SER A 334 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV ALA A 335 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV VAL A 336 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV ASP A 337 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV HIS A 338 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV HIS A 339 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV HIS A 340 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV HIS A 341 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV HIS A 342 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV HIS A 343 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV ALA B 317 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV ALA B 318 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV ALA B 319 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV SER B 320 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV PHE B 321 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV LEU B 322 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV GLU B 323 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV GLN B 324 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV LYS B 325 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV LEU B 326 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV ILE B 327 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV SER B 328 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV GLU B 329 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV GLU B 330 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV ASP B 331 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV LEU B 332 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV ASN B 333 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV SER B 334 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV ALA B 335 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV VAL B 336 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV ASP B 337 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV HIS B 338 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV HIS B 339 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV HIS B 340 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV HIS B 341 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV HIS B 342 UNP G2X3Y1 EXPRESSION TAG
SEQADV 7BBV HIS B 343 UNP G2X3Y1 EXPRESSION TAG
SEQRES 1 A 343 THR PRO THR PRO THR ILE GLN GLU ASP GLY SER PRO ALA
SEQRES 2 A 343 LEU ILE ALA LYS ARG ALA SER VAL THR GLU SER CYS ASN
SEQRES 3 A 343 ILE GLY TYR ALA SER THR ASN GLY GLY THR THR GLY GLY
SEQRES 4 A 343 LYS GLY GLY ALA THR THR THR VAL SER THR LEU ALA GLN
SEQRES 5 A 343 PHE THR LYS ALA ALA GLU SER SER GLY LYS LEU ASN ILE
SEQRES 6 A 343 VAL VAL LYS GLY LYS ILE SER GLY GLY ALA LYS VAL ARG
SEQRES 7 A 343 VAL GLN SER ASP LYS THR ILE ILE GLY GLN LYS GLY SER
SEQRES 8 A 343 GLU LEU VAL GLY THR GLY LEU TYR ILE ASN LYS VAL LYS
SEQRES 9 A 343 ASN VAL ILE VAL ARG ASN MET LYS ILE SER LYS VAL LYS
SEQRES 10 A 343 ASP SER ASN GLY ASP ALA ILE GLY ILE GLN ALA SER LYS
SEQRES 11 A 343 ASN VAL TRP VAL ASP HIS CYS ASP LEU SER SER ASP LEU
SEQRES 12 A 343 LYS SER GLY LYS ASP TYR TYR ASP GLY LEU LEU ASP ILE
SEQRES 13 A 343 THR HIS GLY SER ASP TRP VAL THR VAL SER ASN THR PHE
SEQRES 14 A 343 LEU HIS ASP HIS PHE LYS ALA SER LEU ILE GLY HIS THR
SEQRES 15 A 343 ASP SER ASN ALA LYS GLU ASP LYS GLY LYS LEU HIS VAL
SEQRES 16 A 343 THR TYR ALA ASN ASN TYR TRP TYR ASN VAL ASN SER ARG
SEQRES 17 A 343 ASN PRO SER VAL ARG PHE GLY THR VAL HIS ILE TYR ASN
SEQRES 18 A 343 ASN TYR TYR LEU GLU VAL GLY SER SER ALA VAL ASN THR
SEQRES 19 A 343 ARG MET GLY ALA GLN VAL ARG VAL GLU SER THR VAL PHE
SEQRES 20 A 343 ASP LYS SER THR LYS ASN GLY ILE ILE SER VAL ASP SER
SEQRES 21 A 343 LYS GLU LYS GLY TYR ALA THR VAL GLY ASP ILE SER TRP
SEQRES 22 A 343 GLY SER SER THR ASN THR ALA PRO LYS GLY THR LEU GLY
SEQRES 23 A 343 SER SER ASN ILE PRO TYR SER TYR ASN LEU TYR GLY LYS
SEQRES 24 A 343 ASN ASN VAL LYS ALA ARG VAL TYR GLY THR ALA GLY GLN
SEQRES 25 A 343 THR LEU GLY PHE ALA ALA ALA SER PHE LEU GLU GLN LYS
SEQRES 26 A 343 LEU ILE SER GLU GLU ASP LEU ASN SER ALA VAL ASP HIS
SEQRES 27 A 343 HIS HIS HIS HIS HIS
SEQRES 1 B 343 THR PRO THR PRO THR ILE GLN GLU ASP GLY SER PRO ALA
SEQRES 2 B 343 LEU ILE ALA LYS ARG ALA SER VAL THR GLU SER CYS ASN
SEQRES 3 B 343 ILE GLY TYR ALA SER THR ASN GLY GLY THR THR GLY GLY
SEQRES 4 B 343 LYS GLY GLY ALA THR THR THR VAL SER THR LEU ALA GLN
SEQRES 5 B 343 PHE THR LYS ALA ALA GLU SER SER GLY LYS LEU ASN ILE
SEQRES 6 B 343 VAL VAL LYS GLY LYS ILE SER GLY GLY ALA LYS VAL ARG
SEQRES 7 B 343 VAL GLN SER ASP LYS THR ILE ILE GLY GLN LYS GLY SER
SEQRES 8 B 343 GLU LEU VAL GLY THR GLY LEU TYR ILE ASN LYS VAL LYS
SEQRES 9 B 343 ASN VAL ILE VAL ARG ASN MET LYS ILE SER LYS VAL LYS
SEQRES 10 B 343 ASP SER ASN GLY ASP ALA ILE GLY ILE GLN ALA SER LYS
SEQRES 11 B 343 ASN VAL TRP VAL ASP HIS CYS ASP LEU SER SER ASP LEU
SEQRES 12 B 343 LYS SER GLY LYS ASP TYR TYR ASP GLY LEU LEU ASP ILE
SEQRES 13 B 343 THR HIS GLY SER ASP TRP VAL THR VAL SER ASN THR PHE
SEQRES 14 B 343 LEU HIS ASP HIS PHE LYS ALA SER LEU ILE GLY HIS THR
SEQRES 15 B 343 ASP SER ASN ALA LYS GLU ASP LYS GLY LYS LEU HIS VAL
SEQRES 16 B 343 THR TYR ALA ASN ASN TYR TRP TYR ASN VAL ASN SER ARG
SEQRES 17 B 343 ASN PRO SER VAL ARG PHE GLY THR VAL HIS ILE TYR ASN
SEQRES 18 B 343 ASN TYR TYR LEU GLU VAL GLY SER SER ALA VAL ASN THR
SEQRES 19 B 343 ARG MET GLY ALA GLN VAL ARG VAL GLU SER THR VAL PHE
SEQRES 20 B 343 ASP LYS SER THR LYS ASN GLY ILE ILE SER VAL ASP SER
SEQRES 21 B 343 LYS GLU LYS GLY TYR ALA THR VAL GLY ASP ILE SER TRP
SEQRES 22 B 343 GLY SER SER THR ASN THR ALA PRO LYS GLY THR LEU GLY
SEQRES 23 B 343 SER SER ASN ILE PRO TYR SER TYR ASN LEU TYR GLY LYS
SEQRES 24 B 343 ASN ASN VAL LYS ALA ARG VAL TYR GLY THR ALA GLY GLN
SEQRES 25 B 343 THR LEU GLY PHE ALA ALA ALA SER PHE LEU GLU GLN LYS
SEQRES 26 B 343 LEU ILE SER GLU GLU ASP LEU ASN SER ALA VAL ASP HIS
SEQRES 27 B 343 HIS HIS HIS HIS HIS
HET CA A 401 1
HET MAN A 402 17
HET MAN A 403 17
HET MAN A 404 19
HET MAN A 405 19
HET MAN A 406 19
HET MAN A 407 17
HET CA B 401 1
HET PEG B 402 17
HET MAN B 403 17
HET MAN B 404 19
HET MAN B 405 19
HET MAN B 406 17
HET MAN B 407 19
HET MAN B 408 18
HETNAM CA CALCIUM ION
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 3 CA 2(CA 2+)
FORMUL 4 MAN 12(C6 H12 O6)
FORMUL 11 PEG C4 H10 O3
FORMUL 18 HOH *1051(H2 O)
HELIX 1 AA1 GLY A 28 THR A 32 5 5
HELIX 2 AA2 THR A 49 SER A 59 1 11
HELIX 3 AA3 LYS A 117 GLY A 121 5 5
HELIX 4 AA4 ASN A 185 LYS A 190 1 6
HELIX 5 AA5 GLY A 286 ILE A 290 5 5
HELIX 6 AA6 GLY A 298 ASN A 300 5 3
HELIX 7 AA7 ASN A 301 TYR A 307 1 7
HELIX 8 AA8 GLY B 28 THR B 32 5 5
HELIX 9 AA9 THR B 49 GLU B 58 1 10
HELIX 10 AB1 LYS B 117 GLY B 121 5 5
HELIX 11 AB2 ASN B 185 LYS B 190 1 6
HELIX 12 AB3 GLY B 286 ILE B 290 5 5
HELIX 13 AB4 ASN B 301 TYR B 307 1 7
SHEET 1 AA117 ALA A 43 VAL A 47 0
SHEET 2 AA117 LEU A 63 VAL A 67 1 O VAL A 66 N THR A 45
SHEET 3 AA117 LYS A 83 GLY A 87 1 O THR A 84 N ILE A 65
SHEET 4 AA117 LYS A 104 ARG A 109 1 O ILE A 107 N ILE A 85
SHEET 5 AA117 LYS A 130 ASP A 135 1 O TRP A 133 N VAL A 108
SHEET 6 AA117 ASP A 161 SER A 166 1 O SER A 166 N VAL A 134
SHEET 7 AA117 HIS A 194 ALA A 198 1 O THR A 196 N VAL A 165
SHEET 8 AA117 THR A 216 TYR A 220 1 O HIS A 218 N TYR A 197
SHEET 9 AA117 GLN A 239 ASP A 248 1 O ARG A 241 N ILE A 219
SHEET 10 AA117 TYR A 223 LEU A 225 1 N TYR A 224 O ASP A 248
SHEET 11 AA117 TYR A 201 SER A 207 1 N TRP A 202 O TYR A 223
SHEET 12 AA117 PHE A 169 LYS A 175 1 N PHE A 174 O SER A 207
SHEET 13 AA117 ASP A 138 SER A 140 1 N LEU A 139 O PHE A 169
SHEET 14 AA117 LYS A 112 SER A 114 1 N ILE A 113 O ASP A 138
SHEET 15 AA117 GLU A 92 ASN A 101 1 N LEU A 93 O LYS A 112
SHEET 16 AA117 ILE A 124 GLN A 127 1 O GLY A 125 N ILE A 100
SHEET 17 AA117 LEU A 154 THR A 157 1 O ASP A 155 N ILE A 126
SHEET 1 AA2 9 LYS A 70 VAL A 79 0
SHEET 2 AA2 9 GLU A 92 ASN A 101 1 O GLU A 92 N ILE A 71
SHEET 3 AA2 9 LYS A 112 SER A 114 1 O LYS A 112 N LEU A 93
SHEET 4 AA2 9 ASP A 138 SER A 140 1 O ASP A 138 N ILE A 113
SHEET 5 AA2 9 PHE A 169 LYS A 175 1 O PHE A 169 N LEU A 139
SHEET 6 AA2 9 TYR A 201 SER A 207 1 O SER A 207 N PHE A 174
SHEET 7 AA2 9 TYR A 223 LEU A 225 1 O TYR A 223 N TRP A 202
SHEET 8 AA2 9 GLN A 239 ASP A 248 1 O ASP A 248 N TYR A 224
SHEET 9 AA2 9 TYR A 265 SER A 272 1 O SER A 272 N PHE A 247
SHEET 1 AA3 5 LEU A 178 ILE A 179 0
SHEET 2 AA3 5 SER A 211 ARG A 213 1 O SER A 211 N ILE A 179
SHEET 3 AA3 5 VAL A 232 ARG A 235 1 O ASN A 233 N VAL A 212
SHEET 4 AA3 5 ASN A 253 ILE A 256 1 O ILE A 256 N THR A 234
SHEET 5 AA3 5 THR A 277 ASN A 278 1 O THR A 277 N ILE A 255
SHEET 1 AA417 ALA B 43 VAL B 47 0
SHEET 2 AA417 LEU B 63 VAL B 67 1 O VAL B 66 N THR B 45
SHEET 3 AA417 LYS B 83 GLY B 87 1 O THR B 84 N ILE B 65
SHEET 4 AA417 LYS B 104 ARG B 109 1 O ARG B 109 N ILE B 85
SHEET 5 AA417 LYS B 130 ASP B 135 1 O TRP B 133 N VAL B 108
SHEET 6 AA417 ASP B 161 SER B 166 1 O THR B 164 N VAL B 134
SHEET 7 AA417 HIS B 194 ALA B 198 1 O THR B 196 N VAL B 165
SHEET 8 AA417 THR B 216 TYR B 220 1 O HIS B 218 N TYR B 197
SHEET 9 AA417 GLN B 239 ASP B 248 1 O ARG B 241 N ILE B 219
SHEET 10 AA417 TYR B 223 LEU B 225 1 N TYR B 224 O ASP B 248
SHEET 11 AA417 TYR B 201 SER B 207 1 N TRP B 202 O TYR B 223
SHEET 12 AA417 PHE B 169 LYS B 175 1 N LEU B 170 O TYR B 201
SHEET 13 AA417 ASP B 138 SER B 140 1 N LEU B 139 O PHE B 169
SHEET 14 AA417 LYS B 112 SER B 114 1 N ILE B 113 O ASP B 138
SHEET 15 AA417 GLU B 92 ASN B 101 1 N LEU B 93 O LYS B 112
SHEET 16 AA417 ILE B 124 GLN B 127 1 O GLY B 125 N ILE B 100
SHEET 17 AA417 LEU B 154 THR B 157 1 O ASP B 155 N ILE B 126
SHEET 1 AA5 9 LYS B 70 ARG B 78 0
SHEET 2 AA5 9 GLU B 92 ASN B 101 1 O TYR B 99 N VAL B 77
SHEET 3 AA5 9 LYS B 112 SER B 114 1 O LYS B 112 N LEU B 93
SHEET 4 AA5 9 ASP B 138 SER B 140 1 O ASP B 138 N ILE B 113
SHEET 5 AA5 9 PHE B 169 LYS B 175 1 O PHE B 169 N LEU B 139
SHEET 6 AA5 9 TYR B 201 SER B 207 1 O TYR B 201 N LEU B 170
SHEET 7 AA5 9 TYR B 223 LEU B 225 1 O TYR B 223 N TRP B 202
SHEET 8 AA5 9 GLN B 239 ASP B 248 1 O ASP B 248 N TYR B 224
SHEET 9 AA5 9 TYR B 265 SER B 272 1 O SER B 272 N PHE B 247
SHEET 1 AA6 5 LEU B 178 ILE B 179 0
SHEET 2 AA6 5 SER B 211 ARG B 213 1 O SER B 211 N ILE B 179
SHEET 3 AA6 5 VAL B 232 ARG B 235 1 O ASN B 233 N VAL B 212
SHEET 4 AA6 5 ASN B 253 ILE B 256 1 O ILE B 256 N THR B 234
SHEET 5 AA6 5 THR B 277 ASN B 278 1 O THR B 277 N ILE B 255
LINK OG1 THR A 22 C1 MAN A 406 1555 1555 1.36
LINK OG1 THR A 44 C1 MAN A 403 1555 1555 1.36
LINK OG1 THR A 45 C1 MAN A 407 1555 1555 1.09
LINK OG1 THR A 46 C1 MAN A 402 1555 1555 1.15
LINK OG SER A 48 C1 MAN A 404 1555 1555 1.06
LINK OG1 THR A 54 C1 MAN A 405 1555 1555 1.14
LINK OG1 THR B 22 C1 MAN B 406 1555 1555 1.29
LINK OG1 THR B 44 C1 MAN B 407 1555 1555 1.44
LINK OG1 THR B 45 C1 MAN B 405 1555 1555 1.43
LINK OG1 THR B 46 C1 MAN B 403 1555 1555 1.36
LINK OG SER B 48 C1 MAN B 404 1555 1555 1.01
LINK OG1 THR B 54 C1 MAN B 408 1555 1555 1.10
LINK OD1 ASP A 122 CA CA A 401 1555 1555 2.43
LINK OD2 ASP A 122 CA CA A 401 1555 1555 2.56
LINK OD2 ASP A 151 CA CA A 401 1555 1555 2.51
LINK OD2 ASP A 155 CA CA A 401 1555 1555 2.24
LINK CA CA A 401 O HOH A 568 1555 1555 2.40
LINK CA CA A 401 O HOH A 830 1555 1555 2.44
LINK CA CA A 401 OG SER B 288 1555 1555 2.43
LINK CA CA A 401 O HOH B 790 1555 1555 2.47
LINK OD1 ASP B 122 CA CA B 401 1555 1555 2.46
LINK OD2 ASP B 122 CA CA B 401 1555 1555 2.49
LINK OD2 ASP B 151 CA CA B 401 1555 1555 2.42
LINK OD2 ASP B 155 CA CA B 401 1555 1555 2.32
LINK CA CA B 401 O HOH B 505 1555 1555 2.09
LINK CA CA B 401 O HOH B 623 1555 1555 2.95
LINK CA CA B 401 O HOH B 742 1555 1555 2.26
LINK CA CA B 401 O HOH B 789 1555 1555 2.51
CISPEP 1 ASN A 209 PRO A 210 0 -8.29
CISPEP 2 ASN B 209 PRO B 210 0 -5.13
CRYST1 60.890 59.690 93.870 90.00 96.35 90.00 P 1 21 1 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 0.016423 0.000000 0.001828 0.00000
SCALE2 0.000000 0.016753 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010719 0.00000
MTRIX1 1 0.489435 -0.871308 -0.035712 -40.83195 1
MTRIX2 1 0.869118 0.484037 0.101696 -18.92001 1
MTRIX3 1 -0.071323 -0.080812 0.994174 -4.23548 1
ATOM 1 N ALA A 19 -2.180 3.221 -34.328 1.00 52.09 N
ATOM 2 CA ALA A 19 -2.380 1.786 -34.151 1.00 53.45 C
ATOM 3 C ALA A 19 -2.808 1.128 -35.451 1.00 48.59 C
ATOM 4 O ALA A 19 -3.336 1.802 -36.339 1.00 48.54 O
ATOM 5 CB ALA A 19 -3.436 1.538 -33.094 1.00 46.94 C
ATOM 6 HA ALA A 19 -1.550 1.378 -33.858 1.00 64.16 H
ATOM 7 HB1 ALA A 19 -3.557 0.581 -32.988 1.00 56.35 H
ATOM 8 HB2 ALA A 19 -3.142 1.929 -32.257 1.00 56.35 H
ATOM 9 HB3 ALA A 19 -4.268 1.948 -33.377 1.00 56.35 H
ATOM 10 N SER A 20 -2.586 -0.187 -35.544 1.00 38.01 N
ATOM 11 CA SER A 20 -2.952 -0.989 -36.702 1.00 37.38 C
ATOM 12 C SER A 20 -3.825 -2.166 -36.299 1.00 34.86 C
ATOM 13 O SER A 20 -3.630 -2.774 -35.237 1.00 37.79 O
ATOM 14 CB SER A 20 -1.666 -1.506 -37.397 1.00 43.73 C
ATOM 15 OG SER A 20 -1.917 -2.571 -38.301 1.00 47.84 O
ATOM 16 H SER A 20 -2.210 -0.647 -34.922 1.00 45.63 H
ATOM 17 HA SER A 20 -3.445 -0.443 -37.334 1.00 44.88 H
ATOM 18 HB2 SER A 20 -1.266 -0.772 -37.889 1.00 52.50 H
ATOM 19 HB3 SER A 20 -1.048 -1.815 -36.718 1.00 52.50 H
ATOM 20 HG SER A 20 -2.445 -2.318 -38.904 1.00 57.43 H
ATOM 21 N VAL A 21 -4.770 -2.486 -37.180 1.00 33.19 N
ATOM 22 CA VAL A 21 -5.665 -3.610 -36.955 1.00 33.85 C
ATOM 23 C VAL A 21 -4.884 -4.884 -36.714 1.00 34.25 C
ATOM 24 O VAL A 21 -5.292 -5.706 -35.890 1.00 32.07 O
ATOM 25 CB VAL A 21 -6.622 -3.778 -38.152 1.00 34.72 C
ATOM 26 CG1 VAL A 21 -7.323 -5.162 -38.161 1.00 36.84 C
ATOM 27 CG2 VAL A 21 -7.650 -2.668 -38.204 1.00 40.88 C
ATOM 28 H VAL A 21 -4.911 -2.065 -37.917 1.00 39.85 H
ATOM 29 HA VAL A 21 -6.195 -3.430 -36.167 1.00 40.64 H
ATOM 30 HB VAL A 21 -6.098 -3.719 -38.966 1.00 41.68 H
ATOM 31 HG11 VAL A 21 -8.085 -5.124 -38.760 1.00 44.23 H
ATOM 32 HG12 VAL A 21 -6.696 -5.835 -38.469 1.00 44.23 H
ATOM 33 HG13 VAL A 21 -7.622 -5.370 -37.262 1.00 44.23 H
ATOM 34 HG21 VAL A 21 -8.218 -2.800 -38.979 1.00 49.08 H
ATOM 35 HG22 VAL A 21 -8.183 -2.694 -37.394 1.00 49.08 H
ATOM 36 HG23 VAL A 21 -7.191 -1.816 -38.272 1.00 49.08 H
ATOM 37 N THR A 22 -3.778 -5.081 -37.418 1.00 33.04 N
ATOM 38 CA THR A 22 -3.031 -6.355 -37.350 1.00 34.05 C
ATOM 39 C THR A 22 -1.890 -6.342 -36.346 1.00 31.58 C
ATOM 40 O THR A 22 -1.081 -7.206 -36.440 1.00 34.66 O
ATOM 41 CB THR A 22 -2.567 -6.848 -38.720 1.00 43.47 C
ATOM 42 OG1 THR A 22 -1.730 -5.886 -39.340 1.00 46.64 O
ATOM 43 CG2 THR A 22 -3.761 -7.186 -39.573 1.00 47.55 C
ATOM 44 H THR A 22 -3.404 -4.468 -37.979 1.00 39.67 H
ATOM 45 HA THR A 22 -3.677 -7.023 -37.022 1.00 40.88 H
ATOM 46 HB THR A 22 -2.042 -7.672 -38.582 1.00 52.19 H
ATOM 47 HG21 THR A 22 -4.545 -7.298 -39.006 1.00 57.09 H
ATOM 48 HG22 THR A 22 -3.922 -6.466 -40.209 1.00 57.09 H
ATOM 49 HG23 THR A 22 -3.591 -8.014 -40.057 1.00 57.09 H
ATOM 50 N GLU A 23 -1.845 -5.421 -35.413 1.00 29.23 N
ATOM 51 CA GLU A 23 -0.832 -5.540 -34.365 1.00 29.27 C
ATOM 52 C GLU A 23 -1.128 -6.774 -33.526 1.00 29.92 C
ATOM 53 O GLU A 23 -2.285 -7.025 -33.171 1.00 28.90 O
ATOM 54 CB GLU A 23 -0.852 -4.329 -33.452 1.00 34.06 C
ATOM 55 CG GLU A 23 -0.145 -3.096 -33.995 1.00 46.07 C
ATOM 56 CD GLU A 23 -0.262 -1.901 -33.065 1.00 51.05 C
ATOM 57 OE1 GLU A 23 -1.270 -1.171 -33.155 1.00 38.79 O
ATOM 58 OE2 GLU A 23 0.651 -1.702 -32.249 1.00 53.37 O
ATOM 59 H GLU A 23 -2.330 -4.711 -35.381 1.00 35.10 H
ATOM 60 HA GLU A 23 0.050 -5.627 -34.760 1.00 35.14 H
ATOM 61 HB2 GLU A 23 -1.776 -4.085 -33.284 1.00 40.90 H
ATOM 62 HB3 GLU A 23 -0.422 -4.567 -32.616 1.00 40.90 H
ATOM 63 HG2 GLU A 23 0.797 -3.296 -34.111 1.00 55.31 H
ATOM 64 HG3 GLU A 23 -0.541 -2.855 -34.846 1.00 55.31 H
ATOM 65 N SER A 24 -0.103 -7.567 -33.253 1.00 29.43 N
ATOM 66 CA ASER A 24 -0.211 -8.753 -32.421 0.59 28.69 C
ATOM 67 CA BSER A 24 -0.253 -8.743 -32.415 0.41 28.72 C
ATOM 68 C SER A 24 0.134 -8.406 -30.980 1.00 26.01 C
ATOM 69 O SER A 24 0.729 -7.375 -30.690 1.00 26.16 O
ATOM 70 CB ASER A 24 0.760 -9.817 -32.913 0.59 30.01 C
ATOM 71 CB BSER A 24 0.612 -9.883 -32.942 0.41 29.85 C
ATOM 72 OG ASER A 24 2.108 -9.430 -32.642 0.59 32.22 O
ATOM 73 OG BSER A 24 0.258 -10.230 -34.276 0.41 29.20 O
ATOM 74 H ASER A 24 0.693 -7.433 -33.550 0.59 35.33 H
ATOM 75 H BSER A 24 0.697 -7.444 -33.544 0.41 35.33 H
ATOM 76 HA ASER A 24 -1.114 -9.106 -32.456 0.59 34.45 H
ATOM 77 HA BSER A 24 -1.178 -9.033 -32.423 0.41 34.48 H
ATOM 78 HB2ASER A 24 0.572 -10.652 -32.457 0.59 36.04 H
ATOM 79 HB2BSER A 24 1.541 -9.605 -32.926 0.41 35.84 H
ATOM 80 HB3ASER A 24 0.649 -9.929 -33.870 0.59 36.04 H
ATOM 81 HB3BSER A 24 0.490 -10.659 -32.373 0.41 35.84 H
ATOM 82 HG ASER A 24 2.637 -10.022 -32.916 0.59 38.69 H
ATOM 83 HG BSER A 24 -0.545 -10.474 -34.306 0.41 35.06 H
ATOM 84 N CYS A 25 -0.238 -9.303 -30.059 1.00 24.81 N
ATOM 85 CA CYS A 25 0.038 -9.041 -28.644 1.00 23.20 C
ATOM 86 C CYS A 25 1.545 -9.049 -28.381 1.00 26.85 C
ATOM 87 O CYS A 25 2.221 -10.058 -28.608 1.00 27.21 O
ATOM 88 CB CYS A 25 -0.659 -10.059 -27.759 1.00 26.70 C
ATOM 89 SG CYS A 25 -0.309 -9.762 -25.992 1.00 24.73 S
ATOM 90 H CYS A 25 -0.638 -10.047 -30.221 1.00 29.80 H
ATOM 91 HA CYS A 25 -0.301 -8.162 -28.414 1.00 27.86 H
ATOM 92 HB2 CYS A 25 -1.618 -9.997 -27.894 1.00 32.06 H
ATOM 93 HB3 CYS A 25 -0.345 -10.948 -27.986 1.00 32.06 H
ATOM 94 HG CYS A 25 -0.697 -8.666 -25.696 1.00 29.69 H
ATOM 95 N ASN A 26 2.047 -7.947 -27.822 1.00 23.46 N
ATOM 96 CA ASN A 26 3.448 -7.816 -27.425 1.00 25.68 C
ATOM 97 C ASN A 26 3.591 -7.522 -25.944 1.00 27.80 C
ATOM 98 O ASN A 26 4.586 -6.952 -25.513 1.00 27.90 O
ATOM 99 CB ASN A 26 4.126 -6.719 -28.242 1.00 28.61 C
ATOM 100 CG ASN A 26 3.502 -5.324 -28.016 1.00 43.10 C
ATOM 101 OD1 ASN A 26 2.338 -5.179 -27.608 1.00 33.57 O
ATOM 102 ND2 ASN A 26 4.287 -4.288 -28.294 1.00 46.83 N
ATOM 103 H ASN A 26 1.581 -7.243 -27.659 1.00 28.17 H
ATOM 104 HA ASN A 26 3.908 -8.650 -27.608 1.00 30.84 H
ATOM 105 HB2 ASN A 26 5.062 -6.672 -27.992 1.00 34.35 H
ATOM 106 HB3 ASN A 26 4.046 -6.933 -29.185 1.00 34.35 H
ATOM 107 HD21 ASN A 26 3.994 -3.486 -28.188 1.00 56.22 H
ATOM 108 HD22 ASN A 26 5.089 -4.419 -28.576 1.00 56.22 H
ATOM 109 N ILE A 27 2.608 -7.893 -25.140 1.00 23.95 N
ATOM 110 CA ILE A 27 2.608 -7.587 -23.718 1.00 24.47 C
ATOM 111 C ILE A 27 2.146 -8.833 -22.968 1.00 22.14 C
ATOM 112 O ILE A 27 1.087 -9.387 -23.290 1.00 22.95 O
ATOM 113 CB ILE A 27 1.612 -6.441 -23.380 1.00 25.66 C
ATOM 114 CG1 ILE A 27 1.936 -5.149 -24.147 1.00 26.49 C
ATOM 115 CG2 ILE A 27 1.509 -6.246 -21.864 1.00 25.72 C
ATOM 116 CD1 ILE A 27 0.809 -4.091 -24.013 1.00 27.56 C
ATOM 117 H ILE A 27 1.915 -8.332 -25.398 1.00 28.76 H
ATOM 118 HA ILE A 27 3.497 -7.342 -23.418 1.00 29.39 H
ATOM 119 HB ILE A 27 0.738 -6.732 -23.683 1.00 30.82 H
ATOM 120 HG12 ILE A 27 2.754 -4.766 -23.793 1.00 31.81 H
ATOM 121 HG13 ILE A 27 2.044 -5.355 -25.089 1.00 31.81 H
ATOM 122 HG21 ILE A 27 0.975 -6.962 -21.486 1.00 30.89 H
ATOM 123 HG22 ILE A 27 2.401 -6.263 -21.483 1.00 30.89 H
ATOM 124 HG23 ILE A 27 1.087 -5.393 -21.678 1.00 30.89 H
ATOM 125 HD11 ILE A 27 0.833 -3.712 -23.121 1.00 33.09 H
ATOM 126 HD12 ILE A 27 0.954 -3.393 -24.671 1.00 33.09 H
ATOM 127 HD13 ILE A 27 -0.047 -4.520 -24.170 1.00 33.09 H
ATOM 128 N GLY A 28 2.881 -9.238 -21.937 1.00 22.37 N
ATOM 129 CA GLY A 28 2.391 -10.178 -20.981 1.00 22.48 C
ATOM 130 C GLY A 28 2.198 -11.606 -21.481 1.00 20.75 C
ATOM 131 O GLY A 28 2.717 -12.056 -22.480 1.00 21.93 O
ATOM 132 H GLY A 28 3.682 -8.968 -21.780 1.00 26.87 H
ATOM 133 HA2 GLY A 28 3.004 -10.208 -20.235 1.00 26.99 H
ATOM 134 HA3 GLY A 28 1.535 -9.865 -20.649 1.00 26.99 H
ATOM 135 N TYR A 29 1.416 -12.336 -20.671 1.00 19.34 N
ATOM 136 CA TYR A 29 1.283 -13.775 -20.893 1.00 20.47 C
ATOM 137 C TYR A 29 0.649 -14.144 -22.224 1.00 21.32 C
ATOM 138 O TYR A 29 0.982 -15.191 -22.775 1.00 22.58 O
ATOM 139 CB TYR A 29 0.482 -14.420 -19.771 1.00 22.82 C
ATOM 140 CG TYR A 29 1.250 -14.653 -18.479 1.00 19.90 C
ATOM 141 CD1 TYR A 29 2.305 -15.593 -18.428 1.00 21.34 C
ATOM 142 CD2 TYR A 29 0.928 -13.962 -17.320 1.00 21.09 C
ATOM 143 CE1 TYR A 29 2.980 -15.807 -17.214 1.00 22.55 C
ATOM 144 CE2 TYR A 29 1.598 -14.174 -16.129 1.00 22.31 C
ATOM 145 CZ TYR A 29 2.617 -15.098 -16.085 1.00 24.27 C
ATOM 146 OH TYR A 29 3.251 -15.244 -14.872 1.00 31.65 O
ATOM 147 H TYR A 29 0.965 -12.029 -20.007 1.00 23.23 H
ATOM 148 HA TYR A 29 2.170 -14.167 -20.879 1.00 24.58 H
ATOM 149 HB2 TYR A 29 -0.273 -13.848 -19.563 1.00 27.40 H
ATOM 150 HB3 TYR A 29 0.162 -15.282 -20.078 1.00 27.40 H
ATOM 151 HD1 TYR A 29 2.539 -16.077 -19.187 1.00 25.64 H
ATOM 152 HD2 TYR A 29 0.233 -13.345 -17.342 1.00 25.33 H
ATOM 153 HE1 TYR A 29 3.676 -16.422 -17.172 1.00 27.08 H
ATOM 154 HE2 TYR A 29 1.363 -13.697 -15.366 1.00 26.79 H
ATOM 155 HH TYR A 29 3.867 -15.812 -14.936 1.00 38.01 H
ATOM 156 N ALA A 30 -0.239 -13.318 -22.789 1.00 21.93 N
ATOM 157 CA ALA A 30 -0.808 -13.651 -24.089 1.00 21.38 C
ATOM 158 C ALA A 30 0.217 -13.553 -25.211 1.00 22.52 C
ATOM 159 O ALA A 30 -0.071 -14.019 -26.313 1.00 24.14 O
ATOM 160 CB ALA A 30 -2.017 -12.741 -24.375 1.00 22.03 C
ATOM 161 H ALA A 30 -0.519 -12.580 -22.448 1.00 26.34 H
ATOM 162 HA ALA A 30 -1.128 -14.566 -24.062 1.00 25.67 H
ATOM 163 HB1 ALA A 30 -2.684 -12.876 -23.684 1.00 26.46 H
ATOM 164 HB2 ALA A 30 -1.723 -11.817 -24.375 1.00 26.46 H
ATOM 165 HB3 ALA A 30 -2.387 -12.971 -25.242 1.00 26.46 H
ATOM 166 N SER A 31 1.390 -12.970 -24.939 1.00 21.90 N
ATOM 167 CA SER A 31 2.458 -12.951 -25.932 1.00 25.63 C
ATOM 168 C SER A 31 3.299 -14.216 -25.883 1.00 23.41 C
ATOM 169 O SER A 31 4.171 -14.387 -26.753 1.00 25.46 O
ATOM 170 CB SER A 31 3.329 -11.696 -25.749 1.00 27.38 C
ATOM 171 OG SER A 31 4.220 -11.854 -24.661 1.00 26.39 O
ATOM 172 H SER A 31 1.587 -12.584 -24.197 1.00 26.30 H
ATOM 173 HA SER A 31 2.058 -12.901 -26.814 1.00 30.77 H
ATOM 174 HB2 SER A 31 3.843 -11.547 -26.558 1.00 32.88 H
ATOM 175 HB3 SER A 31 2.753 -10.935 -25.577 1.00 32.88 H
ATOM 176 HG SER A 31 4.689 -11.163 -24.571 1.00 31.69 H
ATOM 177 N THR A 32 3.050 -15.099 -24.918 1.00 24.05 N
ATOM 178 CA THR A 32 3.800 -16.331 -24.778 1.00 23.53 C
ATOM 179 C THR A 32 2.978 -17.490 -25.354 1.00 25.19 C
ATOM 180 O THR A 32 1.837 -17.326 -25.832 1.00 25.16 O
ATOM 181 CB THR A 32 4.151 -16.652 -23.319 1.00 23.71 C
ATOM 182 OG1 THR A 32 2.966 -17.073 -22.624 1.00 23.56 O
ATOM 183 CG2 THR A 32 4.759 -15.481 -22.587 1.00 24.20 C
ATOM 184 H THR A 32 2.438 -15.001 -24.322 1.00 28.88 H
ATOM 185 HA THR A 32 4.627 -16.264 -25.281 1.00 28.25 H
ATOM 186 HB THR A 32 4.795 -17.377 -23.305 1.00 28.47 H
ATOM 187 HG1 THR A 32 3.150 -17.251 -21.824 1.00 28.30 H
ATOM 188 HG21 THR A 32 5.006 -15.745 -21.687 1.00 29.06 H
ATOM 189 HG22 THR A 32 5.552 -15.174 -23.054 1.00 29.06 H
ATOM 190 HG23 THR A 32 4.120 -14.753 -22.537 1.00 29.06 H
ATOM 191 N ASN A 33 3.549 -18.705 -25.297 1.00 24.15 N
ATOM 192 CA ASN A 33 2.828 -19.931 -25.646 1.00 23.81 C
ATOM 193 C ASN A 33 2.130 -19.823 -27.000 1.00 25.46 C
ATOM 194 O ASN A 33 0.963 -20.193 -27.157 1.00 30.65 O
ATOM 195 CB ASN A 33 1.858 -20.319 -24.520 1.00 27.14 C
ATOM 196 CG ASN A 33 2.606 -20.893 -23.338 1.00 26.11 C
ATOM 197 OD1 ASN A 33 2.766 -22.118 -23.237 1.00 29.61 O
ATOM 198 ND2 ASN A 33 3.061 -20.051 -22.450 1.00 24.73 N
ATOM 199 H ASN A 33 4.363 -18.841 -25.056 1.00 29.00 H
ATOM 200 HA ASN A 33 3.477 -20.648 -25.720 1.00 28.59 H
ATOM 201 HB2 ASN A 33 1.376 -19.531 -24.224 1.00 32.58 H
ATOM 202 HB3 ASN A 33 1.239 -20.992 -24.845 1.00 32.58 H
ATOM 203 HD21 ASN A 33 3.491 -20.340 -21.764 1.00 29.70 H
ATOM 204 HD22 ASN A 33 2.931 -19.207 -22.552 1.00 29.70 H
ATOM 205 N GLY A 34 2.863 -19.322 -27.979 1.00 27.73 N
ATOM 206 CA GLY A 34 2.395 -19.172 -29.334 1.00 33.22 C
ATOM 207 C GLY A 34 1.998 -17.765 -29.699 1.00 32.22 C
ATOM 208 O GLY A 34 1.901 -17.453 -30.905 1.00 31.74 O
ATOM 209 H GLY A 34 3.672 -19.051 -27.871 1.00 33.30 H
ATOM 210 HA2 GLY A 34 3.095 -19.454 -29.943 1.00 39.88 H
ATOM 211 HA3 GLY A 34 1.627 -19.748 -29.472 1.00 39.88 H
ATOM 212 N GLY A 35 1.702 -16.913 -28.687 1.00 27.39 N
ATOM 213 CA GLY A 35 1.314 -15.553 -28.979 1.00 29.09 C
ATOM 214 C GLY A 35 -0.146 -15.426 -29.349 1.00 24.46 C
ATOM 215 O GLY A 35 -0.903 -16.388 -29.367 1.00 27.59 O
ATOM 216 H GLY A 35 1.723 -17.111 -27.850 1.00 32.88 H
ATOM 217 HA2 GLY A 35 1.482 -14.997 -28.202 1.00 34.93 H
ATOM 218 HA3 GLY A 35 1.847 -15.218 -29.717 1.00 34.93 H
ATOM 219 N THR A 36 -0.539 -14.188 -29.642 1.00 25.69 N