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HEADER HYDROLASE/VIRAL PROTEIN 15-MAY-13 4KR0
TITLE COMPLEX STRUCTURE OF MERS-COV SPIKE RBD BOUND TO CD26
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ADCP-2, DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION
COMPND 5 ANTIGEN CD26, TP103, DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM, DIPEPTIDYL
COMPND 6 PEPTIDASE IV SOLUBLE FORM;
COMPND 7 EC: 3.4.14.5;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: S PROTEIN;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: UNP RESIDUES 367-606;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ADCP2, CD26, DPP4;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HIGH5;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PFAST-BAC1;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HUMAN BETACORONAVIRUS 2C EMC/2012;
SOURCE 14 ORGANISM_TAXID: 1235996;
SOURCE 15 GENE: S, SPIKE;
SOURCE 16 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 17 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 19 EXPRESSION_SYSTEM_CELL_LINE: HIGH5;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR: PFAST-BAC1
KEYWDS 8-BLADED BETA-PROPELLER DOMAIN, ALPHA/BETA HYDROLASE DOMAIN, BLADES
KEYWDS 2 IV AND V, CD26 BETA-PROPELLER, HYDROLASE-VIRAL PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.LU,Y.HU,Q.WANG,J.QI,F.GAO,Y.LI,Y.ZHANG,W.ZHANG,Y.YUAN,B.ZHANG,
AUTHOR 2 Y.SHI,J.YAN,G.F.GAO
REVDAT 1 10-JUL-13 4KR0 0
JRNL AUTH G.LU,Y.HU,Q.WANG,J.QI,F.GAO,Y.LI,Y.ZHANG,W.ZHANG,Y.YUAN,
JRNL AUTH 2 J.BAO,B.ZHANG,Y.SHI,J.YAN,G.F.GAO
JRNL TITL MOLECULAR BASIS OF BINDING BETWEEN NOVEL HUMAN CORONAVIRUS
JRNL TITL 2 MERS-COV AND ITS RECEPTOR CD26
JRNL REF NATURE 2013
JRNL REFN ESSN 1476-4687
JRNL DOI 10.1038/NATURE12328
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 53432
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 2712
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 48.8584 - 7.2037 1.00 3001 172 0.2134 0.2042
REMARK 3 2 7.2037 - 5.7207 1.00 2805 131 0.2146 0.2859
REMARK 3 3 5.7207 - 4.9983 1.00 2741 133 0.1780 0.1961
REMARK 3 4 4.9983 - 4.5417 1.00 2715 144 0.1506 0.1658
REMARK 3 5 4.5417 - 4.2164 1.00 2708 125 0.1534 0.1550
REMARK 3 6 4.2164 - 3.9679 1.00 2672 142 0.1683 0.2079
REMARK 3 7 3.9679 - 3.7693 1.00 2636 183 0.1809 0.2275
REMARK 3 8 3.7693 - 3.6052 1.00 2650 147 0.1852 0.2302
REMARK 3 9 3.6052 - 3.4665 1.00 2624 148 0.2060 0.2405
REMARK 3 10 3.4665 - 3.3469 1.00 2620 150 0.2122 0.2652
REMARK 3 11 3.3469 - 3.2423 1.00 2606 150 0.2215 0.2649
REMARK 3 12 3.2423 - 3.1496 1.00 2642 143 0.2299 0.2719
REMARK 3 13 3.1496 - 3.0667 1.00 2608 147 0.2236 0.2903
REMARK 3 14 3.0667 - 2.9919 1.00 2629 136 0.2334 0.2847
REMARK 3 15 2.9919 - 2.9239 1.00 2618 144 0.2369 0.3361
REMARK 3 16 2.9239 - 2.8617 1.00 2626 141 0.2419 0.2784
REMARK 3 17 2.8617 - 2.8044 1.00 2583 140 0.2383 0.3057
REMARK 3 18 2.8044 - 2.7515 1.00 2615 112 0.2528 0.3321
REMARK 3 19 2.7515 - 2.7024 0.99 2621 124 0.2561 0.3297
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.760
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 : 0.006 7983
REMARK 3 ANGLE : 1.028 10867
REMARK 3 CHIRALITY : 0.073 1197
REMARK 3 PLANARITY : 0.004 1361
REMARK 3 DIHEDRAL : 19.079 2905
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -19.8772 39.4682 16.8127
REMARK 3 T TENSOR
REMARK 3 T11: 0.1531 T22: 0.2612
REMARK 3 T33: 0.2129 T12: -0.0289
REMARK 3 T13: 0.0060 T23: -0.0246
REMARK 3 L TENSOR
REMARK 3 L11: 0.1898 L22: 0.2612
REMARK 3 L33: 0.3489 L12: -0.0430
REMARK 3 L13: -0.1785 L23: 0.2142
REMARK 3 S TENSOR
REMARK 3 S11: 0.0019 S12: 0.0894 S13: -0.0424
REMARK 3 S21: 0.0158 S22: -0.0261 S23: 0.0406
REMARK 3 S31: -0.0017 S32: 0.1122 S33: -0.0438
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 4KR0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-MAY-13.
REMARK 100 THE RCSB ID CODE IS RCSB079685.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97930
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53576
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.11500
REMARK 200 R SYM (I) : 0.11500
REMARK 200 FOR THE DATA SET : 18.6800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.90
REMARK 200 R MERGE FOR SHELL (I) : 0.63900
REMARK 200 R SYM FOR SHELL (I) : 0.63900
REMARK 200 FOR SHELL : 3.688
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: 2BGR AND 4KQZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% V/V 2-PROPANOL, 0.1M SODIUM ACETATE
REMARK 280 PH4.5, 26% PEG 550, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 175.86633
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 351.73267
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 263.79950
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 439.66583
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 87.93317
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 175.86633
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 351.73267
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 439.66583
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 263.79950
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 87.93317
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 77330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 72.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 BIOMT1 2 0.500000 0.866025 0.000000 -55.11200
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 95.45678
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 87.93317
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 ALA A 34
REMARK 465 ASP A 35
REMARK 465 GLY A 36
REMARK 465 ILE A 37
REMARK 465 GLN A 38
REMARK 465 HIS A 767
REMARK 465 HIS A 768
REMARK 465 HIS A 769
REMARK 465 HIS A 770
REMARK 465 HIS A 771
REMARK 465 HIS A 772
REMARK 465 ALA B 362
REMARK 465 ASP B 363
REMARK 465 GLY B 364
REMARK 465 ILE B 365
REMARK 465 GLN B 366
REMARK 465 GLU B 367
REMARK 465 ALA B 368
REMARK 465 LYS B 369
REMARK 465 PRO B 370
REMARK 465 SER B 371
REMARK 465 GLY B 372
REMARK 465 SER B 373
REMARK 465 VAL B 374
REMARK 465 VAL B 375
REMARK 465 GLU B 376
REMARK 465 GLN B 377
REMARK 465 ALA B 378
REMARK 465 GLU B 379
REMARK 465 GLY B 380
REMARK 465 GLU B 589
REMARK 465 PHE B 590
REMARK 465 ALA B 591
REMARK 465 ASN B 592
REMARK 465 ASP B 593
REMARK 465 THR B 594
REMARK 465 LYS B 595
REMARK 465 ILE B 596
REMARK 465 ALA B 597
REMARK 465 SER B 598
REMARK 465 GLN B 599
REMARK 465 LEU B 600
REMARK 465 GLY B 601
REMARK 465 ASN B 602
REMARK 465 CYS B 603
REMARK 465 VAL B 604
REMARK 465 GLU B 605
REMARK 465 TYR B 606
REMARK 465 HIS B 607
REMARK 465 HIS B 608
REMARK 465 HIS B 609
REMARK 465 HIS B 610
REMARK 465 HIS B 611
REMARK 465 HIS B 612
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 HOH A 901 O HOH A 1041 1.81
REMARK 500 O HOH B 713 O HOH B 717 1.89
REMARK 500 O HOH A 944 O HOH A 1037 1.90
REMARK 500 OH TYR A 211 O HOH A 1016 1.94
REMARK 500 O4 NAG A 807 C2 BMA A 808 2.03
REMARK 500 O HOH A 968 O HOH A 994 2.05
REMARK 500 O4 NAG A 807 O2 BMA A 808 2.05
REMARK 500 O HOH A 993 O HOH A 1046 2.08
REMARK 500 OD2 ASP A 588 O HOH A 1023 2.09
REMARK 500 O GLY A 400 O HOH A 923 2.11
REMARK 500 O HOH A 974 O HOH A 1000 2.12
REMARK 500 OH TYR A 457 O HOH A 957 2.12
REMARK 500 O HOH A 935 O HOH A 1060 2.13
REMARK 500 O6 NAG A 813 O HOH A 953 2.13
REMARK 500 O HOH A 986 O HOH A 1021 2.14
REMARK 500 OH TYR A 299 O HOH A 911 2.15
REMARK 500 O PHE B 399 OH TYR B 523 2.15
REMARK 500 O4 NAG A 807 O5 BMA A 808 2.16
REMARK 500 OH TYR A 381 O HOH A 1022 2.17
REMARK 500 ND2 ASN A 321 C2 NAG A 811 2.18
REMARK 500 OH TYR A 105 O HOH A 987 2.18
REMARK 500 OD2 ASP A 729 O HOH A 941 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 HIS A 66 14.09 -156.41
REMARK 500 GLU A 82 -74.93 -55.08
REMARK 500 ASP A 96 33.03 -78.16
REMARK 500 GLU A 97 27.72 -159.15
REMARK 500 PRO A 109 -6.41 -57.53
REMARK 500 GLN A 123 -92.45 -127.02
REMARK 500 TRP A 124 -159.71 -99.72
REMARK 500 HIS A 162 33.17 -158.16
REMARK 500 ILE A 193 -65.06 -123.05
REMARK 500 VAL A 207 -65.43 -126.91
REMARK 500 SER A 242 -161.23 57.68
REMARK 500 GLN A 320 45.51 -85.29
REMARK 500 THR A 401 57.67 -92.29
REMARK 500 ASN A 450 56.82 -160.57
REMARK 500 ASN A 520 77.84 2.51
REMARK 500 ASN A 562 -157.29 -131.28
REMARK 500 ARG A 597 51.82 -153.31
REMARK 500 THR A 600 -97.57 -106.59
REMARK 500 SER A 630 -123.41 53.59
REMARK 500 ASP A 678 -94.71 -114.93
REMARK 500 ASN A 710 -76.88 -85.88
REMARK 500 ASP A 739 -158.91 -87.24
REMARK 500 GLU B 382 116.40 66.38
REMARK 500 VAL B 396 -39.89 -39.71
REMARK 500 LEU B 456 78.39 -100.15
REMARK 500 SER B 459 58.44 -107.04
REMARK 500 PRO B 485 -108.90 -72.15
REMARK 500 HIS B 486 -37.15 -143.51
REMARK 500 SER B 508 4.59 -69.36
REMARK 500 LYS B 543 117.81 -164.74
REMARK 500 ASN B 582 61.49 -62.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A
REMARK 800 85 RESIDUES 801 TO 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 813 BOUND
REMARK 800 TO ASN A 92
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 803 BOUND
REMARK 800 TO ASN A 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A
REMARK 800 219 RESIDUES 804 TO 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A
REMARK 800 229 RESIDUES 806 TO 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A
REMARK 800 281 RESIDUES 809 TO 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A
REMARK 800 321 RESIDUES 811 TO 812
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KQZ RELATED DB: PDB
REMARK 900 STRUCTURE OF FREE MERS-COV SPIKE RBD
DBREF 4KR0 A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 4KR0 B 367 606 UNP K0BRG7 K0BRG7_9BETC 367 606
SEQADV 4KR0 ALA A 34 UNP P27487 EXPRESSION TAG
SEQADV 4KR0 ASP A 35 UNP P27487 EXPRESSION TAG
SEQADV 4KR0 GLY A 36 UNP P27487 EXPRESSION TAG
SEQADV 4KR0 ILE A 37 UNP P27487 EXPRESSION TAG
SEQADV 4KR0 GLN A 38 UNP P27487 EXPRESSION TAG
SEQADV 4KR0 HIS A 767 UNP P27487 EXPRESSION TAG
SEQADV 4KR0 HIS A 768 UNP P27487 EXPRESSION TAG
SEQADV 4KR0 HIS A 769 UNP P27487 EXPRESSION TAG
SEQADV 4KR0 HIS A 770 UNP P27487 EXPRESSION TAG
SEQADV 4KR0 HIS A 771 UNP P27487 EXPRESSION TAG
SEQADV 4KR0 HIS A 772 UNP P27487 EXPRESSION TAG
SEQADV 4KR0 ALA B 362 UNP K0BRG7 EXPRESSION TAG
SEQADV 4KR0 ASP B 363 UNP K0BRG7 EXPRESSION TAG
SEQADV 4KR0 GLY B 364 UNP K0BRG7 EXPRESSION TAG
SEQADV 4KR0 ILE B 365 UNP K0BRG7 EXPRESSION TAG
SEQADV 4KR0 GLN B 366 UNP K0BRG7 EXPRESSION TAG
SEQADV 4KR0 HIS B 607 UNP K0BRG7 EXPRESSION TAG
SEQADV 4KR0 HIS B 608 UNP K0BRG7 EXPRESSION TAG
SEQADV 4KR0 HIS B 609 UNP K0BRG7 EXPRESSION TAG
SEQADV 4KR0 HIS B 610 UNP K0BRG7 EXPRESSION TAG
SEQADV 4KR0 HIS B 611 UNP K0BRG7 EXPRESSION TAG
SEQADV 4KR0 HIS B 612 UNP K0BRG7 EXPRESSION TAG
SEQRES 1 A 739 ALA ASP GLY ILE GLN SER ARG LYS THR TYR THR LEU THR
SEQRES 2 A 739 ASP TYR LEU LYS ASN THR TYR ARG LEU LYS LEU TYR SER
SEQRES 3 A 739 LEU ARG TRP ILE SER ASP HIS GLU TYR LEU TYR LYS GLN
SEQRES 4 A 739 GLU ASN ASN ILE LEU VAL PHE ASN ALA GLU TYR GLY ASN
SEQRES 5 A 739 SER SER VAL PHE LEU GLU ASN SER THR PHE ASP GLU PHE
SEQRES 6 A 739 GLY HIS SER ILE ASN ASP TYR SER ILE SER PRO ASP GLY
SEQRES 7 A 739 GLN PHE ILE LEU LEU GLU TYR ASN TYR VAL LYS GLN TRP
SEQRES 8 A 739 ARG HIS SER TYR THR ALA SER TYR ASP ILE TYR ASP LEU
SEQRES 9 A 739 ASN LYS ARG GLN LEU ILE THR GLU GLU ARG ILE PRO ASN
SEQRES 10 A 739 ASN THR GLN TRP VAL THR TRP SER PRO VAL GLY HIS LYS
SEQRES 11 A 739 LEU ALA TYR VAL TRP ASN ASN ASP ILE TYR VAL LYS ILE
SEQRES 12 A 739 GLU PRO ASN LEU PRO SER TYR ARG ILE THR TRP THR GLY
SEQRES 13 A 739 LYS GLU ASP ILE ILE TYR ASN GLY ILE THR ASP TRP VAL
SEQRES 14 A 739 TYR GLU GLU GLU VAL PHE SER ALA TYR SER ALA LEU TRP
SEQRES 15 A 739 TRP SER PRO ASN GLY THR PHE LEU ALA TYR ALA GLN PHE
SEQRES 16 A 739 ASN ASP THR GLU VAL PRO LEU ILE GLU TYR SER PHE TYR
SEQRES 17 A 739 SER ASP GLU SER LEU GLN TYR PRO LYS THR VAL ARG VAL
SEQRES 18 A 739 PRO TYR PRO LYS ALA GLY ALA VAL ASN PRO THR VAL LYS
SEQRES 19 A 739 PHE PHE VAL VAL ASN THR ASP SER LEU SER SER VAL THR
SEQRES 20 A 739 ASN ALA THR SER ILE GLN ILE THR ALA PRO ALA SER MET
SEQRES 21 A 739 LEU ILE GLY ASP HIS TYR LEU CYS ASP VAL THR TRP ALA
SEQRES 22 A 739 THR GLN GLU ARG ILE SER LEU GLN TRP LEU ARG ARG ILE
SEQRES 23 A 739 GLN ASN TYR SER VAL MET ASP ILE CYS ASP TYR ASP GLU
SEQRES 24 A 739 SER SER GLY ARG TRP ASN CYS LEU VAL ALA ARG GLN HIS
SEQRES 25 A 739 ILE GLU MET SER THR THR GLY TRP VAL GLY ARG PHE ARG
SEQRES 26 A 739 PRO SER GLU PRO HIS PHE THR LEU ASP GLY ASN SER PHE
SEQRES 27 A 739 TYR LYS ILE ILE SER ASN GLU GLU GLY TYR ARG HIS ILE
SEQRES 28 A 739 CYS TYR PHE GLN ILE ASP LYS LYS ASP CYS THR PHE ILE
SEQRES 29 A 739 THR LYS GLY THR TRP GLU VAL ILE GLY ILE GLU ALA LEU
SEQRES 30 A 739 THR SER ASP TYR LEU TYR TYR ILE SER ASN GLU TYR LYS
SEQRES 31 A 739 GLY MET PRO GLY GLY ARG ASN LEU TYR LYS ILE GLN LEU
SEQRES 32 A 739 SER ASP TYR THR LYS VAL THR CYS LEU SER CYS GLU LEU
SEQRES 33 A 739 ASN PRO GLU ARG CYS GLN TYR TYR SER VAL SER PHE SER
SEQRES 34 A 739 LYS GLU ALA LYS TYR TYR GLN LEU ARG CYS SER GLY PRO
SEQRES 35 A 739 GLY LEU PRO LEU TYR THR LEU HIS SER SER VAL ASN ASP
SEQRES 36 A 739 LYS GLY LEU ARG VAL LEU GLU ASP ASN SER ALA LEU ASP
SEQRES 37 A 739 LYS MET LEU GLN ASN VAL GLN MET PRO SER LYS LYS LEU
SEQRES 38 A 739 ASP PHE ILE ILE LEU ASN GLU THR LYS PHE TRP TYR GLN
SEQRES 39 A 739 MET ILE LEU PRO PRO HIS PHE ASP LYS SER LYS LYS TYR
SEQRES 40 A 739 PRO LEU LEU LEU ASP VAL TYR ALA GLY PRO CYS SER GLN
SEQRES 41 A 739 LYS ALA ASP THR VAL PHE ARG LEU ASN TRP ALA THR TYR
SEQRES 42 A 739 LEU ALA SER THR GLU ASN ILE ILE VAL ALA SER PHE ASP
SEQRES 43 A 739 GLY ARG GLY SER GLY TYR GLN GLY ASP LYS ILE MET HIS
SEQRES 44 A 739 ALA ILE ASN ARG ARG LEU GLY THR PHE GLU VAL GLU ASP
SEQRES 45 A 739 GLN ILE GLU ALA ALA ARG GLN PHE SER LYS MET GLY PHE
SEQRES 46 A 739 VAL ASP ASN LYS ARG ILE ALA ILE TRP GLY TRP SER TYR
SEQRES 47 A 739 GLY GLY TYR VAL THR SER MET VAL LEU GLY SER GLY SER
SEQRES 48 A 739 GLY VAL PHE LYS CYS GLY ILE ALA VAL ALA PRO VAL SER
SEQRES 49 A 739 ARG TRP GLU TYR TYR ASP SER VAL TYR THR GLU ARG TYR
SEQRES 50 A 739 MET GLY LEU PRO THR PRO GLU ASP ASN LEU ASP HIS TYR
SEQRES 51 A 739 ARG ASN SER THR VAL MET SER ARG ALA GLU ASN PHE LYS
SEQRES 52 A 739 GLN VAL GLU TYR LEU LEU ILE HIS GLY THR ALA ASP ASP
SEQRES 53 A 739 ASN VAL HIS PHE GLN GLN SER ALA GLN ILE SER LYS ALA
SEQRES 54 A 739 LEU VAL ASP VAL GLY VAL ASP PHE GLN ALA MET TRP TYR
SEQRES 55 A 739 THR ASP GLU ASP HIS GLY ILE ALA SER SER THR ALA HIS
SEQRES 56 A 739 GLN HIS ILE TYR THR HIS MET SER HIS PHE ILE LYS GLN
SEQRES 57 A 739 CYS PHE SER LEU PRO HIS HIS HIS HIS HIS HIS
SEQRES 1 B 251 ALA ASP GLY ILE GLN GLU ALA LYS PRO SER GLY SER VAL
SEQRES 2 B 251 VAL GLU GLN ALA GLU GLY VAL GLU CYS ASP PHE SER PRO
SEQRES 3 B 251 LEU LEU SER GLY THR PRO PRO GLN VAL TYR ASN PHE LYS
SEQRES 4 B 251 ARG LEU VAL PHE THR ASN CYS ASN TYR ASN LEU THR LYS
SEQRES 5 B 251 LEU LEU SER LEU PHE SER VAL ASN ASP PHE THR CYS SER
SEQRES 6 B 251 GLN ILE SER PRO ALA ALA ILE ALA SER ASN CYS TYR SER
SEQRES 7 B 251 SER LEU ILE LEU ASP TYR PHE SER TYR PRO LEU SER MET
SEQRES 8 B 251 LYS SER ASP LEU SER VAL SER SER ALA GLY PRO ILE SER
SEQRES 9 B 251 GLN PHE ASN TYR LYS GLN SER PHE SER ASN PRO THR CYS
SEQRES 10 B 251 LEU ILE LEU ALA THR VAL PRO HIS ASN LEU THR THR ILE
SEQRES 11 B 251 THR LYS PRO LEU LYS TYR SER TYR ILE ASN LYS CYS SER
SEQRES 12 B 251 ARG LEU LEU SER ASP ASP ARG THR GLU VAL PRO GLN LEU
SEQRES 13 B 251 VAL ASN ALA ASN GLN TYR SER PRO CYS VAL SER ILE VAL
SEQRES 14 B 251 PRO SER THR VAL TRP GLU ASP GLY ASP TYR TYR ARG LYS
SEQRES 15 B 251 GLN LEU SER PRO LEU GLU GLY GLY GLY TRP LEU VAL ALA
SEQRES 16 B 251 SER GLY SER THR VAL ALA MET THR GLU GLN LEU GLN MET
SEQRES 17 B 251 GLY PHE GLY ILE THR VAL GLN TYR GLY THR ASP THR ASN
SEQRES 18 B 251 SER VAL CYS PRO LYS LEU GLU PHE ALA ASN ASP THR LYS
SEQRES 19 B 251 ILE ALA SER GLN LEU GLY ASN CYS VAL GLU TYR HIS HIS
SEQRES 20 B 251 HIS HIS HIS HIS
MODRES 4KR0 ASN A 229 ASN GLYCOSYLATION SITE
MODRES 4KR0 ASN A 321 ASN GLYCOSYLATION SITE
MODRES 4KR0 ASN A 85 ASN GLYCOSYLATION SITE
MODRES 4KR0 ASN A 150 ASN GLYCOSYLATION SITE
MODRES 4KR0 ASN A 219 ASN GLYCOSYLATION SITE
MODRES 4KR0 ASN A 281 ASN GLYCOSYLATION SITE
MODRES 4KR0 ASN A 92 ASN GLYCOSYLATION SITE
HET NAG A 801 14
HET NAG A 802 14
HET NAG A 803 14
HET NAG A 804 14
HET NAG A 805 14
HET NAG A 806 14
HET NAG A 807 14
HET BMA A 808 11
HET NAG A 809 14
HET NAG A 810 14
HET NAG A 811 14
HET NAG A 812 14
HET NAG A 813 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM BMA BETA-D-MANNOSE
FORMUL 3 NAG 12(C8 H15 N O6)
FORMUL 6 BMA C6 H12 O6
FORMUL 10 HOH *194(H2 O)
HELIX 1 1 THR A 44 ASN A 51 1 8
HELIX 2 2 GLU A 91 ASP A 96 5 6
HELIX 3 3 ASP A 200 VAL A 207 1 8
HELIX 4 4 PRO A 290 ILE A 295 1 6
HELIX 5 5 LEU A 340 GLN A 344 5 5
HELIX 6 6 GLU A 421 MET A 425 5 5
HELIX 7 7 ASN A 497 LEU A 504 1 8
HELIX 8 8 GLN A 505 VAL A 507 5 3
HELIX 9 9 ASN A 562 THR A 570 1 9
HELIX 10 10 GLY A 587 HIS A 592 1 6
HELIX 11 11 ALA A 593 ASN A 595 5 3
HELIX 12 12 THR A 600 LYS A 615 1 16
HELIX 13 13 SER A 630 GLY A 641 1 12
HELIX 14 14 ARG A 658 TYR A 662 5 5
HELIX 15 15 ASP A 663 GLY A 672 1 10
HELIX 16 16 ASN A 679 SER A 686 1 8
HELIX 17 17 VAL A 688 VAL A 698 5 11
HELIX 18 18 HIS A 712 ASP A 725 1 14
HELIX 19 19 SER A 744 PHE A 763 1 20
HELIX 20 20 PHE B 385 SER B 390 1 6
HELIX 21 21 GLN B 395 PHE B 399 5 5
HELIX 22 22 ASN B 410 PHE B 418 1 9
HELIX 23 23 SER B 429 ASN B 436 1 8
HELIX 24 24 PRO B 449 LEU B 456 5 8
HELIX 25 25 GLY B 462 ASN B 468 1 7
SHEET 1 A 4 ARG A 61 TRP A 62 0
SHEET 2 A 4 GLU A 67 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 A 4 ASN A 75 ASN A 80 -1 O LEU A 77 N TYR A 70
SHEET 4 A 4 SER A 86 LEU A 90 -1 O PHE A 89 N ILE A 76
SHEET 1 B 4 ILE A 102 ILE A 107 0
SHEET 2 B 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 B 4 TYR A 128 ASP A 136 -1 O SER A 131 N TYR A 118
SHEET 4 B 4 GLN A 141 ILE A 143 -1 O ILE A 143 N ILE A 134
SHEET 1 C 4 THR A 152 TRP A 157 0
SHEET 2 C 4 LEU A 164 TRP A 168 -1 O VAL A 167 N GLN A 153
SHEET 3 C 4 ASP A 171 LYS A 175 -1 O LYS A 175 N LEU A 164
SHEET 4 C 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 D 3 ILE A 194 ASN A 196 0
SHEET 2 D 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 D 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 E 4 ILE A 194 ASN A 196 0
SHEET 2 E 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 E 4 THR A 265 ASN A 272 -1 O VAL A 271 N LEU A 223
SHEET 4 E 4 SER A 284 ILE A 287 -1 O ILE A 285 N VAL A 270
SHEET 1 F 2 LEU A 235 PHE A 240 0
SHEET 2 F 2 LYS A 250 PRO A 255 -1 O LYS A 250 N PHE A 240
SHEET 1 G 4 HIS A 298 TRP A 305 0
SHEET 2 G 4 ARG A 310 ARG A 317 -1 O LEU A 316 N TYR A 299
SHEET 3 G 4 TYR A 322 TYR A 330 -1 O ASP A 326 N LEU A 313
SHEET 4 G 4 TRP A 337 ASN A 338 -1 O ASN A 338 N ASP A 329
SHEET 1 H 4 HIS A 298 TRP A 305 0
SHEET 2 H 4 ARG A 310 ARG A 317 -1 O LEU A 316 N TYR A 299
SHEET 3 H 4 TYR A 322 TYR A 330 -1 O ASP A 326 N LEU A 313
SHEET 4 H 4 HIS A 345 MET A 348 -1 O GLU A 347 N SER A 323
SHEET 1 I 4 HIS A 363 PHE A 364 0
SHEET 2 I 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 I 4 ARG A 382 GLN A 388 -1 O PHE A 387 N PHE A 371
SHEET 4 I 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 J 4 VAL A 404 LEU A 410 0
SHEET 2 J 4 TYR A 414 SER A 419 -1 O TYR A 416 N ALA A 409
SHEET 3 J 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 J 4 ASP A 438 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 K 4 TYR A 457 PHE A 461 0
SHEET 2 K 4 TYR A 467 CYS A 472 -1 O ARG A 471 N SER A 458
SHEET 3 K 4 LEU A 479 SER A 484 -1 O LEU A 479 N CYS A 472
SHEET 4 K 4 LYS A 489 GLU A 495 -1 O LEU A 494 N TYR A 480
SHEET 1 L 8 SER A 511 ILE A 518 0
SHEET 2 L 8 LYS A 523 LEU A 530 -1 O LEU A 530 N SER A 511
SHEET 3 L 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 L 8 TYR A 540 ASP A 545 1 N ASP A 545 O ALA A 576
SHEET 5 L 8 VAL A 619 TRP A 629 1 O ASP A 620 N TYR A 540
SHEET 6 L 8 CYS A 649 VAL A 653 1 O VAL A 653 N GLY A 628
SHEET 7 L 8 GLU A 699 GLY A 705 1 O LEU A 701 N ALA A 652
SHEET 8 L 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 M 5 LYS B 400 PHE B 404 0
SHEET 2 M 5 SER B 440 SER B 447 -1 O LEU B 443 N LEU B 402
SHEET 3 M 5 GLN B 568 GLN B 576 -1 O GLY B 572 N ASP B 444
SHEET 4 M 5 THR B 477 THR B 483 -1 N ILE B 480 O PHE B 571
SHEET 5 M 5 SER B 419 SER B 426 -1 N SER B 426 O THR B 477
SHEET 1 N 2 CYS B 407 TYR B 409 0
SHEET 2 N 2 VAL B 584 PRO B 586 1 O CYS B 585 N TYR B 409
SHEET 1 O 4 GLU B 513 PRO B 515 0
SHEET 2 O 4 LYS B 496 LEU B 506 -1 N ARG B 505 O VAL B 514
SHEET 3 O 4 TRP B 553 ALA B 562 -1 O SER B 559 N TYR B 499
SHEET 4 O 4 TYR B 540 GLN B 544 -1 N TYR B 541 O ALA B 556
SSBOND 1 CYS A 328 CYS A 339 1555 1555 2.03
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.04
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.03
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.04
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.03
SSBOND 6 CYS B 383 CYS B 407 1555 1555 2.04
SSBOND 7 CYS B 425 CYS B 478 1555 1555 2.03
SSBOND 8 CYS B 437 CYS B 585 1555 1555 2.03
SSBOND 9 CYS B 503 CYS B 526 1555 1555 2.04
LINK O4 NAG A 806 C1 NAG A 807 1555 1555 1.43
LINK ND2 ASN A 229 C1 NAG A 806 1555 1555 1.43
LINK O4 NAG A 804 C1 NAG A 805 1555 1555 1.44
LINK ND2 ASN A 321 C1 NAG A 811 1555 1555 1.44
LINK O4 NAG A 809 C1 NAG A 810 1555 1555 1.44
LINK ND2 ASN A 85 C1 NAG A 801 1555 1555 1.44
LINK O4 NAG A 801 C1 NAG A 802 1555 1555 1.44
LINK O4 NAG A 807 C1 BMA A 808 1555 1555 1.44
LINK ND2 ASN A 150 C1 NAG A 803 1555 1555 1.44
LINK O4 NAG A 811 C1 NAG A 812 1555 1555 1.44
LINK ND2 ASN A 219 C1 NAG A 804 1555 1555 1.45
LINK ND2 ASN A 281 C1 NAG A 809 1555 1555 1.45
LINK ND2 ASN A 92 C1 NAG A 813 1555 1555 1.45
CISPEP 1 GLY A 474 PRO A 475 0 1.98
SITE 1 AC1 5 VAL A 78 TYR A 83 ASN A 85 SER A 86
SITE 2 AC1 5 SER A 87
SITE 1 AC2 5 GLU A 73 ASN A 74 ASN A 75 ASN A 92
SITE 2 AC2 5 HOH A 953
SITE 1 AC3 1 ASN A 150
SITE 1 AC4 6 ASN A 219 THR A 221 GLN A 308 GLU A 309
SITE 2 AC4 6 TYR A 330 GLU A 332
SITE 1 AC5 6 GLN A 227 ASN A 229 THR A 231 LYS A 267
SITE 2 AC5 6 TRP B 535 GLU B 536
SITE 1 AC6 5 TRP A 187 VAL A 279 ASN A 281 HOH A 901
SITE 2 AC6 5 HOH A1041
SITE 1 AC7 4 ILE A 319 ASN A 321 SER A 349 ARG A 596
CRYST1 110.224 110.224 527.599 90.00 90.00 120.00 P 61 2 2 12
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 0.009072 0.005238 0.000000 0.00000
SCALE2 0.000000 0.010476 0.000000 0.00000
SCALE3 0.000000 0.000000 0.001895 0.00000
TER 5964 PRO A 766
TER 7573 LEU B 588
MASTER 442 0 13 25 60 0 12 6 7944 2 204 77
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