HEADER PROTEIN BINDING 12-NOV-18 6I4V
TITLE ALPHA-1-ANTITRYPSIN QUEEN'S (K154N) VARIANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-1-ANTITRYPSIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALPHA-1 PROTEASE INHIBITOR,ALPHA-1-ANTIPROTEINASE,SERPIN A1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SERPINA1, AAT, PI, PRO0684, PRO2209;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: K12;
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: XL-1 BLUE;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS ANTITRYPSIN, PROTEASE INHIBITOR, SERPIN, MUTANT, DEFICIENCY, PROTEIN
KEYWDS 2 BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR I.ALDOBIYAN,D.A.LOMAS,J.A.IRVING
REVDAT 2 24-JAN-24 6I4V 1 REMARK
REVDAT 1 20-NOV-19 6I4V 0
JRNL AUTH I.ALDOBIYAN,J.A.IRVING,D.A.LOMAS
JRNL TITL STRUCTURAL DETERMINANTS OF INSTABILITY IN
JRNL TITL 2 ALPHA-1-ANTITRYPSIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.78 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13-2998
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) : 1.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 37224
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 1904
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 43.6131 - 4.2888 0.99 2627 133 0.1623 0.1853
REMARK 3 2 4.2888 - 3.4046 1.00 2562 141 0.1560 0.1483
REMARK 3 3 3.4046 - 2.9743 1.00 2536 138 0.1856 0.2177
REMARK 3 4 2.9743 - 2.7024 1.00 2560 126 0.1943 0.2754
REMARK 3 5 2.7024 - 2.5087 1.00 2534 110 0.1974 0.2215
REMARK 3 6 2.5087 - 2.3608 1.00 2533 143 0.1934 0.2376
REMARK 3 7 2.3608 - 2.2426 1.00 2471 147 0.1927 0.2653
REMARK 3 8 2.2426 - 2.1450 1.00 2521 137 0.2015 0.2765
REMARK 3 9 2.1450 - 2.0624 1.00 2521 139 0.2059 0.2577
REMARK 3 10 2.0624 - 1.9912 1.00 2522 118 0.2122 0.2557
REMARK 3 11 1.9912 - 1.9290 1.00 2476 164 0.2312 0.2615
REMARK 3 12 1.9290 - 1.8738 1.00 2473 159 0.2596 0.2863
REMARK 3 13 1.8738 - 1.8245 1.00 2511 118 0.2836 0.2989
REMARK 3 14 1.8245 - 1.7800 1.00 2473 131 0.3290 0.3728
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.680
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.03
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.04
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 24 THROUGH 174 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4390 0.3265 16.6960
REMARK 3 T TENSOR
REMARK 3 T11: 0.2652 T22: 0.3189
REMARK 3 T33: 0.2723 T12: 0.0592
REMARK 3 T13: 0.0025 T23: -0.0563
REMARK 3 L TENSOR
REMARK 3 L11: 4.4559 L22: 2.0111
REMARK 3 L33: 1.9590 L12: -0.5526
REMARK 3 L13: -0.4477 L23: -0.1064
REMARK 3 S TENSOR
REMARK 3 S11: -0.1183 S12: -0.0919 S13: 0.2988
REMARK 3 S21: 0.2223 S22: 0.1758 S23: -0.1449
REMARK 3 S31: -0.0386 S32: 0.3322 S33: -0.0773
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 175 THROUGH 394 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7746 -0.3269 27.5222
REMARK 3 T TENSOR
REMARK 3 T11: 0.3074 T22: 0.1921
REMARK 3 T33: 0.2704 T12: 0.0600
REMARK 3 T13: 0.0051 T23: 0.0313
REMARK 3 L TENSOR
REMARK 3 L11: 3.0972 L22: 1.1205
REMARK 3 L33: 2.6601 L12: -0.7512
REMARK 3 L13: -1.8538 L23: 1.0333
REMARK 3 S TENSOR
REMARK 3 S11: -0.0349 S12: -0.0743 S13: 0.0820
REMARK 3 S21: 0.1525 S22: 0.0979 S23: 0.0332
REMARK 3 S31: 0.1516 S32: 0.1747 S33: -0.0810
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): 7.6994 -19.2325 35.9632
REMARK 3 T TENSOR
REMARK 3 T11: 1.2625 T22: 1.0776
REMARK 3 T33: 1.2017 T12: 0.1579
REMARK 3 T13: -0.1672 T23: 0.1111
REMARK 3 L TENSOR
REMARK 3 L11: 3.5010 L22: 6.1392
REMARK 3 L33: 4.4238 L12: 1.3347
REMARK 3 L13: 0.5236 L23: -4.7468
REMARK 3 S TENSOR
REMARK 3 S11: -0.1353 S12: 0.6406 S13: -0.7426
REMARK 3 S21: 0.1431 S22: 0.0476 S23: -0.4005
REMARK 3 S31: -0.1489 S32: -0.1359 S33: 0.0885
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 6I4V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1200012823.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JUL-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.75
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97925
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : KIRKPATRICK BAEZ BIMORPH MIRROR
REMARK 200 PAIR
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS JAN 26, 2018
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.6.2, XIA2 0.5.580
REMARK 200 -G8B4A78DF-DIALS-1.10
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37234
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.780
REMARK 200 RESOLUTION RANGE LOW (A) : 52.990
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 1.33200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.8.1
REMARK 200 STARTING MODEL: 1QLP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 1500, 0.1M SPG (SUCCINATE
REMARK 280 -PHOSPHATE-GLYCINE), 0.5MM DSS (4,4-DIMETHYL-4-SILAPENTANE-1-
REMARK 280 SULFONIC ACID), PH 5.75, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 57.23000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 19.47500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 57.23000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 19.47500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 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 MET A -9
REMARK 465 ARG A -8
REMARK 465 GLY A -7
REMARK 465 SER A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 THR A 1
REMARK 465 ASP A 2
REMARK 465 PRO A 3
REMARK 465 GLN A 4
REMARK 465 GLY A 5
REMARK 465 ASP A 6
REMARK 465 ALA A 7
REMARK 465 ALA A 8
REMARK 465 GLN A 9
REMARK 465 LYS A 10
REMARK 465 THR A 11
REMARK 465 ASP A 12
REMARK 465 THR A 13
REMARK 465 SER A 14
REMARK 465 HIS A 15
REMARK 465 HIS A 16
REMARK 465 ASP A 17
REMARK 465 GLN A 18
REMARK 465 ASP A 19
REMARK 465 HIS A 20
REMARK 465 PRO A 21
REMARK 465 THR A 22
REMARK 465 PHE A 23
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 25 CD CE NZ
REMARK 470 HIS A 43 CG ND1 CD2 CE1 NE2
REMARK 470 ASN A 46 CG OD1 ND2
REMARK 470 SER A 47 OG
REMARK 470 GLU A 86 CD OE1 OE2
REMARK 470 GLU A 94 CD OE1 OE2
REMARK 470 GLN A 97 OE1 NE2
REMARK 470 GLU A 98 CG CD OE1 OE2
REMARK 470 ARG A 101 NE CZ NH1 NH2
REMARK 470 GLN A 105 CG CD OE1 NE2
REMARK 470 ASP A 107 CG OD1 OD2
REMARK 470 GLN A 111 CG CD OE1 NE2
REMARK 470 LYS A 125 CD CE NZ
REMARK 470 GLU A 132 CG CD OE1 OE2
REMARK 470 LYS A 135 CG CD CE NZ
REMARK 470 LYS A 136 CG CD CE NZ
REMARK 470 GLU A 151 CD OE1 OE2
REMARK 470 GLU A 162 CD OE1 OE2
REMARK 470 LYS A 163 CE NZ
REMARK 470 LYS A 168 CG CD CE NZ
REMARK 470 ASP A 171 CG OD1 OD2
REMARK 470 LYS A 174 CG CD CE NZ
REMARK 470 GLU A 175 CG CD OE1 OE2
REMARK 470 ARG A 178 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 179 CG OD1 OD2
REMARK 470 GLU A 199 CD OE1 OE2
REMARK 470 LYS A 201 CE NZ
REMARK 470 GLU A 204 CD OE1 OE2
REMARK 470 LYS A 233 CG CD CE NZ
REMARK 470 LYS A 234 CE NZ
REMARK 470 GLU A 257 CG CD OE1 OE2
REMARK 470 LYS A 274 CG CD CE NZ
REMARK 470 GLU A 277 CD OE1 OE2
REMARK 470 GLU A 279 CD OE1 OE2
REMARK 470 LYS A 310 CE NZ
REMARK 470 GLU A 324 CG CD OE1 OE2
REMARK 470 LYS A 343 CE NZ
REMARK 470 GLU A 346 CG CD OE1 OE2
REMARK 470 LYS A 380 CE NZ
REMARK 470 LYS A 394 CG CD CE NZ
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 ALA A 70 -133.37 52.45
REMARK 500 ASN A 81 33.95 73.54
REMARK 500 ASN A 247 56.93 -109.73
REMARK 500 LYS A 343 -30.89 -133.84
REMARK 500 ASN A 390 108.14 -164.41
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 residue GLY A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H3B A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GLY A 403
DBREF 6I4V A 2 394 UNP P01009 A1AT_HUMAN 26 418
SEQADV 6I4V MET A -9 UNP P01009 INITIATING METHIONINE
SEQADV 6I4V ARG A -8 UNP P01009 EXPRESSION TAG
SEQADV 6I4V GLY A -7 UNP P01009 EXPRESSION TAG
SEQADV 6I4V SER A -6 UNP P01009 EXPRESSION TAG
SEQADV 6I4V HIS A -5 UNP P01009 EXPRESSION TAG
SEQADV 6I4V HIS A -4 UNP P01009 EXPRESSION TAG
SEQADV 6I4V HIS A -3 UNP P01009 EXPRESSION TAG
SEQADV 6I4V HIS A -2 UNP P01009 EXPRESSION TAG
SEQADV 6I4V HIS A -1 UNP P01009 EXPRESSION TAG
SEQADV 6I4V HIS A 0 UNP P01009 EXPRESSION TAG
SEQADV 6I4V THR A 1 UNP P01009 EXPRESSION TAG
SEQADV 6I4V ASN A 154 UNP P01009 LYS 178 ENGINEERED MUTATION
SEQADV 6I4V SER A 232 UNP P01009 CYS 256 ENGINEERED MUTATION
SEQRES 1 A 404 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP PRO
SEQRES 2 A 404 GLN GLY ASP ALA ALA GLN LYS THR ASP THR SER HIS HIS
SEQRES 3 A 404 ASP GLN ASP HIS PRO THR PHE ASN LYS ILE THR PRO ASN
SEQRES 4 A 404 LEU ALA GLU PHE ALA PHE SER LEU TYR ARG GLN LEU ALA
SEQRES 5 A 404 HIS GLN SER ASN SER THR ASN ILE PHE PHE SER PRO VAL
SEQRES 6 A 404 SER ILE ALA THR ALA PHE ALA MET LEU SER LEU GLY THR
SEQRES 7 A 404 LYS ALA ASP THR HIS ASP GLU ILE LEU GLU GLY LEU ASN
SEQRES 8 A 404 PHE ASN LEU THR GLU ILE PRO GLU ALA GLN ILE HIS GLU
SEQRES 9 A 404 GLY PHE GLN GLU LEU LEU ARG THR LEU ASN GLN PRO ASP
SEQRES 10 A 404 SER GLN LEU GLN LEU THR THR GLY ASN GLY LEU PHE LEU
SEQRES 11 A 404 SER GLU GLY LEU LYS LEU VAL ASP LYS PHE LEU GLU ASP
SEQRES 12 A 404 VAL LYS LYS LEU TYR HIS SER GLU ALA PHE THR VAL ASN
SEQRES 13 A 404 PHE GLY ASP THR GLU GLU ALA ASN LYS GLN ILE ASN ASP
SEQRES 14 A 404 TYR VAL GLU LYS GLY THR GLN GLY LYS ILE VAL ASP LEU
SEQRES 15 A 404 VAL LYS GLU LEU ASP ARG ASP THR VAL PHE ALA LEU VAL
SEQRES 16 A 404 ASN TYR ILE PHE PHE LYS GLY LYS TRP GLU ARG PRO PHE
SEQRES 17 A 404 GLU VAL LYS ASP THR GLU GLU GLU ASP PHE HIS VAL ASP
SEQRES 18 A 404 GLN VAL THR THR VAL LYS VAL PRO MET MET LYS ARG LEU
SEQRES 19 A 404 GLY MET PHE ASN ILE GLN HIS SER LYS LYS LEU SER SER
SEQRES 20 A 404 TRP VAL LEU LEU MET LYS TYR LEU GLY ASN ALA THR ALA
SEQRES 21 A 404 ILE PHE PHE LEU PRO ASP GLU GLY LYS LEU GLN HIS LEU
SEQRES 22 A 404 GLU ASN GLU LEU THR HIS ASP ILE ILE THR LYS PHE LEU
SEQRES 23 A 404 GLU ASN GLU ASP ARG ARG SER ALA SER LEU HIS LEU PRO
SEQRES 24 A 404 LYS LEU SER ILE THR GLY THR TYR ASP LEU LYS SER VAL
SEQRES 25 A 404 LEU GLY GLN LEU GLY ILE THR LYS VAL PHE SER ASN GLY
SEQRES 26 A 404 ALA ASP LEU SER GLY VAL THR GLU GLU ALA PRO LEU LYS
SEQRES 27 A 404 LEU SER LYS ALA VAL HIS LYS ALA VAL LEU THR ILE ASP
SEQRES 28 A 404 GLU LYS GLY THR GLU ALA ALA GLY ALA MET PHE LEU GLU
SEQRES 29 A 404 ALA ILE PRO MET SER ILE PRO PRO GLU VAL LYS PHE ASN
SEQRES 30 A 404 LYS PRO PHE VAL PHE LEU MET ILE GLU GLN ASN THR LYS
SEQRES 31 A 404 SER PRO LEU PHE MET GLY LYS VAL VAL ASN PRO THR GLN
SEQRES 32 A 404 LYS
HET GLY A 401 10
HET H3B A 402 11
HET GLY A 403 7
HETNAM GLY GLYCINE
HETNAM H3B 3-TRIMETHYLSILYLPROPANE-1-SULFONIC ACID
FORMUL 2 GLY 2(C2 H5 N O2)
FORMUL 3 H3B C6 H16 O3 S SI
FORMUL 5 HOH *195(H2 O)
HELIX 1 AA1 ILE A 26 SER A 45 1 20
HELIX 2 AA2 SER A 53 LEU A 66 1 14
HELIX 3 AA3 LYS A 69 LEU A 80 1 12
HELIX 4 AA4 PRO A 88 ASN A 104 1 17
HELIX 5 AA5 VAL A 127 LEU A 137 1 11
HELIX 6 AA6 ASP A 149 THR A 165 1 17
HELIX 7 AA7 GLU A 199 THR A 203 5 5
HELIX 8 AA8 LYS A 259 LEU A 267 1 9
HELIX 9 AA9 THR A 268 ASN A 278 1 11
HELIX 10 AB1 LEU A 299 LEU A 306 1 8
HELIX 11 AB2 THR A 309 SER A 313 5 5
SHEET 1 AA1 7 ILE A 50 PHE A 52 0
SHEET 2 AA1 7 PRO A 382 VAL A 388 -1 O LYS A 387 N ILE A 50
SHEET 3 AA1 7 PHE A 370 GLU A 376 -1 N PHE A 372 O GLY A 386
SHEET 4 AA1 7 ALA A 248 PRO A 255 -1 N ILE A 251 O LEU A 373
SHEET 5 AA1 7 SER A 237 TYR A 244 -1 N MET A 242 O ALA A 250
SHEET 6 AA1 7 THR A 214 SER A 232 -1 N SER A 232 O SER A 237
SHEET 7 AA1 7 GLU A 204 ASP A 211 -1 N PHE A 208 O VAL A 216
SHEET 1 AA2 8 ILE A 50 PHE A 52 0
SHEET 2 AA2 8 PRO A 382 VAL A 388 -1 O LYS A 387 N ILE A 50
SHEET 3 AA2 8 PHE A 370 GLU A 376 -1 N PHE A 372 O GLY A 386
SHEET 4 AA2 8 ALA A 248 PRO A 255 -1 N ILE A 251 O LEU A 373
SHEET 5 AA2 8 SER A 237 TYR A 244 -1 N MET A 242 O ALA A 250
SHEET 6 AA2 8 THR A 214 SER A 232 -1 N SER A 232 O SER A 237
SHEET 7 AA2 8 ARG A 282 PRO A 289 -1 O ARG A 282 N PHE A 227
SHEET 8 AA2 8 GLU A 363 LYS A 365 1 O VAL A 364 N HIS A 287
SHEET 1 AA3 5 GLU A 141 VAL A 145 0
SHEET 2 AA3 5 LEU A 112 SER A 121 1 N LEU A 118 O PHE A 143
SHEET 3 AA3 5 PHE A 182 LYS A 191 -1 O PHE A 189 N THR A 113
SHEET 4 AA3 5 LYS A 331 ILE A 340 1 O VAL A 333 N ASN A 186
SHEET 5 AA3 5 LEU A 291 ASP A 298 -1 N ILE A 293 O LEU A 338
SITE 1 AC1 8 GLY A 148 GLN A 230 SER A 232 LYS A 233
SITE 2 AC1 8 LYS A 234 PHE A 275 HOH A 502 HOH A 619
SITE 1 AC2 7 GLN A 109 ARG A 196 LEU A 245 ALA A 350
SITE 2 AC2 7 PHE A 352 GLN A 393 LYS A 394
SITE 1 AC3 3 LYS A 365 ASN A 367 HOH A 558
CRYST1 114.460 38.950 89.850 90.00 103.95 90.00 C 1 2 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 0.008737 0.000000 0.002170 0.00000
SCALE2 0.000000 0.025674 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011468 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
