HEADER BLOOD CLOTTING 13-NOV-18 6I58
TITLE ALLOSTERIC ACTIVATION OF HUMAN PREKALLIKREIN BY APPLE DOMAIN DISC
TITLE 2 ROTATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COAGULATION FACTOR XI;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FXI,PLASMA THROMBOPLASTIN ANTECEDENT,PTA;
COMPND 5 EC: 3.4.21.27
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS PREKALLIKREIN, ACTIVATION, HIGH MOLECULAR WEIGHT KININOGEN, FACTOR
KEYWDS 2 XI, BLOOD CLOTTING
EXPDTA X-RAY DIFFRACTION
AUTHOR C.LI,M.PATHAK,K.MCCRAE,I.DREVENY,J.EMSLEY
REVDAT 4 24-JAN-24 6I58 1 REMARK HETSYN
REVDAT 3 29-JUL-20 6I58 1 COMPND REMARK HETNAM SSBOND
REVDAT 3 2 1 LINK SITE ATOM
REVDAT 2 08-MAY-19 6I58 1 JRNL
REVDAT 1 06-MAR-19 6I58 0
SPRSDE 06-MAR-19 6I58 2F83
JRNL AUTH C.LI,K.M.VOOS,M.PATHAK,G.HALL,K.R.MCCRAE,I.DREVENY,R.LI,
JRNL AUTH 2 J.EMSLEY
JRNL TITL PLASMA KALLIKREIN STRUCTURE REVEALS APPLE DOMAIN DISC
JRNL TITL 2 ROTATED CONFORMATION COMPARED TO FACTOR XI.
JRNL REF J.THROMB.HAEMOST. V. 17 759 2019
JRNL REFN ESSN 1538-7836
JRNL PMID 30801944
JRNL DOI 10.1111/JTH.14418
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.PAPAGRIGORIOU,P.A.MCEWAN,P.N.WALSH,J.EMSLEY
REMARK 1 TITL CRYSTAL STRUCTURE OF THE FACTOR XI ZYMOGEN REVEALS A PATHWAY
REMARK 1 TITL 2 FOR TRANSACTIVATION.
REMARK 1 REF NAT. STRUCT. MOL. BIOL. V. 13 557 2006
REMARK 1 REFN ISSN 1545-9993
REMARK 1 PMID 16699514
REMARK 1 DOI 10.1038/NSMB1095
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 23605
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2641
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1596
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.3150
REMARK 3 BIN FREE R VALUE SET COUNT : 169
REMARK 3 BIN FREE R VALUE : 0.4160
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4599
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 68
REMARK 3 SOLVENT ATOMS : 83
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.09000
REMARK 3 B22 (A**2) : -0.09000
REMARK 3 B33 (A**2) : 0.19000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.570
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.340
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.267
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.797
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4768 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4249 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6477 ; 1.770 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9884 ; 1.073 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 585 ; 7.557 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 200 ;35.145 ;23.900
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 774 ;19.385 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;20.180 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 729 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5236 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 972 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2347 ; 5.452 ; 7.240
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2346 ; 5.445 ; 7.239
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2926 ; 8.165 ;10.844
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2927 ; 8.164 ;10.846
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2420 ; 5.178 ; 7.711
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2420 ; 5.178 ; 7.711
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3551 ; 8.028 ;11.366
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5169 ;11.379 ;84.367
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5170 ;11.378 ;84.367
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6I58 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1200012843.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-SEP-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9334
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23616
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 39.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 8.800
REMARK 200 R MERGE (I) : 0.08750
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.67
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 0.60200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
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: 2F83
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM HEPES AND 22% (V/V) PEG
REMARK 280 1000, PH 7.5, EVAPORATION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 125.53000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 40.38000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 40.38000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 188.29500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 40.38000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 40.38000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 62.76500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 40.38000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 40.38000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 188.29500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 40.38000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 40.38000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 62.76500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 125.53000
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: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -76.0 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 0.000000 1.000000 0.000000 -80.76000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 80.76000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLU A 1
REMARK 465 GLN A 318
REMARK 465 ALA A 319
REMARK 465 SER A 320
REMARK 465 ARG A 504
REMARK 465 LYS A 505
REMARK 465 LEU A 506
REMARK 465 ARG A 507
REMARK 465 ARG A 546
REMARK 465 GLU A 547
REMARK 465 GLY A 548
REMARK 465 GLY A 549
REMARK 465 LYS A 550
REMARK 465 ASP A 551
REMARK 465 ALA A 552
REMARK 465 CYS A 553
REMARK 465 CYS A 581
REMARK 465 ALA A 582
REMARK 465 GLN A 583
REMARK 465 ARG A 584
REMARK 465 ALA A 606
REMARK 465 VAL A 607
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 8 CG CD CE
REMARK 480 LYS A 113 CG CD CE NZ
REMARK 480 LYS A 230 CG CD CE NZ
REMARK 480 LYS A 252 CD CE NZ
REMARK 480 LYS A 255 NZ
REMARK 480 LYS A 301 CE
REMARK 480 ARG A 479 CG CD NE CZ NH1 NH2
REMARK 480 GLN A 515 CG
REMARK 480 LYS A 529 CB CG CD CE NZ
REMARK 480 ARG A 530 CZ NH1 NH2
REMARK 480 LYS A 535 CD CE NZ
REMARK 480 ARG A 586 CD NE
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 90 -62.52 -97.34
REMARK 500 ALA A 91 -8.37 81.37
REMARK 500 ARG A 144 131.12 -33.88
REMARK 500 ASP A 194 -153.23 -127.15
REMARK 500 LYS A 253 138.43 -179.47
REMARK 500 VAL A 271 -49.00 -142.96
REMARK 500 ASN A 322 -134.11 48.97
REMARK 500 LYS A 325 71.49 -156.05
REMARK 500 VAL A 371 109.03 -58.04
REMARK 500 SER A 434 -35.64 -38.80
REMARK 500 LYS A 455 -62.19 -122.91
REMARK 500 ALA A 517 116.31 -162.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 391 PRO A 392 -65.56
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 A 883 DISTANCE = 6.34 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6I44 RELATED DB: PDB
REMARK 900 RELATED ID: 6I4W RELATED DB: PDB
DBREF 6I58 A 1 607 UNP P03951 FA11_HUMAN 19 625
SEQRES 1 A 607 GLU CYS VAL THR GLN LEU LEU LYS ASP THR CYS PHE GLU
SEQRES 2 A 607 GLY GLY ASP ILE THR THR VAL PHE THR PRO SER ALA LYS
SEQRES 3 A 607 TYR CYS GLN VAL VAL CYS THR TYR HIS PRO ARG CYS LEU
SEQRES 4 A 607 LEU PHE THR PHE THR ALA GLU SER PRO SER GLU ASP PRO
SEQRES 5 A 607 THR ARG TRP PHE THR CYS VAL LEU LYS ASP SER VAL THR
SEQRES 6 A 607 GLU THR LEU PRO ARG VAL ASN ARG THR ALA ALA ILE SER
SEQRES 7 A 607 GLY TYR SER PHE LYS GLN CYS SER HIS GLN ILE SER ALA
SEQRES 8 A 607 CYS ASN LYS ASP ILE TYR VAL ASP LEU ASP MET LYS GLY
SEQRES 9 A 607 ILE ASN TYR ASN SER SER VAL ALA LYS SER ALA GLN GLU
SEQRES 10 A 607 CYS GLN GLU ARG CYS THR ASP ASP VAL HIS CYS HIS PHE
SEQRES 11 A 607 PHE THR TYR ALA THR ARG GLN PHE PRO SER LEU GLU HIS
SEQRES 12 A 607 ARG ASN ILE CYS LEU LEU LYS HIS THR GLN THR GLY THR
SEQRES 13 A 607 PRO THR ARG ILE THR LYS LEU ASP LYS VAL VAL SER GLY
SEQRES 14 A 607 PHE SER LEU LYS SER CYS ALA LEU SER ASN LEU ALA CYS
SEQRES 15 A 607 ILE ARG ASP ILE PHE PRO ASN THR VAL PHE ALA ASP SER
SEQRES 16 A 607 ASN ILE ASP SER VAL MET ALA PRO ASP ALA PHE VAL CYS
SEQRES 17 A 607 GLY ARG ILE CYS THR HIS HIS PRO GLY CYS LEU PHE PHE
SEQRES 18 A 607 THR PHE PHE SER GLN GLU TRP PRO LYS GLU SER GLN ARG
SEQRES 19 A 607 ASN LEU CYS LEU LEU LYS THR SER GLU SER GLY LEU PRO
SEQRES 20 A 607 SER THR ARG ILE LYS LYS SER LYS ALA LEU SER GLY PHE
SEQRES 21 A 607 SER LEU GLN SER CYS ARG HIS SER ILE PRO VAL PHE CYS
SEQRES 22 A 607 HIS SER SER PHE TYR HIS ASP THR ASP PHE LEU GLY GLU
SEQRES 23 A 607 GLU LEU ASP ILE VAL ALA ALA LYS SER HIS GLU ALA CYS
SEQRES 24 A 607 GLN LYS LEU CYS THR ASN ALA VAL ARG CYS GLN PHE PHE
SEQRES 25 A 607 THR TYR THR PRO ALA GLN ALA SER CYS ASN GLU GLY LYS
SEQRES 26 A 607 GLY LYS CYS TYR LEU LYS LEU SER SER ASN GLY SER PRO
SEQRES 27 A 607 THR LYS ILE LEU HIS GLY ARG GLY GLY ILE SER GLY TYR
SEQRES 28 A 607 THR LEU ARG LEU CYS LYS MET ASP ASN GLU CYS THR THR
SEQRES 29 A 607 LYS ILE LYS PRO ARG ILE VAL GLY GLY THR ALA SER VAL
SEQRES 30 A 607 ARG GLY GLU TRP PRO TRP GLN VAL THR LEU HIS THR THR
SEQRES 31 A 607 SER PRO THR GLN ARG HIS LEU CYS GLY GLY SER ILE ILE
SEQRES 32 A 607 GLY ASN GLN TRP ILE LEU THR ALA ALA HIS CYS PHE TYR
SEQRES 33 A 607 GLY VAL GLU SER PRO LYS ILE LEU ARG VAL TYR SER GLY
SEQRES 34 A 607 ILE LEU ASN GLN SER GLU ILE LYS GLU ASP THR SER PHE
SEQRES 35 A 607 PHE GLY VAL GLN GLU ILE ILE ILE HIS ASP GLN TYR LYS
SEQRES 36 A 607 MET ALA GLU SER GLY TYR ASP ILE ALA LEU LEU LYS LEU
SEQRES 37 A 607 GLU THR THR VAL ASN TYR THR ASP SER GLN ARG PRO ILE
SEQRES 38 A 607 CYS LEU PRO SER LYS GLY ASP ARG ASN VAL ILE TYR THR
SEQRES 39 A 607 ASP CYS TRP VAL THR GLY TRP GLY TYR ARG LYS LEU ARG
SEQRES 40 A 607 ASP LYS ILE GLN ASN THR LEU GLN LYS ALA LYS ILE PRO
SEQRES 41 A 607 LEU VAL THR ASN GLU GLU CYS GLN LYS ARG TYR ARG GLY
SEQRES 42 A 607 HIS LYS ILE THR HIS LYS MET ILE CYS ALA GLY TYR ARG
SEQRES 43 A 607 GLU GLY GLY LYS ASP ALA CYS LYS GLY ASP SER GLY GLY
SEQRES 44 A 607 PRO LEU SER CYS LYS HIS ASN GLU VAL TRP HIS LEU VAL
SEQRES 45 A 607 GLY ILE THR SER TRP GLY GLU GLY CYS ALA GLN ARG GLU
SEQRES 46 A 607 ARG PRO GLY VAL TYR THR ASN VAL VAL GLU TYR VAL ASP
SEQRES 47 A 607 TRP ILE LEU GLU LYS THR GLN ALA VAL
HET NAG B 1 14
HET NAG B 2 14
HET CL A 701 1
HET CL A 702 1
HET CL A 703 1
HET CL A 704 1
HET CL A 705 1
HET PEG A 706 7
HET NAG A 707 14
HET NAG A 708 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM CL CHLORIDE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 2 NAG 4(C8 H15 N O6)
FORMUL 3 CL 5(CL 1-)
FORMUL 8 PEG C4 H10 O3
FORMUL 11 HOH *83(H2 O)
HELIX 1 AA1 SER A 24 HIS A 35 1 12
HELIX 2 AA2 SER A 114 ASP A 124 1 11
HELIX 3 AA3 LEU A 172 ALA A 176 5 5
HELIX 4 AA4 ASP A 204 HIS A 215 1 12
HELIX 5 AA5 LYS A 230 ARG A 234 5 5
HELIX 6 AA6 CYS A 265 ILE A 269 5 5
HELIX 7 AA7 SER A 295 ASN A 305 1 11
HELIX 8 AA8 LEU A 355 ASP A 359 5 5
HELIX 9 AA9 ASN A 360 THR A 364 5 5
HELIX 10 AB1 ALA A 411 TYR A 416 5 6
HELIX 11 AB2 SER A 420 LYS A 422 5 3
HELIX 12 AB3 ASN A 432 ILE A 436 5 5
HELIX 13 AB4 SER A 485 ARG A 489 5 5
HELIX 14 AB5 THR A 523 LYS A 529 1 7
HELIX 15 AB6 TYR A 596 GLN A 605 1 10
SHEET 1 AA1 2 THR A 10 PHE A 12 0
SHEET 2 AA1 2 ARG A 70 ASN A 72 -1 O VAL A 71 N CYS A 11
SHEET 1 AA2 4 ASP A 16 PHE A 21 0
SHEET 2 AA2 4 THR A 57 LYS A 61 -1 O CYS A 58 N VAL A 20
SHEET 3 AA2 4 LEU A 40 THR A 44 -1 N LEU A 40 O LYS A 61
SHEET 4 AA2 4 ALA A 76 TYR A 80 -1 O ILE A 77 N PHE A 43
SHEET 1 AA3 5 ILE A 96 LYS A 103 0
SHEET 2 AA3 5 ARG A 159 PHE A 170 -1 O THR A 161 N ASP A 101
SHEET 3 AA3 5 PHE A 130 ALA A 134 -1 N TYR A 133 O VAL A 167
SHEET 4 AA3 5 ILE A 146 HIS A 151 -1 O ILE A 146 N ALA A 134
SHEET 5 AA3 5 ILE A 105 VAL A 111 -1 N SER A 110 O CYS A 147
SHEET 1 AA4 5 PHE A 187 VAL A 191 0
SHEET 2 AA4 5 ILE A 251 PHE A 260 -1 O SER A 258 N PHE A 187
SHEET 3 AA4 5 PHE A 220 PHE A 224 -1 N PHE A 223 O LEU A 257
SHEET 4 AA4 5 LEU A 236 THR A 241 -1 O LYS A 240 N PHE A 220
SHEET 5 AA4 5 SER A 195 MET A 201 -1 N VAL A 200 O CYS A 237
SHEET 1 AA5 5 TYR A 278 LEU A 284 0
SHEET 2 AA5 5 LYS A 340 TYR A 351 -1 O LEU A 342 N ASP A 282
SHEET 3 AA5 5 PHE A 311 THR A 315 -1 N TYR A 314 O ILE A 348
SHEET 4 AA5 5 GLY A 326 LEU A 332 -1 O LYS A 327 N THR A 315
SHEET 5 AA5 5 GLU A 286 ALA A 293 -1 N LEU A 288 O LEU A 330
SHEET 1 AA6 7 GLN A 384 THR A 389 0
SHEET 2 AA6 7 ARG A 395 ILE A 402 -1 O LEU A 397 N LEU A 387
SHEET 3 AA6 7 TRP A 407 THR A 410 -1 O LEU A 409 N SER A 401
SHEET 4 AA6 7 ALA A 464 LEU A 468 -1 O ALA A 464 N THR A 410
SHEET 5 AA6 7 PHE A 443 ILE A 450 -1 N GLN A 446 O LYS A 467
SHEET 6 AA6 7 LEU A 424 SER A 428 -1 N VAL A 426 O PHE A 443
SHEET 7 AA6 7 GLN A 384 THR A 389 -1 N HIS A 388 O ARG A 425
SHEET 1 AA7 7 GLN A 515 LYS A 518 0
SHEET 2 AA7 7 CYS A 496 GLY A 500 -1 N GLY A 500 O GLN A 515
SHEET 3 AA7 7 PRO A 560 HIS A 565 -1 O SER A 562 N TRP A 497
SHEET 4 AA7 7 VAL A 568 TRP A 577 -1 O GLY A 573 N LEU A 561
SHEET 5 AA7 7 GLY A 588 ASN A 592 -1 O THR A 591 N ILE A 574
SHEET 6 AA7 7 MET A 540 ALA A 543 -1 N ILE A 541 O TYR A 590
SHEET 7 AA7 7 LEU A 521 VAL A 522 -1 N VAL A 522 O CYS A 542
SSBOND 1 CYS A 2 CYS A 85 1555 1555 2.04
SSBOND 2 CYS A 28 CYS A 58 1555 1555 2.04
SSBOND 3 CYS A 32 CYS A 38 1555 1555 2.14
SSBOND 4 CYS A 92 CYS A 175 1555 1555 1.94
SSBOND 5 CYS A 118 CYS A 147 1555 1555 2.04
SSBOND 6 CYS A 122 CYS A 128 1555 1555 2.10
SSBOND 7 CYS A 182 CYS A 265 1555 1555 2.04
SSBOND 8 CYS A 208 CYS A 237 1555 1555 2.06
SSBOND 9 CYS A 212 CYS A 218 1555 1555 2.13
SSBOND 10 CYS A 273 CYS A 356 1555 1555 2.04
SSBOND 11 CYS A 299 CYS A 328 1555 1555 2.07
SSBOND 12 CYS A 303 CYS A 309 1555 1555 2.09
SSBOND 13 CYS A 321 CYS A 321 1555 7465 2.77
SSBOND 14 CYS A 362 CYS A 482 1555 1555 2.08
SSBOND 15 CYS A 398 CYS A 414 1555 1555 2.02
SSBOND 16 CYS A 496 CYS A 563 1555 1555 2.09
SSBOND 17 CYS A 527 CYS A 542 1555 1555 2.07
LINK ND2 ASN A 72 C1 NAG A 707 1555 1555 1.46
LINK ND2 ASN A 108 C1 NAG B 1 1555 1555 1.46
LINK ND2 ASN A 432 C1 NAG A 708 1555 1555 1.42
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.43
CRYST1 80.760 80.760 251.060 90.00 90.00 90.00 P 43 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012382 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012382 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003983 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
