Header list of 2bpr.pdb file
Complete list - r 9 2 Bytes
HEADER MOLECULAR CHAPERONE 11-AUG-98 2BPR
TITLE NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, 25 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNAK;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SUBSTRATE BINDING DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: XL-1 BLUE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS MOLECULAR CHAPERONE, HSP70, PEPTIDE BINDING, PROTEIN FOLDING
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR H.WANG,A.V.KUROCHKIN,Y.PANG,W.HU,G.C.FLYNN,E.R.P.ZUIDERWEG
REVDAT 4 09-MAR-22 2BPR 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2BPR 1 VERSN
REVDAT 2 27-APR-99 2BPR 1 COMPND REMARK TITLE SOURCE
REVDAT 2 2 1 JRNL
REVDAT 1 02-MAR-99 2BPR 0
JRNL AUTH H.WANG,A.V.KUROCHKIN,Y.PANG,W.HU,G.C.FLYNN,E.R.ZUIDERWEG
JRNL TITL NMR SOLUTION STRUCTURE OF THE 21 KDA CHAPERONE PROTEIN DNAK
JRNL TITL 2 SUBSTRATE BINDING DOMAIN: A PREVIEW OF CHAPERONE-PROTEIN
JRNL TITL 3 INTERACTION.
JRNL REF BIOCHEMISTRY V. 37 7929 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9609686
JRNL DOI 10.1021/BI9800855
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISCOVER
REMARK 3 AUTHORS : MSI
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 REFERENCE CITED ABOVE
REMARK 4
REMARK 4 2BPR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177854.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 50 MM INORGANIC PHOSPHATE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : H2O AND D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA; HN(CA)HA; HN(CO)CA;
REMARK 210 HA(CACO)NH; CP H(C)CCH-TOCSY; CP
REMARK 210 (H)CCH-TOCSY; CP (H)C(CCACO)NH-
REMARK 210 TOCSY; 15N-RESOLVED NOESY-HSQC;
REMARK 210 13C RESOLVED NOESY-HMQC; 4D 13C
REMARK 210 RESOLVED HMQC-NOESY-HSQC; HNHA-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500; AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : BIOSYM
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND RESTRAINED
REMARK 210 MOLECULAR DYNAMICS WITH
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : TOTAL ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: MONOMERIC
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. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-25
REMARK 465 RES C SSSEQI
REMARK 465 ARG A 371
REMARK 465 GLY A 372
REMARK 465 SER A 373
REMARK 465 HIS A 374
REMARK 465 HIS A 375
REMARK 465 HIS A 376
REMARK 465 HIS A 377
REMARK 465 HIS A 378
REMARK 465 HIS A 379
REMARK 465 GLY A 380
REMARK 465 GLY A 554
REMARK 465 ASP A 555
REMARK 465 LYS A 556
REMARK 465 LEU A 557
REMARK 465 PRO A 558
REMARK 465 ALA A 559
REMARK 465 ASP A 560
REMARK 465 ASP A 561
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 HA VAL A 516 HB2 GLU A 520 1.22
REMARK 500 H LEU A 397 H SER A 398 1.25
REMARK 500 O ASP A 510 HB2 LYS A 514 1.32
REMARK 500 O GLN A 442 HB3 LYS A 452 1.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 16 HIS A 439 CG HIS A 439 CD2 0.064
REMARK 500 20 HIS A 439 CG HIS A 439 CD2 0.059
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 LEU A 411 N - CA - CB ANGL. DEV. = 12.6 DEGREES
REMARK 500 1 HIS A 422 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 1 ILE A 438 N - CA - C ANGL. DEV. = -17.6 DEGREES
REMARK 500 1 HIS A 439 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 1 ALA A 449 N - CA - CB ANGL. DEV. = 8.8 DEGREES
REMARK 500 1 LEU A 454 CB - CA - C ANGL. DEV. = 12.1 DEGREES
REMARK 500 1 GLN A 456 CB - CA - C ANGL. DEV. = 13.0 DEGREES
REMARK 500 1 HIS A 485 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 1 GLU A 511 N - CA - C ANGL. DEV. = -22.3 DEGREES
REMARK 500 1 VAL A 516 CA - CB - CG2 ANGL. DEV. = 11.5 DEGREES
REMARK 500 1 HIS A 541 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 1 HIS A 544 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 2 LEU A 411 N - CA - CB ANGL. DEV. = 14.4 DEGREES
REMARK 500 2 HIS A 422 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 2 ILE A 438 CB - CA - C ANGL. DEV. = 15.9 DEGREES
REMARK 500 2 ILE A 438 N - CA - C ANGL. DEV. = -22.0 DEGREES
REMARK 500 2 HIS A 439 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 2 VAL A 440 CA - CB - CG1 ANGL. DEV. = 9.5 DEGREES
REMARK 500 2 ALA A 449 N - CA - CB ANGL. DEV. = 9.1 DEGREES
REMARK 500 2 LEU A 454 CB - CA - C ANGL. DEV. = 17.8 DEGREES
REMARK 500 2 GLN A 456 CB - CA - C ANGL. DEV. = 12.1 DEGREES
REMARK 500 2 HIS A 485 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 2 HIS A 541 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 2 HIS A 544 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 3 LEU A 411 N - CA - CB ANGL. DEV. = 14.1 DEGREES
REMARK 500 3 HIS A 422 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 3 HIS A 439 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 3 ALA A 449 N - CA - CB ANGL. DEV. = 8.5 DEGREES
REMARK 500 3 HIS A 485 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 3 GLU A 511 N - CA - C ANGL. DEV. = -23.1 DEGREES
REMARK 500 3 GLU A 520 N - CA - CB ANGL. DEV. = 14.7 DEGREES
REMARK 500 3 HIS A 541 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 3 HIS A 544 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 4 LEU A 411 N - CA - CB ANGL. DEV. = 12.2 DEGREES
REMARK 500 4 HIS A 422 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 4 SER A 434 N - CA - CB ANGL. DEV. = -20.2 DEGREES
REMARK 500 4 HIS A 439 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 4 VAL A 440 CG1 - CB - CG2 ANGL. DEV. = -10.1 DEGREES
REMARK 500 4 ALA A 449 N - CA - CB ANGL. DEV. = 10.4 DEGREES
REMARK 500 4 LEU A 454 CB - CA - C ANGL. DEV. = 19.8 DEGREES
REMARK 500 4 HIS A 485 ND1 - CE1 - NE2 ANGL. DEV. = 9.0 DEGREES
REMARK 500 4 GLU A 511 N - CA - C ANGL. DEV. = -23.4 DEGREES
REMARK 500 4 HIS A 541 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 4 HIS A 544 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 5 SER A 398 N - CA - CB ANGL. DEV. = 9.1 DEGREES
REMARK 500 5 LEU A 411 N - CA - CB ANGL. DEV. = 13.8 DEGREES
REMARK 500 5 HIS A 422 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 5 HIS A 439 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 5 VAL A 440 CB - CA - C ANGL. DEV. = 12.7 DEGREES
REMARK 500 5 ALA A 449 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 262 ANGLE DEVIATIONS.
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 1 ARG A 385 -36.92 -160.06
REMARK 500 1 ASP A 388 91.89 -166.48
REMARK 500 1 LEU A 390 -48.69 -140.94
REMARK 500 1 LEU A 397 -8.44 -163.45
REMARK 500 1 SER A 398 136.64 88.42
REMARK 500 1 LEU A 399 111.59 -164.69
REMARK 500 1 ASN A 415 18.47 82.80
REMARK 500 1 LYS A 421 119.80 -160.26
REMARK 500 1 GLN A 433 97.72 -163.62
REMARK 500 1 SER A 434 -29.76 -153.98
REMARK 500 1 GLU A 444 -70.98 -134.12
REMARK 500 1 ARG A 445 176.79 -59.01
REMARK 500 1 ASN A 451 58.10 -105.96
REMARK 500 1 GLN A 456 -137.85 -143.81
REMARK 500 1 PHE A 457 -130.98 -137.39
REMARK 500 1 ILE A 462 59.44 -108.73
REMARK 500 1 ASN A 463 140.64 66.73
REMARK 500 1 ARG A 467 123.75 28.95
REMARK 500 1 MET A 469 -66.11 -143.53
REMARK 500 1 PRO A 470 69.80 -115.00
REMARK 500 1 LYS A 491 48.41 -95.89
REMARK 500 1 SER A 493 14.04 -153.69
REMARK 500 1 ALA A 503 94.29 -161.05
REMARK 500 1 LEU A 507 151.10 66.49
REMARK 500 1 ARG A 517 -73.81 -72.24
REMARK 500 1 GLN A 534 33.35 90.63
REMARK 500 1 THR A 535 91.80 25.03
REMARK 500 1 ARG A 536 -23.15 -162.15
REMARK 500 1 ASN A 537 137.24 63.33
REMARK 500 1 GLN A 538 -83.69 -148.60
REMARK 500 1 HIS A 541 -79.97 70.95
REMARK 500 1 HIS A 544 75.12 57.92
REMARK 500 1 GLN A 549 76.15 60.69
REMARK 500 2 LEU A 390 -31.32 -154.95
REMARK 500 2 LEU A 397 -7.30 -162.45
REMARK 500 2 SER A 398 131.79 86.45
REMARK 500 2 LEU A 399 111.89 -161.40
REMARK 500 2 MET A 404 102.02 -51.18
REMARK 500 2 ASN A 415 10.69 85.67
REMARK 500 2 SER A 427 -166.63 -164.03
REMARK 500 2 ALA A 429 -18.57 -151.91
REMARK 500 2 ASN A 432 -63.36 -163.48
REMARK 500 2 SER A 434 6.59 -167.13
REMARK 500 2 ALA A 435 119.24 -165.66
REMARK 500 2 HIS A 439 58.19 -168.38
REMARK 500 2 GLU A 444 -60.53 -138.86
REMARK 500 2 ASP A 450 52.32 -117.26
REMARK 500 2 ASN A 451 52.35 -105.77
REMARK 500 2 GLN A 456 -134.23 -141.84
REMARK 500 2 PHE A 457 -137.37 -139.83
REMARK 500
REMARK 500 THIS ENTRY HAS 830 RAMACHANDRAN OUTLIERS.
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 THR A 395 PRO A 396 1 -147.25
REMARK 500 THR A 395 PRO A 396 2 -141.58
REMARK 500 THR A 395 PRO A 396 3 -148.03
REMARK 500 ALA A 465 PRO A 466 3 -127.05
REMARK 500 THR A 395 PRO A 396 4 -147.31
REMARK 500 THR A 395 PRO A 396 11 -145.24
REMARK 500 THR A 395 PRO A 396 12 -144.98
REMARK 500 MET A 469 PRO A 470 13 59.39
REMARK 500 ALA A 465 PRO A 466 14 -124.71
REMARK 500 ALA A 465 PRO A 466 15 -141.07
REMARK 500 THR A 395 PRO A 396 17 -147.79
REMARK 500 THR A 395 PRO A 396 18 -142.75
REMARK 500 THR A 395 PRO A 396 21 -140.02
REMARK 500 ALA A 465 PRO A 466 21 -143.75
REMARK 500 THR A 395 PRO A 396 22 -149.56
REMARK 500 THR A 395 PRO A 396 24 -144.56
REMARK 500 THR A 395 PRO A 396 25 -143.31
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2BPR A 380 561 UNP P0A6Y8 DNAK_ECOLI 379 560
SEQADV 2BPR SER A 381 UNP P0A6Y8 VAL 380 CONFLICT
SEQADV 2BPR ILE A 382 UNP P0A6Y8 LEU 381 CONFLICT
SEQADV 2BPR GLU A 383 UNP P0A6Y8 THR 382 CONFLICT
SEQADV 2BPR ARG A 385 UNP P0A6Y8 ASP 384 CONFLICT
SEQRES 1 A 191 ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ILE GLU
SEQRES 2 A 191 GLY ARG VAL LYS ASP VAL LEU LEU LEU ASP VAL THR PRO
SEQRES 3 A 191 LEU SER LEU GLY ILE GLU THR MET GLY GLY VAL MET THR
SEQRES 4 A 191 THR LEU ILE ALA LYS ASN THR THR ILE PRO THR LYS HIS
SEQRES 5 A 191 SER GLN VAL PHE SER THR ALA GLU ASP ASN GLN SER ALA
SEQRES 6 A 191 VAL THR ILE HIS VAL LEU GLN GLY GLU ARG LYS ARG ALA
SEQRES 7 A 191 ALA ASP ASN LYS SER LEU GLY GLN PHE ASN LEU ASP GLY
SEQRES 8 A 191 ILE ASN PRO ALA PRO ARG GLY MET PRO GLN ILE GLU VAL
SEQRES 9 A 191 THR PHE ASP ILE ASP ALA ASP GLY ILE LEU HIS VAL SER
SEQRES 10 A 191 ALA LYS ASP LYS ASN SER GLY LYS GLU GLN LYS ILE THR
SEQRES 11 A 191 ILE LYS ALA SER SER GLY LEU ASN GLU ASP GLU ILE GLN
SEQRES 12 A 191 LYS MET VAL ARG ASP ALA GLU ALA ASN ALA GLU ALA ASP
SEQRES 13 A 191 ARG LYS PHE GLU GLU LEU VAL GLN THR ARG ASN GLN GLY
SEQRES 14 A 191 ASP HIS LEU LEU HIS SER THR ARG LYS GLN VAL GLU GLU
SEQRES 15 A 191 ALA GLY ASP LYS LEU PRO ALA ASP ASP
HELIX 1 1 GLU A 509 LEU A 532 1 24
SHEET 1 A 2 ILE A 401 THR A 403 0
SHEET 2 A 2 VAL A 407 THR A 409 -1 N THR A 409 O ILE A 401
SHEET 1 B 4 THR A 420 PHE A 426 0
SHEET 2 B 4 ILE A 472 ILE A 478 -1 N ILE A 478 O THR A 420
SHEET 3 B 4 ILE A 483 ASP A 490 -1 N LYS A 489 O GLU A 473
SHEET 4 B 4 GLU A 496 LYS A 502 -1 N ILE A 501 O LEU A 484
SHEET 1 C 2 ALA A 435 ILE A 438 0
SHEET 2 C 2 PHE A 457 ASP A 460 -1 N LEU A 459 O VAL A 436
SHEET 1 D 2 VAL A 440 GLN A 442 0
SHEET 2 D 2 LYS A 452 LEU A 454 -1 N LEU A 454 O VAL A 440
CISPEP 1 ILE A 418 PRO A 419 1 8.70
CISPEP 2 MET A 469 PRO A 470 1 3.57
CISPEP 3 ILE A 418 PRO A 419 2 8.04
CISPEP 4 ALA A 465 PRO A 466 2 -7.60
CISPEP 5 MET A 469 PRO A 470 2 13.73
CISPEP 6 ILE A 418 PRO A 419 3 6.65
CISPEP 7 ILE A 418 PRO A 419 4 4.34
CISPEP 8 ASN A 463 PRO A 464 4 7.03
CISPEP 9 MET A 469 PRO A 470 4 1.39
CISPEP 10 ILE A 418 PRO A 419 5 7.11
CISPEP 11 MET A 469 PRO A 470 5 0.52
CISPEP 12 ILE A 418 PRO A 419 6 4.98
CISPEP 13 ASN A 463 PRO A 464 6 9.73
CISPEP 14 MET A 469 PRO A 470 6 8.85
CISPEP 15 ILE A 418 PRO A 419 7 8.71
CISPEP 16 ASN A 463 PRO A 464 7 8.61
CISPEP 17 MET A 469 PRO A 470 7 -0.95
CISPEP 18 ILE A 418 PRO A 419 8 5.14
CISPEP 19 ASN A 463 PRO A 464 8 1.18
CISPEP 20 MET A 469 PRO A 470 8 -0.84
CISPEP 21 ILE A 418 PRO A 419 9 5.93
CISPEP 22 ASN A 463 PRO A 464 9 9.01
CISPEP 23 MET A 469 PRO A 470 9 -0.99
CISPEP 24 ILE A 418 PRO A 419 10 5.31
CISPEP 25 ILE A 418 PRO A 419 11 8.58
CISPEP 26 MET A 469 PRO A 470 11 -3.68
CISPEP 27 ILE A 418 PRO A 419 12 9.09
CISPEP 28 ASN A 463 PRO A 464 12 -19.92
CISPEP 29 ALA A 465 PRO A 466 12 -16.03
CISPEP 30 MET A 469 PRO A 470 12 3.60
CISPEP 31 ILE A 418 PRO A 419 13 9.10
CISPEP 32 ASN A 463 PRO A 464 13 4.48
CISPEP 33 ILE A 418 PRO A 419 14 0.05
CISPEP 34 MET A 469 PRO A 470 14 6.83
CISPEP 35 ILE A 418 PRO A 419 15 5.82
CISPEP 36 ASN A 463 PRO A 464 15 3.72
CISPEP 37 MET A 469 PRO A 470 15 0.32
CISPEP 38 ILE A 418 PRO A 419 16 -0.76
CISPEP 39 ASN A 463 PRO A 464 16 -0.27
CISPEP 40 MET A 469 PRO A 470 16 11.43
CISPEP 41 ILE A 418 PRO A 419 17 7.83
CISPEP 42 ASN A 463 PRO A 464 17 -21.78
CISPEP 43 ALA A 465 PRO A 466 17 -8.95
CISPEP 44 ILE A 418 PRO A 419 18 7.40
CISPEP 45 ASN A 463 PRO A 464 18 0.87
CISPEP 46 MET A 469 PRO A 470 18 1.42
CISPEP 47 ILE A 418 PRO A 419 19 -0.67
CISPEP 48 ASN A 463 PRO A 464 19 10.33
CISPEP 49 MET A 469 PRO A 470 19 5.74
CISPEP 50 ILE A 418 PRO A 419 20 5.83
CISPEP 51 ASN A 463 PRO A 464 20 10.20
CISPEP 52 MET A 469 PRO A 470 20 13.30
CISPEP 53 ILE A 418 PRO A 419 21 10.12
CISPEP 54 ASN A 463 PRO A 464 21 -4.16
CISPEP 55 ILE A 418 PRO A 419 22 8.83
CISPEP 56 ASN A 463 PRO A 464 22 8.49
CISPEP 57 MET A 469 PRO A 470 22 3.11
CISPEP 58 ILE A 418 PRO A 419 23 5.40
CISPEP 59 MET A 469 PRO A 470 23 3.33
CISPEP 60 ILE A 418 PRO A 419 24 8.84
CISPEP 61 ALA A 465 PRO A 466 24 -9.74
CISPEP 62 MET A 469 PRO A 470 24 6.28
CISPEP 63 ILE A 418 PRO A 419 25 9.61
CISPEP 64 ASN A 463 PRO A 464 25 11.49
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 9 2 Bytes