| content |
HEADER HYDROLASE 20-JUL-16 5GNG
TITLE CRYSTAL STRUCTURE OF BIOG FROM HAEMOPHILUS INFLUENZAE AT 1.26
TITLE 2 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN HI_1552;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE (STRAIN ATCC 51907 / DSM
SOURCE 3 11121 / KW20 / RD);
SOURCE 4 ORGANISM_TAXID: 71421;
SOURCE 5 STRAIN: ATCC 51907 / DSM 11121 / KW20 / RD;
SOURCE 6 GENE: HI_1552;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS ALPHA/BETA-HYDROLASE FOLD, PIMELOYL-ACP METHYL ESTERASE, BIOTIN
KEYWDS 2 BIOSYNTHESIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SHI,Z.GUO
REVDAT 1 07-DEC-16 5GNG 0
JRNL AUTH J.SHI,X.CAO,Y.CHEN,J.E.CRONAN,Z.GUO
JRNL TITL AN ATYPICAL ALPHA/BETA HYDROLASE FOLD REVEALED IN THE
JRNL TITL 2 CRYSTAL STRUCTURE OF PIMELOYL-ACYL CARRIER PROTEIN METHYL
JRNL TITL 3 ESTERASE BIOG FROM HAEMOPHILUS INFLUENZAE
JRNL REF BIOCHEMISTRY 2016
JRNL REFN ISSN 0006-2960
JRNL DOI 10.1021/ACS.BIOCHEM.6B00818
REMARK 2
REMARK 2 RESOLUTION. 1.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 105604
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.148
REMARK 3 R VALUE (WORKING SET) : 0.145
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.980
REMARK 3 FREE R VALUE TEST SET COUNT : 2088
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 30.4006 - 3.0363 0.97 7920 152 0.0955 0.1431
REMARK 3 2 3.0363 - 2.4103 0.92 7409 136 0.1234 0.1959
REMARK 3 3 2.4103 - 2.1057 0.95 7643 146 0.1445 0.1857
REMARK 3 4 2.1057 - 1.9132 0.95 7622 143 0.1568 0.1742
REMARK 3 5 1.9132 - 1.7761 0.94 7565 156 0.1602 0.1711
REMARK 3 6 1.7761 - 1.6714 0.94 7531 144 0.1679 0.1591
REMARK 3 7 1.6714 - 1.5877 0.93 7408 140 0.1669 0.2023
REMARK 3 8 1.5877 - 1.5186 0.92 7368 138 0.1770 0.2180
REMARK 3 9 1.5186 - 1.4601 0.91 7315 142 0.2149 0.2282
REMARK 3 10 1.4601 - 1.4098 0.91 7259 128 0.2027 0.2274
REMARK 3 11 1.4098 - 1.3657 0.90 7175 138 0.2204 0.1991
REMARK 3 12 1.3657 - 1.3266 0.89 7155 139 0.2343 0.2749
REMARK 3 13 1.3266 - 1.2917 0.89 7115 139 0.2432 0.2805
REMARK 3 14 1.2917 - 1.2602 0.89 7080 145 0.2780 0.3663
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.54
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: 0.4600
REMARK 3 OPERATOR: -H,K,L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 3673
REMARK 3 ANGLE : 0.872 5006
REMARK 3 CHIRALITY : 0.035 524
REMARK 3 PLANARITY : 0.004 641
REMARK 3 DIHEDRAL : 14.272 1306
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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5GNG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1300001108.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105669
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.260
REMARK 200 RESOLUTION RANGE LOW (A) : 30.392
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.26
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.62200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHENIX 1.8.4_1496
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MAGNESIUM ACETATE, 0.1M SODIUM
REMARK 280 CACODYLATE, 25% PEG 8000, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 289K
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 33.91500
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 HIS A 215
REMARK 465 LEU A 216
REMARK 465 GLU A 217
REMARK 465 HIS A 218
REMARK 465 HIS A 219
REMARK 465 HIS A 220
REMARK 465 HIS A 221
REMARK 465 HIS A 222
REMARK 465 HIS A 223
REMARK 465 HIS B 215
REMARK 465 LEU B 216
REMARK 465 GLU B 217
REMARK 465 HIS B 218
REMARK 465 HIS B 219
REMARK 465 HIS B 220
REMARK 465 HIS B 221
REMARK 465 HIS B 222
REMARK 465 HIS B 223
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 GLU A 34 CG CD OE1 OE2
REMARK 470 ARG A 79 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 127 CD CE NZ
REMARK 470 ASP A 214 OD1 OD2
REMARK 470 GLN B 9 CG CD OE1 NE2
REMARK 470 ARG B 79 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 214 OD1 OD2
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 B 338 O HOH B 441 1.86
REMARK 500 NH1 ARG B 57 O HOH B 301 1.88
REMARK 500 O HOH B 402 O HOH B 572 1.94
REMARK 500 O HOH A 461 O HOH A 514 1.95
REMARK 500 O HOH B 303 O HOH B 359 1.96
REMARK 500 O HOH A 369 O HOH A 535 1.97
REMARK 500 O HOH A 556 O HOH A 586 2.00
REMARK 500 O HOH A 590 O HOH A 608 2.00
REMARK 500 O HOH B 524 O HOH B 641 2.01
REMARK 500 O HOH B 537 O HOH B 540 2.02
REMARK 500 O HOH A 495 O HOH A 525 2.02
REMARK 500 O HOH A 576 O HOH A 577 2.04
REMARK 500 O HOH B 324 O HOH B 586 2.04
REMARK 500 O HOH B 525 O HOH B 620 2.04
REMARK 500 O HOH A 430 O HOH A 504 2.04
REMARK 500 O HOH A 628 O HOH A 640 2.05
REMARK 500 O HOH A 613 O HOH A 632 2.05
REMARK 500 O HOH B 524 O HOH B 609 2.06
REMARK 500 O HOH B 565 O HOH B 577 2.06
REMARK 500 O HOH B 585 O HOH B 602 2.06
REMARK 500 OE1 GLU A 143 O HOH A 301 2.07
REMARK 500 O HOH A 510 O HOH A 601 2.07
REMARK 500 O HOH A 370 O HOH B 542 2.08
REMARK 500 O HOH B 422 O HOH B 523 2.09
REMARK 500 OE1 GLU B 143 O HOH B 302 2.09
REMARK 500 O HOH B 509 O HOH B 601 2.09
REMARK 500 O HOH B 308 O HOH B 599 2.10
REMARK 500 O HOH B 494 O HOH B 566 2.10
REMARK 500 O HOH B 424 O HOH B 447 2.10
REMARK 500 OG SER B 65 O HOH B 303 2.10
REMARK 500 O HOH A 318 O HOH A 423 2.11
REMARK 500 O HOH B 511 O HOH B 637 2.11
REMARK 500 O HOH B 390 O HOH B 484 2.11
REMARK 500 O HOH A 580 O HOH A 597 2.12
REMARK 500 O HOH A 527 O HOH A 536 2.12
REMARK 500 O HOH B 473 O HOH B 598 2.13
REMARK 500 O HOH B 483 O HOH B 489 2.13
REMARK 500 O HOH A 446 O HOH A 590 2.13
REMARK 500 O HOH B 571 O HOH B 633 2.13
REMARK 500 O HOH B 491 O HOH B 637 2.13
REMARK 500 O HOH B 646 O HOH B 648 2.13
REMARK 500 O HOH B 465 O HOH B 590 2.13
REMARK 500 O HOH A 524 O HOH B 534 2.14
REMARK 500 O HOH B 427 O HOH B 440 2.14
REMARK 500 O HOH A 348 O HOH A 620 2.14
REMARK 500 NE2 GLN A 194 O HOH A 302 2.16
REMARK 500 O HOH B 537 O HOH B 591 2.17
REMARK 500 NH2 ARG B 139 O HOH B 304 2.18
REMARK 500 O HOH A 507 O HOH A 579 2.18
REMARK 500 O HOH A 569 O HOH A 623 2.19
REMARK 500
REMARK 500 THIS ENTRY HAS 55 CLOSE CONTACTS
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 637 O HOH A 655 2554 2.02
REMARK 500 O HOH A 608 O HOH B 628 1554 2.05
REMARK 500 O HOH A 512 O HOH B 482 1554 2.10
REMARK 500 O HOH A 602 O HOH A 619 2544 2.10
REMARK 500 O HOH B 538 O HOH B 566 2555 2.11
REMARK 500 O HOH A 598 O HOH B 553 1554 2.18
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 ASP A 43 71.26 57.15
REMARK 500 ARG A 57 -80.19 -75.49
REMARK 500 SER A 65 -126.10 61.42
REMARK 500 ILE A 177 -63.56 -101.71
REMARK 500 ARG B 57 -78.88 -80.84
REMARK 500 SER B 65 -129.23 63.05
REMARK 500 ASP B 94 127.08 -171.25
REMARK 500 ILE B 177 -64.62 -100.67
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 657 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH A 658 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH A 659 DISTANCE = 6.73 ANGSTROMS
REMARK 525 HOH A 660 DISTANCE = 6.76 ANGSTROMS
REMARK 525 HOH A 661 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH A 662 DISTANCE = 6.96 ANGSTROMS
REMARK 525 HOH A 663 DISTANCE = 7.47 ANGSTROMS
REMARK 525 HOH B 658 DISTANCE = 5.95 ANGSTROMS
DBREF 5GNG A 1 215 UNP P44251 Y1552_HAEIN 1 215
DBREF 5GNG B 1 215 UNP P44251 Y1552_HAEIN 1 215
SEQADV 5GNG LEU A 216 UNP P44251 EXPRESSION TAG
SEQADV 5GNG GLU A 217 UNP P44251 EXPRESSION TAG
SEQADV 5GNG HIS A 218 UNP P44251 EXPRESSION TAG
SEQADV 5GNG HIS A 219 UNP P44251 EXPRESSION TAG
SEQADV 5GNG HIS A 220 UNP P44251 EXPRESSION TAG
SEQADV 5GNG HIS A 221 UNP P44251 EXPRESSION TAG
SEQADV 5GNG HIS A 222 UNP P44251 EXPRESSION TAG
SEQADV 5GNG HIS A 223 UNP P44251 EXPRESSION TAG
SEQADV 5GNG LEU B 216 UNP P44251 EXPRESSION TAG
SEQADV 5GNG GLU B 217 UNP P44251 EXPRESSION TAG
SEQADV 5GNG HIS B 218 UNP P44251 EXPRESSION TAG
SEQADV 5GNG HIS B 219 UNP P44251 EXPRESSION TAG
SEQADV 5GNG HIS B 220 UNP P44251 EXPRESSION TAG
SEQADV 5GNG HIS B 221 UNP P44251 EXPRESSION TAG
SEQADV 5GNG HIS B 222 UNP P44251 EXPRESSION TAG
SEQADV 5GNG HIS B 223 UNP P44251 EXPRESSION TAG
SEQRES 1 A 223 MET LYS THR LYS PHE TYR ASP TYR GLN GLY GLU HIS LEU
SEQRES 2 A 223 ILE LEU TYR PHE ALA GLY TRP GLY THR PRO PRO ASP ALA
SEQRES 3 A 223 VAL ASN HIS LEU ILE LEU PRO GLU ASN HIS ASP LEU LEU
SEQRES 4 A 223 ILE CYS TYR ASP TYR GLN ASP LEU ASN LEU ASP PHE ASP
SEQRES 5 A 223 LEU SER ALA TYR ARG HIS ILE ARG LEU VAL ALA TRP SER
SEQRES 6 A 223 MET GLY VAL TRP VAL ALA GLU ARG VAL LEU GLN GLY ILE
SEQRES 7 A 223 ARG LEU LYS SER ALA THR ALA VAL ASN GLY THR GLY LEU
SEQRES 8 A 223 PRO CYS ASP ASP SER PHE GLY ILE PRO TYR ALA ILE PHE
SEQRES 9 A 223 LYS GLY THR LEU GLU ASN LEU THR GLU ASN THR ARG LEU
SEQRES 10 A 223 LYS PHE GLU ARG ARG ILE CYS GLY ASP LYS ALA SER PHE
SEQRES 11 A 223 GLU ARG TYR GLN LEU PHE PRO ALA ARG PRO PHE ASP GLU
SEQRES 12 A 223 ILE HIS GLN GLU LEU THR ALA LEU PHE ALA MET ILE GLN
SEQRES 13 A 223 GLN ASP LYS ARG ILE ASP LEU ILE HIS TRP ALA ASN ALA
SEQRES 14 A 223 TRP VAL SER SER ARG ASP LYS ILE PHE THR PRO ALA ASN
SEQRES 15 A 223 GLN HIS GLN TYR TRP ALA LEU ARG CYS ALA VAL GLN GLU
SEQRES 16 A 223 ILE GLU GLY GLU HIS TYR VAL PHE SER ARG PHE THR HIS
SEQRES 17 A 223 TRP SER ALA LEU TRP ASP HIS LEU GLU HIS HIS HIS HIS
SEQRES 18 A 223 HIS HIS
SEQRES 1 B 223 MET LYS THR LYS PHE TYR ASP TYR GLN GLY GLU HIS LEU
SEQRES 2 B 223 ILE LEU TYR PHE ALA GLY TRP GLY THR PRO PRO ASP ALA
SEQRES 3 B 223 VAL ASN HIS LEU ILE LEU PRO GLU ASN HIS ASP LEU LEU
SEQRES 4 B 223 ILE CYS TYR ASP TYR GLN ASP LEU ASN LEU ASP PHE ASP
SEQRES 5 B 223 LEU SER ALA TYR ARG HIS ILE ARG LEU VAL ALA TRP SER
SEQRES 6 B 223 MET GLY VAL TRP VAL ALA GLU ARG VAL LEU GLN GLY ILE
SEQRES 7 B 223 ARG LEU LYS SER ALA THR ALA VAL ASN GLY THR GLY LEU
SEQRES 8 B 223 PRO CYS ASP ASP SER PHE GLY ILE PRO TYR ALA ILE PHE
SEQRES 9 B 223 LYS GLY THR LEU GLU ASN LEU THR GLU ASN THR ARG LEU
SEQRES 10 B 223 LYS PHE GLU ARG ARG ILE CYS GLY ASP LYS ALA SER PHE
SEQRES 11 B 223 GLU ARG TYR GLN LEU PHE PRO ALA ARG PRO PHE ASP GLU
SEQRES 12 B 223 ILE HIS GLN GLU LEU THR ALA LEU PHE ALA MET ILE GLN
SEQRES 13 B 223 GLN ASP LYS ARG ILE ASP LEU ILE HIS TRP ALA ASN ALA
SEQRES 14 B 223 TRP VAL SER SER ARG ASP LYS ILE PHE THR PRO ALA ASN
SEQRES 15 B 223 GLN HIS GLN TYR TRP ALA LEU ARG CYS ALA VAL GLN GLU
SEQRES 16 B 223 ILE GLU GLY GLU HIS TYR VAL PHE SER ARG PHE THR HIS
SEQRES 17 B 223 TRP SER ALA LEU TRP ASP HIS LEU GLU HIS HIS HIS HIS
SEQRES 18 B 223 HIS HIS
FORMUL 3 HOH *721(H2 O)
HELIX 1 AA1 PRO A 23 ASN A 28 5 6
HELIX 2 AA2 MET A 66 LEU A 75 1 10
HELIX 3 AA3 PRO A 100 ASN A 110 1 11
HELIX 4 AA4 THR A 112 GLY A 125 1 14
HELIX 5 AA5 ASP A 126 GLN A 134 1 9
HELIX 6 AA6 PRO A 140 ASP A 158 1 19
HELIX 7 AA7 THR A 179 ALA A 188 1 10
HELIX 8 AA8 VAL A 202 PHE A 206 5 5
HELIX 9 AA9 HIS A 208 TRP A 213 5 6
HELIX 10 AB1 PRO B 23 ASN B 28 5 6
HELIX 11 AB2 MET B 66 LEU B 75 1 10
HELIX 12 AB3 PRO B 100 ASN B 110 1 11
HELIX 13 AB4 THR B 112 GLY B 125 1 14
HELIX 14 AB5 ASP B 126 GLN B 134 1 9
HELIX 15 AB6 PRO B 140 ASP B 158 1 19
HELIX 16 AB7 THR B 179 ALA B 188 1 10
HELIX 17 AB8 VAL B 202 PHE B 206 5 5
HELIX 18 AB9 TRP B 209 ASP B 214 1 6
SHEET 1 AA1 7 LYS A 2 TYR A 6 0
SHEET 2 AA1 7 HIS A 36 TYR A 42 -1 O ILE A 40 N LYS A 4
SHEET 3 AA1 7 HIS A 12 PHE A 17 1 N TYR A 16 O CYS A 41
SHEET 4 AA1 7 ILE A 59 TRP A 64 1 O VAL A 62 N LEU A 15
SHEET 5 AA1 7 SER A 82 VAL A 86 1 O THR A 84 N LEU A 61
SHEET 6 AA1 7 ASN A 168 SER A 172 1 O TRP A 170 N ALA A 85
SHEET 7 AA1 7 ALA A 192 ILE A 196 1 O GLN A 194 N ALA A 169
SHEET 1 AA2 7 LYS B 2 TYR B 6 0
SHEET 2 AA2 7 HIS B 36 TYR B 42 -1 O LEU B 38 N TYR B 6
SHEET 3 AA2 7 HIS B 12 PHE B 17 1 N TYR B 16 O CYS B 41
SHEET 4 AA2 7 ILE B 59 TRP B 64 1 O ARG B 60 N LEU B 15
SHEET 5 AA2 7 SER B 82 VAL B 86 1 O VAL B 86 N ALA B 63
SHEET 6 AA2 7 ASN B 168 SER B 172 1 O TRP B 170 N ALA B 85
SHEET 7 AA2 7 ALA B 192 ILE B 196 1 O GLN B 194 N ALA B 169
CRYST1 45.950 67.830 67.990 90.00 90.01 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 0.021763 0.000000 0.000004 0.00000
SCALE2 0.000000 0.014743 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014708 0.00000
TER 1773 ASP A 214
TER 3553 ASP B 214
MASTER 372 0 0 18 14 0 0 6 4244 2 0 36
END |